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Extracellular galectin-3 has been shown to induce MMP9 secretion. Here, we demonstrate that galectin-3 induces MMP9 at transcript level and it is dependent on the surface levels of poly-N-acetyllactosamine (polyLacNAc). By employing signalling pathway inhibitors, MMP9 expression was shown to be induced via p38 MAP-kinase pathway. Using clones of melanoma cells expressing shRNAs to lysosome-associated membrane protein-1 (LAMP1), a major carrier of polyLacNAc, surface LAMP1 was demonstrated to serve as one of the key mediators of galectin-3-induced MMP9 expression via p38 MAPK pathway.",{"EN":260,"VI":261},"Extracellular galectin-3 induces MMP9 expression by activating p38 MAPK pathway via lysosome-associated membrane protein-1 (LAMP1)","Galectin-3 ngoại bào kích thích biểu hiện MMP9 bằng cách kích hoạt con đường p38 MAPK qua protein-1 màng liên kết lysosome (LAMP1)",{"VOID":263},"Gupta GP, Massague J (2006) Cancer metastasis: building a framework. Cell 127:679–695\nValastyan S, Weinberg RA (2011) Tumor metastasis: molecular insights and evolving paradigms. Cell 147:275–292\nPoste G, Nicolson GL (1980) Arrest and metastasis of blood-borne tumor cells are modified by fusion of plasma membrane vesicles from highly metastatic cells. Proc Natl Acad Sci USA 77:399–403\nMcGary EC, Lev DC, Bar-Eli M (2002) Cellular adhesion pathways and metastatic potential of human melanoma. Cancer Biol Ther 1:459–465\nHiraizumi S, Takasaki S, Ohuchi N, Harada Y, Nose M, Mori S, Kobata A (1992) Altered glycosylation of membrane glycoproteins associated with human mammary carcinoma. Jpn J Cancer Res 83:1063–1072\nDennis JW, Laferte S, Waghorne C, Breitman ML, Kerbel RS (1987) Beta 1-6 branching of Asn-linked oligosaccharides is directly associated with metastasis. Science 236:582–585\nDennis JW, Granovsky M, Warren CE (1999) Glycoprotein glycosylation and cancer progression. Biochim Biophys Acta 1473:21–34\nHanderson T, Pawelek JM (2003) Beta1,6-branched oligosaccharides and coarse vesicles: a common, pervasive phenotype in melanoma and other human cancers. Cancer Res 63:5363–5369\nKrishnan V, Bane SM, Kawle PD, Naresh KN, Kalraiya RD (2005) Altered melanoma cell surface glycosylation mediates organ specific adhesion and metastasis via lectin receptors on the lung vascular endothelium. Clin Exp Metastasis 22:11–24\nDange MC, Srinivasan N, More SK, Bane SM, Upadhya A, Ingle AD, Gude RP, Mukhopadhyaya R, Kalraiya RD (2014) Galectin-3 expressed on different lung compartments promotes organ specific metastasis by facilitating arrest, extravasation and organ colonization via high affinity ligands on melanoma cells. Clin Exp Metastasis 31:661–673\nSrinivasan N, Bane SM, Ahire SD, Ingle AD, Kalraiya RD (2009) Poly N-acetyllactosamine substitutions on N- and not O-oligosaccharides or Thomsen-Friedenreich antigen facilitate lung specific metastasis of melanoma cells via galectin-3. Glycoconj J 26:445–456\nAgarwal AK, Gude RP, Kalraiya RD (2014) Regulation of melanoma metastasis to lungs by cell surface Lysosome Associated Membrane Protein-1 (LAMP1) via galectin-3. Biochem Biophys Res Commun 449:332–337\nReddy BV, Kalraiya RD (2006) Sialilated beta1,6 branched N-oligosaccharides modulate adhesion, chemotaxis and motility of melanoma cells: effect on invasion and spontaneous metastasis properties. Biochim Biophys Acta 1760:1393–1402\nHu X, Beeton C (2010) Detection of functional matrix metalloproteinases by zymography. J Vis Exp 45:2445\nLivak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25:402–408\nGialeli C, Theocharis AD, Karamanos NK (2011) Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting. FEBS J 278:16–27\nOverall CM, Lopez-Otin C (2002) Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat Rev Cancer 2:657–672\nChakraborti S, Mandal M, Das S, Mandal A, Chakraborti T (2003) Regulation of matrix metalloproteinases: an overview. Mol Cell Biochem 253:269–285\nKim SH, Turnbull J, Guimond S (2011) Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor. J Endocrinol 209:139–151\nVincenti MP, Brinckerhoff CE (2007) Signal transduction and cell-type specific regulation of matrix metalloproteinase gene expression: can MMPs be good for you? J Cell Physiol 213:355–364\nElola MT, Wolfenstein-Todel C, Troncoso MF, Vasta GR, Rabinovich GA (2007) Galectins: matricellular glycan-binding proteins linking cell adhesion, migration, and survival. Cell Mol Life Sci 64:1679–1700\nNangia-Makker P, Balan V, Raz A (2008) Regulation of tumor progression by extracellular galectin-3. Cancer Microenviron 1:43–51\nFortuna-Costa A, Gomes AM, Kozlowski EO, Stelling MP, Pavao MS (2014) Extracellular galectin-3 in tumor progression and metastasis. Front Oncol 4:138\nRanjan A, Bane SM, Kalraiya RD (2014) Glycosylation of the laminin receptor (alpha3beta1) regulates its association with tetraspanin CD151: impact on cell spreading, motility, degradation and invasion of basement membrane by tumor cells. Exp Cell Res 322:249–264\nSen T, Dutta A, Maity G, Chatterjee A (2010) Fibronectin induces matrix metalloproteinase-9 (MMP-9) in human laryngeal carcinoma cells by involving multiple signalling pathways. Biochimie 92:1422–1434\nMauris J, Woodward AM, Cao Z, Panjwani N, Argueso P (2014) Molecular basis for MMP9 induction and disruption of epithelial cell-cell contacts by galectin-3. J Cell Sci 127(14):3141–3148\nChen YJ, Wei YY, Chen HT, Fong YC, Hsu CJ, Tsai CH, Hsu HC, Liu SH, Tang CH (2009) Osteopontin increases migration and MMP-9 up-regulation via alphavbeta3 integrin, FAK, ERK, and NF-kappaB-dependent pathway in human chondrosarcoma cells. J Cell Physiol 221:98–108\nZhou D (2003) Why are glycoproteins modified by poly-N-acetyllactosamine glyco-conjugates? Curr Protein Pept Sci 4:1–9\nHirabayashi J, Hashidate T, Arata Y, Nishi N, Nakamura T, Hirashima M, Urashima T, Oka T, Futai M, Muller WE, Yagi F, Kasai K (2002) Oligosaccharide specificity of galectins: a search by frontal affinity chromatography. Biochim Biophys Acta 1572:232–254\nFukuda M (1991) Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking. J Biol Chem 266:21327–21330\nCarlsson SR, Fukuda M (1989) Structure of human lysosomal membrane glycoprotein 1. Assignment of disulfide bonds and visualization of its domain arrangement. J Biol Chem 264:20526–20531\nSaitoh O, Wang WC, Lotan R, Fukuda M (1992) Differential glycosylation and cell surface expression of lysosomal membrane glycoproteins in sublines of a human colon cancer exhibiting distinct metastatic potentials. J Biol Chem 267:5700–5711\nAgarwal AK, Kalraiya RD (2014) Glycosylation regulates the expression of Lysosome Associated Membrane Protein-1 (LAMP1) on the cell surface. J Biosci Tech 5:556–563\nInohara H, Raz A (1994) Identification of human melanoma cellular and secreted ligands for galectin-3. Biochem Biophys Res Commun 201:1366–1375\nSarafian V, Jadot M, Foidart JM, Letesson JJ, Van den Brule F, Castronovo V, Wattiaux R, Coninck SW (1998) Expression of Lamp-1 and Lamp-2 and their interactions with galectin-3 in human tumor cells. Int J Cancer 75:105–111\nFederici C, Brambilla D, Lozupone F, Matarrese P, de Milito A, Lugini L, Iessi E, Cecchetti S, Marino M, Perdicchio M, Logozzi M, Spada M, Malorni W, Fais S (2009) Pleiotropic function of ezrin in human metastatic melanomas. Int J Cancer 124:2804–2812\nBrambilla D, Fais S (2009) The Janus-faced role of ezrin in “linking” cells to either normal or metastatic phenotype. Int J Cancer 125:2239–2245\nWicki A, Lehembre F, Wick N, Hantusch B, Kerjaschki D, Christofori G (2006) Tumor invasion in the absence of epithelial-mesenchymal transition: podoplanin-mediated remodelling of the actin cytoskeleton. Cancer Cell 9:261–272\nBoscher C, Nabi IR (2013) Galectin-3- and phospho-caveolin-1-dependent outside-in integrin signalling mediates the EGF motogenic response in mammary cancer cells. Mol Biol Cell 24:2134–2145\nGarner OB, Baum LG (2008) Galectin-glycan lattices regulate cell-surface glycoprotein organization and signalling. Biochem Soc Trans 36:1472–1477\nGoetz JG, Joshi B, Lajoie P, Strugnell SS, Scudamore T, Kojic LD, Nabi IR (2008) Concerted regulation of focal adhesion dynamics by galectin-3 and tyrosine-phosphorylated caveolin-1. J Cell Biol 180:1261–1275\nLajoie P, Partridge EA, Guay G, Goetz JG, Pawling J, Lagana A, Joshi B, Dennis JW, Nabi IR (2007) Plasma membrane domain organization regulates EGFR signalling in tumor cells. J Cell Biol 179:341–356\nPartridge EA, Le Roy C, Di Guglielmo GM, Pawling J, Cheung P, Granovsky M, Nabi IR, Wrana JL, Dennis JW (2004) Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis. 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The present study explores the mechanism of chronic hypobaric hypoxia mediated skeletal muscle wasting by evaluating changes in protein turnover and various proteolytic pathways. Male Sprague–Dawley rats weighing about 200 g were exposed to hypobaric hypoxia (7,620 m) for different durations of exposure. Physical performance of rats was measured by treadmill running experiments. Protein synthesis, protein degradation rates were determined by 14C-Leucine incorporation and tyrosine release, respectively. Chymotrypsin-like enzyme activity of the ubiquitin–proteasome pathway and calpains were studied fluorimetrically as well as using western blots. Declined physical performance by more than 20%, in terms of time taken in exhaustion on treadmill, following chronic hypobaric hypoxia was observed. Compared to 1.5-fold increase in protein synthesis, the increase in protein degradation was much higher (five-folds), which consequently resulted in skeletal muscle mass loss. Myofibrillar protein level declined from 46.79 ± 1.49 mg\u002Fg tissue at sea level to 37.36 ± 1.153 (P \u003C 0.05) at high altitude. However, the reduction in sarcoplasmic proteins was less as compared to myofibrillar protein. Upregulation of Ub-proteasome pathway (five-fold over control) and calpains (three-fold) has been found to be important factors for the enhanced protein degradation rate. The study provided strong evidences suggesting that elevated protein turnover rate lead to skeletal muscle atrophy under chronic hypobaric hypoxia via ubiquitin–proteasome pathway and calpains.",{"EN":385,"VI":386},"Chronic hypobaric hypoxia mediated skeletal muscle atrophy: role of ubiquitin–proteasome pathway and calpains","Teo cơ xương qua trung gian thiếu oxy áp suất thấp mạn tính: Vai trò của con đường ubiquitin–proteasome và các calpain",{"VOID":388},"Fulco CS, Friedlander AL, Muza SR, Rock PB, Robinson S, Lammi E, Baker R, Fulco CJ, Lewis SF, Cymerman A (2002) Energy intake deficit and physical performance at altitude. Aviat Space Environ Med 73:758–765\nBharadwaj H, Prasad J, Pramanik SN, Kishnani S, Zachariah T, Chaudhary KL, Sridharan K, Srivastava KK (2000) Effect of prolonged exposure to high altitude on skeletal muscles of Indian soldiers. Def Sci J 50:167–176\nMacdonald JH, Oliver SJ, Hillyer K, Sanders S, Smith Z, Williams C, Yates D, Ginnever H, Scanlon E, Roberts E, Murphy D, Lawley J, Chichester E (2009) Body composition at high altitude: a randomized placebo-controlled trial of dietary carbohydrate supplementation. Am J Clin Nutr 90:1193–1202\nSridharan K, Mukherjee AK, Grover SK, Kumaria MML, Arora BS, Rai RM (1987) Assessment of nutritional status and physical work capacity of road construction workers at altitude of 2150–2750 m on two different ration scales. Nutr Rep Int 35:1269–1277\nBrouns F (1992) Nutritional aspects of health and performance at lowland and altitude. Int J Sports Med 13:S100–S106\nSchols AM (2002) Pulmonary cachexia. Int J Cardiol 85:101–110\nHoppeler H, Vogt M (2001) Muscle tissue adaptations to hypoxia. J Exp Biol 204:3133–3139\nHoppeler H, Kleinert E, Schlegel C, Claassen H, Howald H, Kayar SR, Cerretelli P (1990) Muscular exercise at high altitude. II. Morphological adaptation of skeletal muscle to chronic hypoxia. Int J Sports Med 11:S3–S9\nMartinelli M, Winterhalder R, Cerretelli P, Howald H, Hoppeler H (1990) Muscle lipofuscin content and satellite cell volume is increased after high altitude exposure in humans. Experientia 46:672–676\nKung-tung C, Yu-yawn C, Huey-june W, Chen-kang C, Wen-tsung L, Yen-yuan L, Chieh-chung L, Rong-sen Y, Jung-charng L (2008) Decreased anaerobic performance and hormone adaptation after expedition to Peak Lenin. Chin Med J 121:2229–2233\nBigard AX, Douce P, Merino D, Lienhard F, Guezennec CY (1996) Changes in dietary protein intake fail to prevent decrease in muscle growth induced by severe hypoxia in rats. J Appl Physiol 80:208–215\nPreedy VR, Smith DM, Sugden PH (1985) The effects of 6 hr hypoxia on protein synthesis in rat tissue in vivo & in vitro. Biochem J 228:179–185\nPreedy VR, Sugden PH (1989) The effects of fasting or hypoxia on rates of protein synthesis in vivo in subcellular fractions of rat heart and gastrocnemius muscle. Biochem J 257:519–527\nIioka TK, Sugito K, Moriya T, Kuriyama T (2002) Effects of insulin like growth factor on nitrogen balance during hypoxic exposure. Eur Respir J 20:293–299\nVigano A, Ripamonti M, Palma SD, Capitanio D, Vasso M, Wait R, Lundby C, Cerretelli P, Gelfi C (2008) Proteins modulation in human skeletal muscle in the early phase of adaptation to hypobaric hypoxia. Proteomics 8:4668–4679\nImoberdorf R, Garlick PJ, McNurlan MA, Casella GA, Marini JC, Turgay M, Bartsch P, Ballmer PE (2006) Skeletal muscle protein synthesis after active or passive ascent to high altitude. Med Sci Sports Exerc 38:1082–1087\nHolm L, Haslund ML, Robach P, van Hall G, Calbet JA, Saltin B, Lundby C (2010) Skeletal muscle myofibrillar and sarcoplasmic protein synthesis rates are affected differently by altitude-induced hypoxia in native lowlanders. PLoS ONE 20:e15606\nRennie MJ (1985) Muscle protein turnover and the wasting due to injury and disease. Br Med Bull 41:257–264\nCai D, Lee KK, Li M, Tang MK, Chan KM (2004) Ubiquitin expression is upregulated in human and rat skeletal muscles during aging. Arch Biochem Biophys 425:42–50\nReid MB (2005) Response of the ubiquitin–proteasome pathway to changes in muscle activity. Am J Physiol Regul Integr Comp Physiol 288:R1423–R1431\nMammucari C, Milan G, Romanello V, Masiero E, Rudolf R, Piccolo PD, Burden SJ, Lisi RD, Sandri C, Zhao J, Goldberg AL, Schiaffino S, Sandri M (2007) FoxO3 controls autophagy in skeletal muscle in vivo. Cell Metab 6:458–471\nAttaix D, Mosoni L, Dardevet D, Combaret L, Mirand PP, Grizard J (2005) Altered responses in skeletal muscle protein turnover during aging in anabolic and catabolic periods. Int J Biochem Cell Biol 37:2098–2114\nEnns DL, Raastad T, Ugelstad I, Belcastro AN (2007) Calpain\u002Fcalpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle. Eur J Appl Physiol 100:445–455\nDardevet D, Sornet C, Vary T, Grizard J (1996) Phosphotidylinositol 3-kinase and p70 S6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I. Endocrinology 137:4089–4094\nVary TC, Dardevet D, Grizard J, Voisin L, Buffiere C, Denis P, Breuille D, Obled C (1998) Differential regulation of skeletal muscle protein turnover by insulin and IGF-1 after bacteremia. Am J Physiol Endocrinol Metab 275:E584–E593\nVentrucci G, Mello MAR, Marcondes G (2004) Proteasome activity is altered in skeletal muscle tissue of tumour-bearing rats fed a leucine-rich diet. Endocr Relat Cancer 11:887–895\nWaalkes TP, Udenfriend S (1957) A fluorimetric method for the estimation of tyrosine in plasma and tissues. J Lab Clin Med 50:733–736\nHepple RT, Qin M, Nakamoto H, Goto S (2008) Caloric restriction optimizes the proteasome activity. Am J Physiol Regul Integr Comp Physiol 295:R1231–R1237\nMastrocola R, Reffo P, Penna F, Tomasinelli CE, Boccuzzi G, Baccino FM, Aragno M, Costelli P (2008) Muscle wasting in diabetic and in tumor bearing rats: role of oxidative stress. Free Radic Biol Med 44:584–593\nOron U (1990) Proteolytic enzyme activity in rat hind limb muscle in fetus and during post natal development. Int J Dev Biol 34:457–460\nLowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265–275\nKoopman R, Gehrig SM, Leger B, Walrand S, Murphy KT, Lynch GS (2010) Cellular mechanisms underlying temporal changes in skeletal muscle protein synthesis and breakdown during chronic β-adrenoceptor stimulation in mice. J Physiol 588:4811–4823\nKvamme E, Torgner IA, Svenneby G (1985) Glutaminase from mammalian tissue. Methods Enzymol 113:241–244\nElliott WH (1955) Glutamine synthesis. In: Colowick SP, Kaplan NO (eds) Methods enzymol II. pp 337–339\nCathcart R, Schwiers E, Ames BN (1983) Detection of pico mole levels of hyderoperoxides using fluorescent dichlorofluoroscein assay. Anal Biochem 134:111–116\nBuege JA, Aust SD (1978) Microsomal lipid peroxidation. Methods Enzymol 52:302–310\nDutta A, Ray K, Singh VK, Vats P, Singh SN, Singh SB (2008) L-carnitine supplementation attenuates intermittent hypoxia-induced oxidative stress and delays muscle fatigue in rats. Exp Physiol 93:1139–1146\nTisdale MJ (2005) The Ub-proteasome pathway as a therapeutic target for muscle wasting. J Support Oncol 3:209–217\nHowald H, Pette D, Simoneau JA, Uber A, Hoppeler H, Cerretelli P (1990) Effect of chronic hypoxia on muscle enzyme activities. Int J Sports Med S10–S14\nVats P, Mukherjee AK, Kumria MM, Singh SN, Patil SK, Rangnathan S, Sridharan K (1999) Changes in activity levels of glutamine synthetase, glutaminase and glycogen synthetase in rats subjected to hypoxic stress. Int J Biometeorol 42:205–209\nShang F, Gong Taylor A (1997) Activity of ubiquitin-dependent pathway in response to oxidative stress. Ubiquitin-activating enzyme is transiently up-regulated. J Biol Chem 272:23086–23093\nFernandes R, Ramalho J, Pereira P (2006) Oxidative stress upregulates ubiquitin proteasome pathway in retinal endothelial cells. Mol Vis 12:1526–1535\nHermann J, Gulati R, Napoli C, Woodrum LLO, Porcel MR, Sica V, Simari RD, Ciechanover A, Lerman A (2003) Oxidative stress-related increase in ubiquitination in early coronary atherogenesis. FASEB 17:1730–1732\nGomes M, Maria CC, Tisdale MJ (2002) Induction of protein catabolism and the ubiquitin proteasome pathway by mild oxidative stress. Cancer Lett 180:69–74\nSagi SKS, Patir H, Mishra C, Pradhan G, Mastoori SR, Ilavazhagan G (2008) Role of oxidative stress and NFkB in hypoxia induced pulmonary edema. Exp Biol Med 233:1088–1098\nMarfella R, Amico MD, Filippo CD, Baldi A, Siniscalchi M, Sasso FC, Portoghese M, Carbonara O, Crescenzi B, Sangiuolo P, Nicoletti GF, Rossiello R, Ferraraccio F, Cacciapuoti F, Verza M, Coppola L, Rossi F, Paolisso G (2006) Increased activity of the ubiquitin-proteasome system in patients with symptomatic carotid disease is associated with enhanced inflammation and may destabilize the atherosclerotic plaque: effects of rosiglitazone treatment. 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investigated the effect of omeprazole (OPZ) and lansoprazole (LPZ) on the pathophysiology of myocardial necrosis in rats by inspecting a series of indicators like hemodynamic parameters, biochemical estimations and histopathological changes in the myocardial tissue. Rats received either OPZ, LPZ (50 mg\u002Fkg\u002Fday, p.o.) individually for 7 days with concurrent administration of isoproterenol (ISO) (150 mg\u002Fkg, s.c.) on 6th and 7th day of study period to induce myocardial infarction. On the 8th day after measuring hemodynamic parameters, rats were killed and parameters were evaluated. ECG waves were found to be normal in the treatment group. ISO control rats revealed escalation in the oxidative stress as evidenced by depletion in the content of SOD, GSH, catalase and increase in the level of MDA and NO as compared with the normal rats. Treatment with OPZ and LPZ significantly reduced the ROS, indicated by an increase in the endogenous antioxidants and a decrease in NO and MDA levels. ISO control rats showed a significant elevation in the levels of pro-inflammatory cytokine TNF-α as compared to the normal and treatment group of rats. Administration of OPZ and LPZ does not exhibit any significant toxicity. Our findings reveal that multiple doses of OPZ and LPZ may have distinctly minimized the ISO-induced myocardial necrosis by declining the hmodynamic parameters, oxidative stress and pro-inflammatory cytokine TNF-α in myocardial infarcted rats.",{"EN":552,"VI":553},"Protective effect of omeprazole and lansoprazole on β-receptor stimulated myocardial infarction in Wistar rats","Tác dụng bảo vệ của omeprazole và lansoprazole đối với nhồi máu cơ tim kích thích qua thụ thể β ở chuột cống Wistar",{"EN":555},"",{"VOID":557},"Lobo Filho HG, Ferreira NL, Sousa RBd, Carvalho ERd, Lobo PLD, Lobo Filho JG (2011) Experimental model of myocardial infarction induced by isoproterenol in rats. Braz J Cardiovasc Surg 26:469–476\nLiu YT, Zhou C, Jia HM, Chang X, Zou ZM (2016) Standardized Chinese Formula Xin-Ke-Shu inhibits the myocardium Ca2 overloading and metabolic alternations in isoproterenol-induced myocardial infarction rats. Sci Rep 26(6):30208\nKhan V, Sharma S, Bhandari U, Ali SM, Haque SE (2018) Raspberry ketone protects against isoproterenol-induced myocardial infarction in rats. Life Sci 194:205–212\nOikonomou E, Mourouzis K, Fountoulakis P, Papamikroulis GA, Siasos G, Antonopoulos A, Vogiatzi G, Tsalamadris S, Vavuranakis M, Tousoulis D (2018) Interrelationship between diabetes mellitus and heart failure: the role of peroxisome proliferator-activated receptors in left ventricle performance. Heart Fail Rev 23:389–408\nNakahara K, Fujiwara Y, Tsukahara T, Yamagami H, Tanigawa T, Shiba M, Tominaga K, Watanabe T, Urade Y, Arakawa T (2014) Acid reflux directly causes sleep disturbances in rat with chronic esophagitis. PLoS ONE 9:e106969\nBiswas K, Bandyopadhyay U, Chattopadhyay I, Varadaraj A, Ali E, Banerjee RK (2003) A novel antioxidant and antiapoptotic role of omeprazole to block gastric ulcer through scavenging of hydroxyl radical. J Biol Chem 278:10993–11001\nChanchal SK, Mahajan UB, Siddharth S, Reddy N, Goyal SN, Patil PH, Bommanahalli BP, Kundu CN, Patil CR, Ojha S (2016) In vivo and in vitro protective effects of omeprazole against neuropathic pain. Sci Rep 6:30007\nPatlolla JM, Zhang Y, Li Q, Steele VE, Rao CV (2012) Anti-carcinogenic properties of omeprazole against human colon cancer cells and azoxymethane-induced colonic aberrant crypt foci formation in rats. Int J Oncol 40:170–175\nYates TA, Tomlinson LA, Bhaskaran K, Langan S, Thomas S, Smeeth L, Douglas IJ (2017) Lansoprazole use and tuberculosis incidence in the United Kingdom Clinical Practice Research Datalink: a population based cohort. PLoS Med 14:e1002457\nNeiger R, Gaschen F, Jaggy A (2000) Gastric mucosal lesions in dogs with acute intervertebral disc disease: characterization and effects of omeprazole or misoprostol. J Vet Intern Med 14:33–36\nGoyal SN, Sharma C, Mahajan UB, Patil CR, Agrawal YO, Kumari S, Arya DS, Ojha S (2015) Protective effects of cardamom in isoproterenol-induced myocardial infarction in rats. Int J Mol Sci 16:27457–27469\nMahajan UB, Patil PD, Chandrayan G, Patil CR, Agrawal YO, Ojha S, Goyal SN (2018) Eplerenone pretreatment protects the myocardium against ischaemia\u002Freperfusion injury through the phosphatidylinositol 3-kinase\u002FAkt-dependent pathway in diabetic rats. Mole Cell Biochem 446(1–2):91–103\nMert H, Yılmaz H, Irak K, Yıldırım S, Mert N (2018) Investigation of the protective effect of Kefir against isoproterenol induced myocardial infarction in rats. Korean J Food Sci Anim Resour 38(2):259–272\nSonawane VK, Mahajan UB, Shinde SD, Chatterjee S, Chaudhari SS, Bhangale HA, Ojha S, Goyal SN, Kundu CN, Patil CR (2018) A chemosensitizer drug: Disulfiram prevents doxorubicin-induced cardiac dysfunction and oxidative stress in rats. Cardiovasc Toxicol 18(5):459–470\nMahajan UB, Chandrayan G, Patil CR, Arya DS, Suchal K, Agrawal YO, Ojha S, Goyal SN (2017) The protective effect of apigenin on myocardial injury in diabetic rats mediating activation of the PPAR-γ pathway. Int J Mol Sci 18:756\nReddy NM, Mahajan UB, Patil CR, Agrawal YO, Ojha S, Goyal SN (2015) Eplerenone attenuates cardiac dysfunction and oxidative stress in β-receptor stimulated myocardial infarcted rats. Am J Transl Res 15(9):1602–1611 7(\nGoyal SN, Sharma C, Mahajan UB, Patil CR, Agrawal YO, Kumari S, Arya DS, Ojha S (2015) Protective effects of cardamom in isoproterenol-induced myocardial infarction in rats. Int J Mol Sci 16(11):27457–27469\nPadmanabhan M, Rajadurai M, Prince PSM (2008) Preventive effect of S-allylcysteine on membrane-bound enzymes and glycoproteins in normal and Isoproterenol-induced cardiac toxicity in male Wistar rats. Basic Clin Pharmacol Toxicol 103:507–513\nHill R, Howard A, Gresham G (1960) The electrocardiographic appearances of myocardial infarction in the rat. Br J Exp Pathol 41:633–637\nGhoneim MA, Hassan AI, Mahmoud MG, Asker MS (2016) Protective effect of adansonia digitata against isoproterenol-induced myocardial injury in rats. Anim Biotechnol 27:84–95\nPhaniendra A, Jestadi DB, Periyasamy L (2014) Free radicals: properties, sources, targets, and their implication in various diseases. Indian J Clin Biochem 30(1):11–26\nNagoor Meeran MF, Jagadeesh GS, Selvaraj P (2015) Thymol attenuates inflammation in isoproterenol induced myocardial infarcted rats by inhibiting the release of lysosomal enzymes and downregulating the expressions of proinflammatory cytokines. Eur J Pharmacol 5(754):153–161",{"VOID":559},"10.1007\u002Fs11010-019-03494-y","2025-02-24T16:57:26.441+00:00",[134],"https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs11010-019-03494-y",[564,579,592,605,618,633],{"id":565,"sortIndex":19,"researcher":18,"roles":566,"affiliations":567,"properties":576,"displayName":578,"givenName":18,"familyName":18},"4bec65a7-453e-4411-ad0d-c5defa874a78",[273],[568],{"id":569,"sortIndex":19,"affiliation":570,"properties":18},"9c25572c-499b-4dd8-956d-1afb901b5c52",{"id":569,"createTime":18,"updateTime":18,"relativeEntities":571,"slug":18,"properties":572,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":575,"statistic":18},[],{"title":573},{"VI":574},"Department of Pharmacology, R. C. Patel Institute of Pharmaceutical Education and Research, Shirpur, India",[],{"title":577},{"VI":578},"Ashwini S. Patil",{"id":580,"sortIndex":102,"researcher":18,"roles":581,"affiliations":582,"properties":589,"displayName":591,"givenName":18,"familyName":18},"72c7fdd2-3701-47c2-acbd-c95a75c063f3",[273],[583],{"id":569,"sortIndex":19,"affiliation":584,"properties":18},{"id":569,"createTime":18,"updateTime":18,"relativeEntities":585,"slug":18,"properties":586,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":588,"statistic":18},[],{"title":587},{"VI":574},[],{"title":590},{"VI":591},"Alok D. Singh",{"id":593,"sortIndex":301,"researcher":18,"roles":594,"affiliations":595,"properties":602,"displayName":604,"givenName":18,"familyName":18},"11e84745-d8fe-41cd-a287-23129e2bc54c",[273],[596],{"id":569,"sortIndex":19,"affiliation":597,"properties":18},{"id":569,"createTime":18,"updateTime":18,"relativeEntities":598,"slug":18,"properties":599,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":601,"statistic":18},[],{"title":600},{"VI":574},[],{"title":603},{"VI":604},"Umesh B. Mahajan",{"id":606,"sortIndex":438,"researcher":18,"roles":607,"affiliations":608,"properties":615,"displayName":617,"givenName":18,"familyName":18},"0eed9e70-908c-448d-ad20-611227879cd1",[273],[609],{"id":569,"sortIndex":19,"affiliation":610,"properties":18},{"id":569,"createTime":18,"updateTime":18,"relativeEntities":611,"slug":18,"properties":612,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":614,"statistic":18},[],{"title":613},{"VI":574},[],{"title":616},{"VI":617},"Chandragouda R. Patil",{"id":619,"sortIndex":452,"researcher":18,"roles":620,"affiliations":621,"properties":630,"displayName":632,"givenName":18,"familyName":18},"b10ccab5-9f4e-442a-9b3d-adf5511691ef",[273],[622],{"id":623,"sortIndex":19,"affiliation":624,"properties":18},"9405bab2-073d-40f0-bdcd-5979ad1c336c",{"id":623,"createTime":18,"updateTime":18,"relativeEntities":625,"slug":18,"properties":626,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":629,"statistic":18},[],{"title":627},{"VI":628},"Department of Pharmacology and Therapeutics, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, Abu Dhabi, UAE",[],{"title":631},{"VI":632},"Shreesh Ojha",{"id":634,"sortIndex":468,"researcher":18,"roles":635,"affiliations":636,"properties":651,"displayName":653,"givenName":18,"familyName":18},"5eb0d5e5-40c4-4a80-ac03-5b637af999ba",[273],[637,645],{"id":638,"sortIndex":19,"affiliation":639,"properties":18},"f03e4167-593e-427a-9c4b-f7ba0038581b",{"id":638,"createTime":18,"updateTime":18,"relativeEntities":640,"slug":18,"properties":641,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":644,"statistic":18},[],{"title":642},{"VI":643},"Shri Vile Parle Kelavani Mandal’s Institute of Pharmacy, Dhule, India",[],{"id":569,"sortIndex":19,"affiliation":646,"properties":18},{"id":569,"createTime":18,"updateTime":18,"relativeEntities":647,"slug":18,"properties":648,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":650,"statistic":18},[],{"title":649},{"VI":574},[],{"title":652},{"VI":653},"Sameer N. Goyal",{"url":18,"publisher":655,"properties":18},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":656,"slug":10,"properties":657,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":660,"manageAffiliations":677,"indexDatabases":688,"url":18,"thumbnailPath":18,"statistic":703,"gsStatistic":18,"type":105,"analyzePriority":18},[],{"issn":658,"title":659},{"VOID":13},{"EN":15},[661,665,669,673],{"id":22,"createTime":18,"updateTime":18,"relativeEntities":662,"label":663,"description":664,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":25},{},{"id":28,"createTime":18,"updateTime":18,"relativeEntities":666,"label":667,"description":668,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":31},{},{"id":34,"createTime":18,"updateTime":18,"relativeEntities":670,"label":671,"description":672,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":37},{},{"id":40,"createTime":18,"updateTime":18,"relativeEntities":674,"label":675,"description":676,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":43},{},[678,683],{"id":47,"createTime":18,"updateTime":18,"relativeEntities":679,"slug":18,"properties":680,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":682,"statistic":18},[],{"title":681},{"EN":51},[],{"id":54,"createTime":18,"updateTime":18,"relativeEntities":684,"slug":18,"properties":685,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":687,"statistic":18},[],{"title":686},{"EN":58},[60],[689,696],{"id":63,"indexDatabase":690,"url":74,"indexYears":75,"academicFieldIds":695,"indexDatabaseRanking":81},{"id":65,"createTime":18,"updateTime":18,"relativeEntities":691,"label":692,"description":693,"key":71,"publicationTags":694,"standard":18},[],{"EN":68,"VI":68},{"EN":68,"VI":70},[73],[77,78,79,80],{"id":83,"indexDatabase":697,"url":18,"indexYears":18,"academicFieldIds":702,"indexDatabaseRanking":18},{"id":85,"createTime":18,"updateTime":18,"relativeEntities":698,"label":699,"description":700,"key":92,"publicationTags":701,"standard":18},[],{"EN":88,"VI":88},{"EN":90,"VI":91},[94,95],[97],{"impactFactor":19,"impactFactorByYear":704,"i10Index":19,"i10IndexLast5Year":19,"totalPublication":100,"totalPublicationByYear":705,"totalCitation":19,"totalCitationByYear":706,"totalCitationPerPublication":19,"totalCitationPerPublicationByYear":707,"hindexLast5Year":19,"hindex":19},{},{"1999":102,"2000":102,"2001":102,"2002":102,"2004":102,"2012":102,"2019":102},{},{},"2019-01-16",2019,[94,81],{"id":712,"createTime":713,"updateTime":714,"relativeEntities":715,"slug":716,"properties":717,"entityType":128,"verifyStatus":129,"verifyTime":727,"verifyNote":130,"languages":18,"translateLanguages":728,"viewCount":19,"primaryUrl":729,"fullTextUrl":18,"authors":730,"publicationType":171,"publisherRelationship":815,"citationCount":18,"citationInfo":18,"publishDate":874,"publishYear":875,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":876,"openAccess":18,"references":18,"isForceReanalyzing":249},"11ccfa17-c52a-4223-9181-f732c445b4c1","2024-01-05T23:14:46.661+00:00","2026-09-10T03:12:04.839+00:00",[],"Mitogenic-lectins-from-Cephalosporium-curvulum-CSL-and-Aspergillus-oryzae-AOL-mediate-host-pathogen-interactions-leading-to-mycotic-keratitis",{"abstract":718,"title":720,"references":723,"doi":725},{"EN":719},"A core-fucose-specific lectin, CSL from Cephalosporium curvulum, has been reported earlier. Here we assign the role for CSL and another lectin AOL, from pathogenic fungus Aspergillus oryzae, in causing mycotic keratitis. CSL and AOL show strong binding to immortalized and primary human corneal epithelial cells (HCECs) which are inhibited by asialofetuin, confirming their glycan-mediated binding. CSL and AOL showed increase in viability at lower concentrations (0.07 µg\u002Fml) whereas at higher concentrations (0.15 µg\u002Fml and 0.30 µg\u002Fml), have inhibitory effect on immortalized HCECs. Lectin-mediated effect was comparable with the effect induced by the Colony Forming Units (CFUs) of C. curvulum and A. oryzae. CFUs induced more than 1.5-fold increase in HCECs proliferation. Both lectins and fungal CFUs induce secretion of proinflammatory cytokines IL6 and IL8 implicated in ocular diseases. This was supported by upregulation of TLR2 and 4 by lectins as revealed by flow cytometry and RT-PCR. CSL and AOL mediate host–pathogen interactions leading to mycotic keratitis. The mechanism of pathogenesis is possibly initiated through surface binding of mycelia through the lectins to TLR2\u002F4 followed by upregulation of proinflammatory cytokines IL6, IL8 and TLR2 and 4. Understanding the mechanism of pathogenesis is of clinical significance in designing and developing therapeutic strategy to control the infection.",{"EN":721,"VI":722},"Mitogenic lectins from Cephalosporium curvulum (CSL) and Aspergillus oryzae (AOL) mediate host–pathogen interactions leading to mycotic keratitis","Các lectin sinh phân bào từ Cephalosporium curvulum (CSL) và Aspergillus oryzae (AOL) làm trung gian cho các tương tác giữa vật chủ và mầm bệnh dẫn đến viêm giác mạc do nấm",{"VOID":724},"Lambiase A, Micera A, Sacchetti M, Mantelli F, Bonini S (2011) Toll-like receptors in ocular surface diseases: overview and new findings. ClinSci (Lond) 120:441–450\nLevin LA, Avery R, Shore JW, Woog JJ, Baker AS (1996) The spectrum of orbital aspergillosis: a clinicopathological review. SurvOphthalmol 41:142–154\nXie L, Dong X, Shi W (2001) Treatment of fungal keratitis by penetrating keratoplasty. Br J Ophthalmol 85:1070–1074\nKlotz SA, Penn CC, Negvesky GJ, Butrus SI (2000) Fungal and parasitic infections of the eye. ClinMicrobiol Rev 13:662–685\nThomas PA (2003) Fungal infections of the cornea. Eye (Lond) 17:852–862\nBharathi MJ, Ramakrishnan R, Meenakshi R, Padmavathy S, Shivakumar C, Srinivasan M (2007) Microbial keratitis in South India: influence of risk factors, climate, and geographical variation. Ophthalmic Epidemiol 14:61–69\nFeizi T (2000) Carbohydrate-mediated recognition systems in innate immunity. Immunol Rev 173:79–88\nLis H, Sharon N (1998) Lectins: carbohydrate-specific proteins that mediate cellular recognition. Chem Rev 98:637–674\nHouser J, Komarek J, Kostlanova N et al (2013) A soluble fucose-specific lectin from Aspergillus fumigatus conidia—structure, specificity and possible role in fungal pathogenicity. PLoS ONE 8:e83077\nYamaki K, Yoshino S (2011) Aspergillus oryzae lectin induces anaphylactoid oedema and mast cell activation through its interaction with fucose of mast cell-bound non-specific IgE. Scand J Immunol 74:445–453\nInamdar SR, Eligar SM, Ballal S, Belur S, Kalraiya RD, Swamy BM (2015) Exquisite specificity of mitogenic lectin from Cephalosporium curvulum to core fucosylated N-glycans. Glycoconj J 33:19–28\nNagre NN, Chachadi VB, Eligar SM et al (2010) Purification and characterization of a mitogenic lectin from Cephalosporium curvulum, a pathogenic fungus causing mycotic keratitis. Biochem Res Int 854656\nGoldman M (1968) In fluorescent antibody methods. Academic Press,New York; 101–61\nSpiro RG, Bhoyroo VD (1974) Structure of the O-glycosidically linked carbohydrate units of fetuin. J BiolChem 249:5704–5717\nRoy S, Sun Y, Pearlman E (2011) Interferon-gamma-induced MD-2 protein expression and lipopolysaccharide (LPS) responsiveness in corneal epithelial cells is mediated by Janus tyrosine kinase-2 activation and direct binding of STAT1 protein to the MD-2 promoter. J BiolChem 286:23753–23762\nMatsumura K, Higashida K, Ishida H et al.(2007) Carbohydrate binding specificity of a fucose-specific lectin from Aspergillus oryzae: a novel probe for core fucose. J BiolChem282:15700-15708\nPlato A, Hardison SE, Brown GD (2015) Pattern recognition receptors in antifungal immunity. Sem Immunopathol 37:97–106\nRoeder A, Kirschning CJ, Rupec RA, Schaller M, Korting HC (2004) Toll-like receptors and innate antifungal responses. Trends Microbiol 12:44–49\nSutmuller RP, den Brok MH, Kramer M et al (2006) Toll-like receptor 2 controls expansion and function of regulatory T cells. J Clin Invest 116:485–494\nIyer SA, Tuli SS, Wagoner RC (2006) Fungal keratitis: emerging trends and treatment outcomes. Eye Contact Lens 32:267–271\nSun Y, Pearlman E (2009) Inhibition of corneal inflammation by the TLR4 antagonist Eritorantetrasodium (E5564). Invest Ophthalmol Vis Sci 50:1247–1254\nLeal SM Jr, Pearlman E (2012) The role of cytokines and pathogen recognition molecules in fungal keratitis—insights from human disease and animal models. Cytokine 58:107–111\nBandopadhyay S, Saha M (DattaChowdhury) (2015) Chapter 3: mycotic keratitis. In: Razzaghi-Abyaneh M, Shams-Ghahfarokhi M, Rai M (eds) Current perspectives in medical mycology: current trends and future prospects 58\nJin X, Qin Q, Lin Z, Chen W, Qu J (2008) Expression of toll-like receptors in the Fusarium solani infected cornea. Curr Eye Res 33:319–324\nJin X, Qin Q, Tu L, Zhou X, Lin Y, Qu J (2007) Toll-like receptors (TLRs) expression and function in response to inactivate hyphae of Fusarium solani in immortalized human corneal epithelial cells. Mol Vis 13:1953–1961\nErdinest N, Aviel G, Moallem E et al (2014) Expression and activation of toll-like receptor 3 and toll-like receptor 4 on human corneal epithelial and conjunctival fibroblasts. J Inflamm (Lond) 11:3\nSun Y, Chandra J, Mukherjee P, Szczotka-Flynn L, Ghannoum MA, Pearlman E (2010) A murine model of contact lens-associated Fusarium keratitis. Invest Ophthalmol Vis Sci 51:1511–1516",{"VOID":726},"10.1007\u002Fs11010-017-3050-9","2024-12-29T04:01:09.019+00:00",[134],"https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs11010-017-3050-9",[731,746,759,774,789,802],{"id":732,"sortIndex":19,"researcher":18,"roles":733,"affiliations":734,"properties":743,"displayName":745,"givenName":18,"familyName":18},"109386a1-5536-4b23-a026-d2f9d5340cda",[273],[735],{"id":736,"sortIndex":19,"affiliation":737,"properties":18},"112b2925-1884-4281-9616-c0595c4a2e2f",{"id":736,"createTime":18,"updateTime":18,"relativeEntities":738,"slug":18,"properties":739,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":742,"statistic":18},[],{"title":740},{"VI":741},"Department of Studies in Biochemistry, Karnatak University, Dharwad, India",[],{"title":744},{"VI":745},"Suhas Ballal",{"id":747,"sortIndex":102,"researcher":18,"roles":748,"affiliations":749,"properties":756,"displayName":758,"givenName":18,"familyName":18},"d6f7b95a-022a-436f-b53d-8cda5535750a",[273],[750],{"id":736,"sortIndex":19,"affiliation":751,"properties":18},{"id":736,"createTime":18,"updateTime":18,"relativeEntities":752,"slug":18,"properties":753,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":755,"statistic":18},[],{"title":754},{"VI":741},[],{"title":757},{"VI":758},"Shivakumar Belur",{"id":760,"sortIndex":301,"researcher":18,"roles":761,"affiliations":762,"properties":771,"displayName":773,"givenName":18,"familyName":18},"3e4c7183-60bc-4635-a546-a620163aed60",[273],[763],{"id":764,"sortIndex":19,"affiliation":765,"properties":18},"7ff51ee2-d578-4107-8eb6-114f98cfe2dd",{"id":764,"createTime":18,"updateTime":18,"relativeEntities":766,"slug":18,"properties":767,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":770,"statistic":18},[],{"title":768},{"EN":769},"Advanced Centre for Treatment, Research and Education in Cancer, Navi Mumbai, India",[],{"title":772},{"VI":773},"Preeti Laha",{"id":775,"sortIndex":438,"researcher":18,"roles":776,"affiliations":777,"properties":786,"displayName":788,"givenName":18,"familyName":18},"7fe8ef70-cc18-4332-87f9-291de5f562a7",[273],[778],{"id":779,"sortIndex":19,"affiliation":780,"properties":18},"69c908cf-44ec-4e11-a3cd-7619a286fed7",{"id":779,"createTime":18,"updateTime":18,"relativeEntities":781,"slug":18,"properties":782,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":785,"statistic":18},[],{"title":783},{"VI":784},"Prof. Brien Holden Eye Research Centre, LV Prasad Eye Institute, Hyderabad, India",[],{"title":787},{"VI":788},"Sanhita Roy",{"id":790,"sortIndex":452,"researcher":18,"roles":791,"affiliations":792,"properties":799,"displayName":801,"givenName":18,"familyName":18},"68b3af89-9ebd-44fb-87d0-260af3f9fee1",[273],[793],{"id":736,"sortIndex":19,"affiliation":794,"properties":18},{"id":736,"createTime":18,"updateTime":18,"relativeEntities":795,"slug":18,"properties":796,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":798,"statistic":18},[],{"title":797},{"VI":741},[],{"title":800},{"VI":801},"B. M. Swamy",{"id":803,"sortIndex":468,"researcher":18,"roles":804,"affiliations":805,"properties":812,"displayName":814,"givenName":18,"familyName":18},"f6e06735-e2db-4e18-9114-cfe081c74574",[273],[806],{"id":736,"sortIndex":19,"affiliation":807,"properties":18},{"id":736,"createTime":18,"updateTime":18,"relativeEntities":808,"slug":18,"properties":809,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":811,"statistic":18},[],{"title":810},{"VI":741},[],{"title":813},{"VI":814},"Shashikala R. Inamdar",{"url":729,"publisher":816,"properties":869},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":817,"slug":10,"properties":818,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":821,"manageAffiliations":838,"indexDatabases":849,"url":18,"thumbnailPath":18,"statistic":864,"gsStatistic":18,"type":105,"analyzePriority":18},[],{"issn":819,"title":820},{"VOID":13},{"EN":15},[822,826,830,834],{"id":22,"createTime":18,"updateTime":18,"relativeEntities":823,"label":824,"description":825,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":25},{},{"id":28,"createTime":18,"updateTime":18,"relativeEntities":827,"label":828,"description":829,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":31},{},{"id":34,"createTime":18,"updateTime":18,"relativeEntities":831,"label":832,"description":833,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":37},{},{"id":40,"createTime":18,"updateTime":18,"relativeEntities":835,"label":836,"description":837,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":43},{},[839,844],{"id":47,"createTime":18,"updateTime":18,"relativeEntities":840,"slug":18,"properties":841,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":843,"statistic":18},[],{"title":842},{"EN":51},[],{"id":54,"createTime":18,"updateTime":18,"relativeEntities":845,"slug":18,"properties":846,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":848,"statistic":18},[],{"title":847},{"EN":58},[60],[850,857],{"id":63,"indexDatabase":851,"url":74,"indexYears":75,"academicFieldIds":856,"indexDatabaseRanking":81},{"id":65,"createTime":18,"updateTime":18,"relativeEntities":852,"label":853,"description":854,"key":71,"publicationTags":855,"standard":18},[],{"EN":68,"VI":68},{"EN":68,"VI":70},[73],[77,78,79,80],{"id":83,"indexDatabase":858,"url":18,"indexYears":18,"academicFieldIds":863,"indexDatabaseRanking":18},{"id":85,"createTime":18,"updateTime":18,"relativeEntities":859,"label":860,"description":861,"key":92,"publicationTags":862,"standard":18},[],{"EN":88,"VI":88},{"EN":90,"VI":91},[94,95],[97],{"impactFactor":19,"impactFactorByYear":865,"i10Index":19,"i10IndexLast5Year":19,"totalPublication":100,"totalPublicationByYear":866,"totalCitation":19,"totalCitationByYear":867,"totalCitationPerPublication":19,"totalCitationPerPublicationByYear":868,"hindexLast5Year":19,"hindex":19},{},{"1999":102,"2000":102,"2001":102,"2002":102,"2004":102,"2012":102,"2019":102},{},{},{"pages":870,"volume":872},{"VOID":871},"209-219",{"VOID":873},"434","2017-05-03",2017,[94,81],{"id":878,"createTime":879,"updateTime":880,"relativeEntities":881,"slug":882,"properties":883,"entityType":128,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":893,"viewCount":19,"primaryUrl":894,"fullTextUrl":18,"authors":895,"publicationType":171,"publisherRelationship":911,"citationCount":18,"citationInfo":18,"publishDate":970,"publishYear":971,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":972,"openAccess":18,"references":18,"isForceReanalyzing":249},"3003b901-89cf-42de-b938-8ab333a9546d","2023-12-01T02:10:32.175+00:00","2026-09-09T09:13:05.920+00:00",[],"Incorporation-of-3H-N-ethylmaleimide-into-sheep-red-cell-membrane-thiol-groups-following-protection-by-diamide-induced-oxidation",{"abstract":884,"title":886,"references":889,"doi":891},{"EN":885},"The thiol oxidant diazene dicarboxylic acid bis [N,N-dimethylamide] (diamide) is known to reversibly activate K-Cl cotransport in sheep red blood cells [1]. Although the detailed mechanism of activation is unknown, functional thiols at the membrane or at the cytoplasmic level are recognized as important. To search for membrane bound thiols involved in the regulation of K-Cl cotransport, sheep red cells were first exposed to diamide at concentrations activating K-Cl cotransport, and then to the alkylating agent N-ethylmaleimide (NEM) in order to block non-oxidized thiols. White ghosts, prepared by osmotic lysis from these cells, were again treated with NEM followed by reduction of the diamide-induced dithiols with dithio-threitol (DTT) concentrations known to reverse the diamide-induced K-Cl flux [1]. Maximum 3H-NEM incorporation into the DTT-reduced thiols occurred at 50 μM DTT. Saturation labelling by 3H-NEM of about 2 × 104 diamide-protected thiols\u002Fcell occurred at 25 μM NEM. Diamide protected about 0.1% of all membrane thiols chemically determined earlier [2]. Membranes from high K (HK) and low K (LK) sheep red cells did not differ significantly in the number of diamide-protected thiols, and polyacrylamide gels revealed a similar protein distribution of 3H-NEM-labelled thiols. Since diamide is known to stimulate K-Cl flux in LK cells ten times more than in HK cells this finding is consistent with the hypothesis of a cytoplasmic control effecting different K-Cl flux activities in the membranes of the two cation genotypic red blood cells.",{"EN":887,"VI":888},"Incorporation of 3H-N-ethylmaleimide into sheep red cell membrane thiol groups following protection by diamide-induced oxidation","Gắn 3H-N-ethylmaleimide vào các nhóm thiol của màng hồng cầu cừu sau khi được bảo vệ bởi quá trình oxi hóa do diamide gây ra",{"VOID":890},"Lauf PK: Thiol-dependent K-Cl transport in sheep red cells. VIII. Activation through metabolically and chemically reversible oxidation by diamide. J Memb Biol 101: 179–188, 1988\nBauer J, Lauf PK: Thiol-dependent passive K-Cl transport in sheep red cells. III. Differential reactivity of N-ethylmaleimide and iodoacetamide. J Memb Biol 73: 257–261, 1983\nLauf PK, Bauer J, Adragna N, Fujise H, Martin A, Zade-Oppen M, Ryu KH, Delpire E: Erythrocyte K-CL cotransport: properties and regulation. Am J Physiol (Cell Physiol)\nLauf PK, Theg BE: A chloride-dependent K+ flux induced by N-ethylmaleimide in genetically low K+ sheep and goat erythrocytes. Biochem Biophys Res Commun 92: 1422–1428, 1980\nRyu KH, Lauf PK: Evidence for inhibitory SH groups in the thiol-activated K-Cl cotransporter of low K sheep red blood cells. Mol Cell Biochem 99: 135–140, 1990\nTucker EM, Ellory JC, Wooding FB, Morgan G, Herbert J: The number and specificity of L antigen sites on low potassium type sheep red cells. Proc R Soc Lond B 194: 271–277, 1976\nLauf PK, Sun W: The binding characteristics of M and L isoantibodies to high and low potassium sheep red cells. J Memb Biol 28: 351–372, 1976\nLauf PK: Labelling by 3H-N-ethylmaleimide of diamide-oxidized thiol groups in sheep red blood cell (SRBC) membranes. FASEB J. 5: 669A, 1991\nLauf PK, Tosteson DC: The M antigen in HK and LK sheep red cell membranes. J Memb Biol 1: 177–193, 1969\nRasmusen BA, Hall JG: Association between potassium concentration and serological type of sheep red blood cells. Science 151: 1551–1552, 1966\nLauf PK: Thiol-dependent passive K-Cl transport in sheep red cells: IV. Furosemide inhibition as function of external Rb+, Na+ and Cl−. J Memb Biol 77: 57–62, 1984\nDelpire E, Lauf PK: Kinetics of DIDS inhibitions of swelling-activated K-Cl cotransport in low K sheep erythrocytes. J Memb Biol in press, 1992\nLauf PK: Thiol-dependent passive K-Cl transport in sheep red cells: VII. Volume-independent freezing by iodoacetamide, and sulfhydryl group heterogeneity. J Memb Biol 98: 237–246, 1987\nLauf PK: Thiol-dependent passive K-Cl transport in sheep red blood cells: X. A hydroxylamine-oxidation induced K-Cl flux blocked by diethylpyrocarbonate. J Memb Biol 118: 153–159, 1990\nKosower NS, Kosower EM, Wertheim B: Diamide, a new reagent for the intracellular oxidation of glutathione to the disulfide. Biochem Biophys Res Commun 37: 593–596, 1969\nKososwer N, Kosower EM: The glutathione status of cells. Int Rev Cytol 54: 109–160, 1976\nJoiner CH, Lauf PK: The correlation between ouabain binding and potassium pump inhibition in human and sheep erythrocytes. J Physiol 283: 155–177, 1978\nJennings ML, Al-Rohil N: Kinetics of activation and inactivation of swelling-stimulated K+\u002FCl− transport. J Gen Physiol 95: 1021–1040, 1990\nJennings ML, Schulz RK: Okadaic inhibition of K-Cl cotransport. Evidence that protein dephosphorylation is necessary for activation of transport by either cell swelling or N-ethylmaleimide. J Gen Physiol 97: 799–818, 1991\nKaji DM, Tsukitani Y: Role of protein phosphatase in activation of K-Cl cotransport in human erythrocytes. Am J Physiol 260 (Cell Physiol 29): C178-C182, 1991\nDelpire E, Lauf PK: Magnesium and ATP dependence of K-Cl cotransport in low K+ sheep red blood cells. J Physiol (London) 441: 219–231, 1991\nParker JC, McManus TJ, Starke LC, Gitelman HJ: Coordinated regulation of Na\u002FH exchange and [K-Cl] cotransport in dog red cells. J Gen Physiol 96: 1141–1152, 1990\nLauf PK: Foreign anions modulate setpoint of K-Cl cotransport in sheep erythrocytes. Am J Physiol 260 (Cell Physiol 29): 178–193, 1991\nBerkowitz LR: Loop diuretic and anion modification of NEM-induced K transport in human red blood cells. Am J Physiol 258 (Cell Physiol 27): C622-C629, 1990\nParker JC: Na+\u002FH+ exchange and volume regulation in nonepithelial cells. In: Na+\u002FH+ Exchange, edited by S. Grinstein, Boca Raton, Fl. CRC Press, 1989, pp 180–188\nHaest CWM, Kamp D, Deuticke B: Topology of membrane sulfhydryl groups in the human erythrocyte. Biochim Biophys Acta 643: 319–326, 1981\nWiedmer T, Lauf PK: Properties of the M antigen solubilized from genetically high potassium sheep red cells. Memb Biochem 4: 31–47, 1981\nFeit PW, Hoffmann EK, Schiodt M, Kristensen PK, Jessen F, Dunham PB: Purification of proteins of the Na-Cl cotransporter from membranes of Ehrlich ascites cells using a bumetanidesepharose affinity column. J Memb Biol 103: 135–147, 1988\nLauf PK: Thiol-dependent K+CI− transport in sheep red blood cells. V. Dependence on metabolism. Am J Physiol 245 (Cell Physiol 14): C445-C448, 1983",{"VOID":892},"10.1007\u002FBF00240292",[134],"http:\u002F\u002Flink.springer.com\u002F10.1007\u002FBF00240292",[896],{"id":897,"sortIndex":19,"researcher":18,"roles":898,"affiliations":899,"properties":908,"displayName":910,"givenName":18,"familyName":18},"faba6b56-59ec-4975-9074-0ff8d0003536",[273],[900],{"id":901,"sortIndex":19,"affiliation":902,"properties":18},"e2d39cc0-ca96-4e1e-bdc1-735c144ad94b",{"id":901,"createTime":18,"updateTime":18,"relativeEntities":903,"slug":18,"properties":904,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":907,"statistic":18},[],{"title":905},{"VI":906},"Department of Physiology and Biophysics, Wright State University, Dayton, USA",[],{"title":909},{"VI":910},"Peter K. Lauf",{"url":894,"publisher":912,"properties":965},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":913,"slug":10,"properties":914,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":917,"manageAffiliations":934,"indexDatabases":945,"url":18,"thumbnailPath":18,"statistic":960,"gsStatistic":18,"type":105,"analyzePriority":18},[],{"issn":915,"title":916},{"VOID":13},{"EN":15},[918,922,926,930],{"id":22,"createTime":18,"updateTime":18,"relativeEntities":919,"label":920,"description":921,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":25},{},{"id":28,"createTime":18,"updateTime":18,"relativeEntities":923,"label":924,"description":925,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":31},{},{"id":34,"createTime":18,"updateTime":18,"relativeEntities":927,"label":928,"description":929,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":37},{},{"id":40,"createTime":18,"updateTime":18,"relativeEntities":931,"label":932,"description":933,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":43},{},[935,940],{"id":47,"createTime":18,"updateTime":18,"relativeEntities":936,"slug":18,"properties":937,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":939,"statistic":18},[],{"title":938},{"EN":51},[],{"id":54,"createTime":18,"updateTime":18,"relativeEntities":941,"slug":18,"properties":942,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":944,"statistic":18},[],{"title":943},{"EN":58},[60],[946,953],{"id":63,"indexDatabase":947,"url":74,"indexYears":75,"academicFieldIds":952,"indexDatabaseRanking":81},{"id":65,"createTime":18,"updateTime":18,"relativeEntities":948,"label":949,"description":950,"key":71,"publicationTags":951,"standard":18},[],{"EN":68,"VI":68},{"EN":68,"VI":70},[73],[77,78,79,80],{"id":83,"indexDatabase":954,"url":18,"indexYears":18,"academicFieldIds":959,"indexDatabaseRanking":18},{"id":85,"createTime":18,"updateTime":18,"relativeEntities":955,"label":956,"description":957,"key":92,"publicationTags":958,"standard":18},[],{"EN":88,"VI":88},{"EN":90,"VI":91},[94,95],[97],{"impactFactor":19,"impactFactorByYear":961,"i10Index":19,"i10IndexLast5Year":19,"totalPublication":100,"totalPublicationByYear":962,"totalCitation":19,"totalCitationByYear":963,"totalCitationPerPublication":19,"totalCitationPerPublicationByYear":964,"hindexLast5Year":19,"hindex":19},{},{"1999":102,"2000":102,"2001":102,"2002":102,"2004":102,"2012":102,"2019":102},{},{},{"pages":966,"volume":968},{"VOID":967},"13-20",{"VOID":969},"114","1992-09-01",1992,[94,81],{"id":974,"createTime":975,"updateTime":976,"relativeEntities":977,"slug":978,"properties":979,"entityType":128,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":989,"viewCount":19,"primaryUrl":990,"fullTextUrl":18,"authors":991,"publicationType":171,"publisherRelationship":1127,"citationCount":18,"citationInfo":18,"publishDate":1186,"publishYear":1187,"citationAnalyzeStatus":17,"lastCitationAnalyze":18,"indexDatabases":1188,"openAccess":18,"references":18,"isForceReanalyzing":249},"9e3f83c1-6a26-4d4b-bf50-810606519e81","2023-12-12T09:35:19.956+00:00","2026-09-08T10:14:37.157+00:00",[],"Berberine-inhibits-gluconeogenesis-in-spontaneous-diabetic-rats-by-regulating-the-AKT-MAPK-NO-cGMP-PKG-signaling-pathway",{"abstract":980,"title":982,"references":985,"doi":987},{"EN":981},"This work was aimed to investigate the action mechanism of berberine (BBR) on gluconeogenesis. The effects of BBR were examined in rat primary hepatocytes and confirmed in vivo in spontaneous diabetic rats. Protein levels were assessed by Western blot. Immunofluorescence staining was utilized for visualizing protein expression, while qRT-PCR helped for the determination of gene expression at the mRNA level. Besides, cGMP concentration was measured using ELISA, whereas NO level was assessed by spectrophotometry. BBR inhibited gluconeogenesis by downregulating G6Pase and PEPCK via inhibition of CREB phosphorylation. Moreover, BBR enhanced NO and cGMP concentrations, leading to the activation of the NO\u002FcGMP\u002FPKG signaling via activating AKT1\u002FMAPK axis. The in vivo experiments were consistent with the findings obtained in vitro. Hence, BBR represents a drug candidate for diabetic patients and its mechanism of action may be driven via the AKT\u002FMAPK\u002FNO\u002FcGMP\u002FPKG pathway.\n",{"EN":983,"VI":984},"Berberine inhibits gluconeogenesis in spontaneous diabetic rats by regulating the AKT\u002FMAPK\u002FNO\u002FcGMP\u002FPKG signaling pathway","Berberine ức chế tân tạo glucose ở chuột cống đái tháo đường tự phát bằng cách điều hòa con đường tín hiệu AKT\u002FMAPK\u002FNO\u002FcGMP\u002FPKG",{"VOID":986},"Costello KR, Schones DE (2018) Chromatin modifications in metabolic disease: potential mediators of long-term disease risk. Wiley Interdiscip Rev Syst Biol Med 10(4):e1416. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fwsbm.1416\nXu X, Yi H, Wu J, Kuang T, Zhang J, Li Q, Du H, Xu T, Jiang G, Fan G (2021) Therapeutic effect of berberine on metabolic diseases: both pharmacological data and clinical evidence. Biomed Pharmacother 133:110984. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.biopha.2020.110984\nSaeedi P, Petersohn I, Salpea P, Malanda B, Karuranga S, Unwin N, Colagiuri S, Guariguata L, Motala AA, Ogurtsova K, Shaw JE, Bright D, Williams R (2019) Global and regional diabetes prevalence estimates for 2019 and projections for 2030 and 2045: results from the international diabetes federation diabetes atlas, 9(th) edition. Diabetes Res Clin Pract 157:107843. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.diabres.2019.107843\nBeagley J, Guariguata L, Weil C, Motala AA (2014) Global estimates of undiagnosed diabetes in adults. Diabetes Res Clin Pract 103(2):150–160. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.diabres.2013.11.001\nPunthakee Z, Goldenberg R, Katz P (2018) Definition, classification and diagnosis of diabetes, prediabetes and metabolic syndrome. Can J Diabetes 42(Suppl 1):S10-s15. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jcjd.2017.10.003\nZhang M, Chen L (2012) Berberine in type 2 diabetes therapy: a new perspective for an old antidiarrheal drug? Acta Pharm Sinica B 2(4):379–386. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.apsb.2012.06.004\nXu M, Xiao Y, Yin J, Hou W, Yu X, Shen L, Liu F, Wei L, Jia W (2014) Berberine promotes glucose consumption independently of AMP-activated protein kinase activation. PLoS ONE 9(7):e103702. https:\u002F\u002Fdoi.org\u002F10.1371\u002Fjournal.pone.0103702\nPatel P (2021) A bird’s eye view on a therapeutically ‘wonder molecule’: Berberine. Phytomed Plus 1(3):100070. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.phyplu.2021.100070\nYin J, Ye J, Jia W (2012) Effects and mechanisms of berberine in diabetes treatment. Acta Pharm Sinica B 2(4):327–334. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.apsb.2012.06.003\nDi S, Han L, An X, Kong R, Gao Z, Yang Y, Wang X, Zhang P, Ding Q, Wu H, Wang H, Zhao L, Tong X (2021) In silico network pharmacology and in vivo analysis of berberine-related mechanisms against type 2 diabetes mellitus and its complications. J Ethnopharmacol 276:114180. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.jep.2021.114180\nZhang B, Pan Y, Xu L, Tang D, Dorfman RG, Zhou Q, Yin Y, Li Y, Zhou L, Zhao S, Zou X, Wang L, Zhang M (2018) Berberine promotes glucose uptake and inhibits gluconeogenesis by inhibiting deacetylase SIRT3. Endocrine 62(3):576–587. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs12020-018-1689-y\nManning BD, Cantley LC (2007) AKT\u002FPKB signaling: navigating downstream. Cell 129(7):1261–1274. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.cell.2007.06.009\nKousteni S (2012) FoxO1, the transcriptional chief of staff of energy metabolism. Bone 50(2):437–443. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.bone.2011.06.034\nCross DA, Alessi DR, Cohen P, Andjelkovich M, Hemmings BA (1995) Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378(6559):785–789. https:\u002F\u002Fdoi.org\u002F10.1038\u002F378785a0\nHuang X, Liu G, Guo J, Su Z (2018) The PI3K\u002FAKT pathway in obesity and type 2 diabetes. Int J Biol Sci 14(11):1483–1496. https:\u002F\u002Fdoi.org\u002F10.7150\u002Fijbs.27173\nBengal E, Aviram S, Hayek T (2020) p38 MAPK in glucose metabolism of skeletal muscle: beneficial or harmful? Int J Mol Sci 21(18):6480. https:\u002F\u002Fdoi.org\u002F10.3390\u002Fijms21186480\nFang P, Sun Y, Gu X, Shi M, Bo P, Zhang Z, Bu L (2019) Baicalin ameliorates hepatic insulin resistance and gluconeogenic activity through inhibition of p38 MAPK\u002FPGC-1α pathway. Phytomedicine 64:153074. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.phymed.2019.153074\nTian X, Liu F, Li Z, Lin Y, Liu H, Hu P, Chen M, Sun Z, Xu Z, Zhang Y, Han L, Zhang Y, Pan G, Huang C (2019) Enhanced anti-diabetic effect of berberine combined with timosaponin B2 in Goto-Kakizaki rats, associated with increased variety and exposure of effective substances through intestinal absorption. Front Pharmacol 10:19–19. https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffphar.2019.00019\nAlmani SA, Memon IA, Shaikh TZ, Khoharo HK, Ujjan I (2017) Berberine protects against metformin-associated lactic acidosis in induced diabetes mellitus. Iran J Basic Med Sci 20(5):511–515. https:\u002F\u002Fdoi.org\u002F10.22038\u002FIJBMS.2017.8675\nMata-Torres G, Andrade-Cetto A, Espinoza-Hernández FA, Cárdenas-Vázquez R (2020) Hepatic glucose output inhibition by Mexican plants used in the treatment of type 2 diabetes. Front Pharmacol 11:215. https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffphar.2020.00215\nXie W, Ye Y, Feng Y, Xu T, Huang S, Shen J, Leng Y (2018) Linderane suppresses hepatic gluconeogenesis by inhibiting the cAMP\u002FPKA\u002FCREB pathway through indirect activation of PDE 3 via ERK\u002FSTAT3. Front Pharmacol 9:476. https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffphar.2018.00476\nWang Y, Zhou X, Zhao D, Wang X, Gurley EC, Liu R, Li X, Hylemon PB, Chen W, Zhou H (2020) Berberine inhibits free fatty acid and LPS-induced inflammation via modulating ER stress response in macrophages and hepatocytes. PLoS ONE 15(5):e0232630–e0232630. https:\u002F\u002Fdoi.org\u002F10.1371\u002Fjournal.pone.0232630\nLi M, Dang Y, Li Q, Zhou W, Zuo J, Yao Z, Zhang L, Ji G (2019) Berberine alleviates hyperglycemia by targeting hepatic glucokinase in diabetic db\u002Fdb mice. Sci Rep 9(1):8003. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41598-019-44576-7\nKalyanaraman H, Schwaerzer G, Ramdani G, Castillo F, Scott BT, Dillmann W, Sah RL, Casteel DE, Pilz RB (2018) Protein kinase G activation reverses oxidative stress and restores osteoblast function and bone formation in male mice with type 1 diabetes. Diabetes 67(4):607–623. https:\u002F\u002Fdoi.org\u002F10.2337\u002Fdb17-0965\nHu X, Feng Y, Liu X, Zhao XF, Yu JH, Yang YS, Sydow-Bäckman M, Hörling J, Zierath JR, Leng Y (2007) Effect of a novel non-thiazolidinedione peroxisome proliferator-activated receptor alpha\u002Fgamma agonist on glucose uptake. Diabetologia 50(5):1048–1057. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs00125-007-0622-3\nChen QM, Xie MZ (1986) Studies on the hypoglycemic effect of Coptis chinensis and berberine. Yao Xue Xue Bao 21(6):401–406\nQuinn PG, Yeagley D (2005) Insulin regulation of PEPCK gene expression: a model for rapid and reversible modulation. Curr Drug Targets Immune Endocr Metabol Disord 5(4):423–437. https:\u002F\u002Fdoi.org\u002F10.2174\u002F156800805774912962\nMues C, Zhou J, Manolopoulos KN, Korsten P, Schmoll D, Klotz LO, Bornstein SR, Klein HH, Barthel A (2009) Regulation of glucose-6-phosphatase gene expression by insulin and metformin. Horm Metab Res 41(10):730–735. https:\u002F\u002Fdoi.org\u002F10.1055\u002Fs-0029-1225360\nHill MJ, Suzuki S, Segars JH, Kino T (2016) CRTC2 is a coactivator of GR and couples GR and CREB in the regulation of hepatic gluconeogenesis. Mol Endocrinol 30(1):104–117. https:\u002F\u002Fdoi.org\u002F10.1210\u002Fme.2015-1237\nHerzig S, Long F, Jhala US, Hedrick S, Quinn R, Bauer A, Rudolph D, Schutz G, Yoon C, Puigserver P, Spiegelman B, Montminy M (2001) CREB regulates hepatic gluconeogenesis through the coactivator PGC-1. Nature 413(6852):179–183. https:\u002F\u002Fdoi.org\u002F10.1038\u002F35093131\nHe L, Sabet A, Djedjos S, Miller R, Sun X, Hussain MA, Radovick S, Wondisford FE (2009) Metformin and insulin suppress hepatic gluconeogenesis through phosphorylation of CREB binding protein. Cell 137(4):635–646. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.cell.2009.03.016\nBassot A, Chauvin MA, Bendridi N, Ji-Cao J, Vial G, Monnier L, Bartosch B, Alves A, Cottet-Rousselle C, Gouriou Y, Rieusset J, Morio B (2019) Regulation of mitochondria-associated membranes (MAMs) by NO\u002FsGC\u002FPKG participates in the control of hepatic insulin response. Cells 8(11):1319. https:\u002F\u002Fdoi.org\u002F10.3390\u002Fcells8111319\nZhang N, Liu X, Zhuang L, Liu X, Zhao H, Shan Y, Liu Z, Li F, Wang Y, Fang J (2020) Berberine decreases insulin resistance in a PCOS rats by improving GLUT4: dual regulation of the PI3K\u002FAKT and MAPK pathways. Regul Toxicol Pharmacol 110:104544. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.yrtph.2019.104544",{"VOID":988},"10.1007\u002Fs11010-022-04604-z",[134],"https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs11010-022-04604-z",[992,1016,1031,1046,1059,1072,1085,1099,1112],{"id":993,"sortIndex":19,"researcher":18,"roles":994,"affiliations":995,"properties":1013,"displayName":1015,"givenName":18,"familyName":18},"6478c2f6-00cb-4028-969f-cfd478e7894a",[273],[996,1004],{"id":997,"sortIndex":19,"affiliation":998,"properties":18},"36fa3658-0bcb-4677-862c-c32b2a255ee0",{"id":997,"createTime":18,"updateTime":18,"relativeEntities":999,"slug":18,"properties":1000,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":1003,"statistic":18},[],{"title":1001},{"VI":1002},"Department of Endocrinology Metabolism, Putuo Hospital, Shanghai University of Traditional Chinese Medicine, Shanghai, 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smoke is a complex mixture of more than 4700 chemical compounds including free radicals and oxidants. Toxicity exhibited by cigarette smoke may be due to combined action of these compounds inducing many cellular processes mediated through reactive oxygen species (ROS). Major player probably nicotine as it is present in tobacco, in higher concentrations. The compounds that induce intracellular oxidative stress recognized as the important agents involved in the damage of biological molecules. Experiments using animal and cell culture model systems suggested that moderately higher concentrations of some forms of ROS like NO and H2O2 can act as signal transducing agents. Nuclear transcription factor κB (NF-κB) an inducible transcription factor detected in neurons found to be involved in many biological processes such as inflammation, innate immunity, development, apoptosis, and antiapoptosis. Our present study demonstrates that nicotine induces ROS levels in a dose dependent manner in rat mesencephalic cells. Electro mobility shift analysis showed that nicotine activates inducible NF-κB by binding to consensus sequence of DNA. Nicotine added to cell culture stimulates the degradation of IκB-α subunit in 2 h. Further activation of c-Jun terminal kinase indicates that nicotine induces oxidative stress leading to activation of stress dependent NF-κB pathway in mesencephalic cells.",{"EN":1199,"VI":1200},"Nicotine induces oxidative stress and activates nuclear transcription factor kappa B in rat mesencephalic cells","Nicotine gây stress oxy hóa và hoạt hóa yếu tố phiên mã hạt nhân kappa B trong các tế bào trung não chuột cống",{"VOID":1202},"Pailer M (1964) Chemistry of nicotine and related alkaloids (including biosynthetic aspects). In: Von Euler US (eds) Tobacco Alkaloids and Related Compounds. The McMillan Co: New york pp. 15–36\nHammond D, Collishaw NE, Callard C (2006) Secret science: tobacco industry research on smoking behaviour and cigarette toxicity. 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FASEB J 7: 1045–1051\nMinna JD (2003) Nicotine exposure and bronchial epithelial cell nicotinic acetylcholine receptor expression in the pathogenesis of lung cancer. J Clin Investig 111: 31–33\nCattaneo MG, D’Atri F, Vicentini IM (1997) Mechanisms of mitogen-activated protein kinase activation by nicotine in small-cell lung carcinoma cells. Biochem J 328: 499–503\nDasgupta P, Rastogi S, Pillai S, Ordonez-Ercan D, Morris M, Haura E, Chellappan S (2006) Nicotine induces cell proliferation by {beta}-arrestin-mediated activation of Src and Rb-Raf-1 pathways. J Clin Invest 3: 7–20\nWang HY, Lee DH, Davis CB, Shank RP (2000) Amyloid peptide Abeta(1–42) binds selectively and with picomolar affinity to alpha7 nicotinic acetylcholinereceptors. J Neurochem 75: 1155–1161\nBaeuerle PA, Kenkel T (1994) Function and activation of NF-kappa B in the immune system. Ann Rev immunol: 12: 141–179\nHuie RE, Padmaja S (1993) The reaction of NO with superoxide. Free Radical Res Commun 18:195–199\nPahl HL (1999) Activators and target genes of Rel\u002FNF-κB transcription factors. Oncogene 18: 6853–6866\nLin A, Karin M (2004) NF-κB in cancer a marked target. Semin Cancer Biol 13: 107–114\nChen LF, Greene WC (2004) Shaping the nuclear action of NF-κB. Nature Rev Mol Cell Biol 5: 392–491\nKaltschmidt C, Kaltschmidt B, Neumann H, Wekerle H, Baeuerle PA (1994) Constitutive NF-κB activity in neurons. Mol Cell Biol 14: 3981–3992\nWidera D, Mikenberg I, Kaltschmidt B, Kaltschmidt C (2006) Potential role of NF-κB in adult neural stem cells; the understand steersman. Int J Devl Neurosci 24: 91–102\nSchneider A, Martin-Villalba A, Weih F, Vogel J, Wirth T, Schwaninger M (1999) NF-kappaB is activated and promotes cell death in focal cerebral ischemia. Nat Med 5: 554–559\nDoolittle DJ, Winegar R, Lee CK, Caldwell WS, Hayes AW, de Bethizy JD (1995) The genotoxic potential of nicotine and its major metabolites. Mutat Res 344: 95–102\nMizusaki S, Okamoto H, Akiyama A, Fukuhara Y (1977) Relation between chemical constituents of tobacco and mutagenic activity of cigarette smoke condensate. Mut Res 48: 319–325\nManna SK, Rangaswamy T, Wise K, Sarkar S, Shishodia S, Biswal S, Ramesh GT (2006) Long term environmental tobacco smoke activates nuclear transcription factor-kappa B, activator protein-1 and stress responsive kinases in mouse brain. Biochem Pharmacol 71:1602–1609\nHusain K, Scotttt BR, Reddy SK, Somani SM (2001) Chronic ethanol and nicotine interaction on rat tissue antioxidant defense system. Alcohol 2: 89–97\nAgarwal BB (2004) Nuclear factor kappa the enemy with in. Cancer cell 6:203–208\nCampain JA (2004) Nicotine potentially a multifunctional carcinogen. Toxicol Sci 79: 1–3\nKarin M (1995) The regulation of AP-1 activity by mitogen-activated protein kinases. J. Biol Chem 270: 16483–16486\nGensch E, Gallup M, Sucher A, Li D, Gebremichael A, Lemjabbar H, Mengistab A, Dasari V, Hotchkiss J, Harkema J, Basbaum C (2004) Tobacco smoke control of mucin production in lung cells requires oxygen radicals AP-1 and JNK. J Biol Chem 279: 39085–39093\nMarwick JA, Kirkham PA, Stevenson CS, Danahay H, Giddings J, Butler K, Donaldson K, Macnee W, Rahman I (2004) Cigarette smoke alters chromatin remodeling and induces proinflammatory genes in rat lungs. Am J Respir Cell Mol Biol 31: 633–642\nManna SK, Ramesh GT (2005) Interleukin-8 induces nuclear transcription factor-κB through TRAF6- dependent pathway. 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It is involved in the biotransformation of xenobiotics and endogenous substrates. Inter-individual genetic polymorphisms of the CYP2E1 gene are associated with different cancer diseases as well as alcohol and nicotine dependence. We report here for the first time three novel alternative spliced mRNA transcripts which are more frequently present in lung carcinoma cell lines as in hepatocyte cell lines. They are unexpected detectable in blood leukocytes from healthy volunteers but not in normal and cancerous lung tissue. The full-length wildtype transcript of CYP2E1 is described to be concomitant to an alternatively spliced mRNA transcript. Stimulation with CYP2E1-inducing agents did not change the splicing transcript pattern. The three splicing variants should lead to truncated non-functional proteins. Thus the genetic diversity of CYP2E1 is additionally extended at the transcriptional level of gene expression. The physiological role of the splicing variants is not known, yet, but they seem to be related to the carcinogenic property of the cell lines. (Mol Cell Biochem xxx: 201–207, 2005)",{"EN":1374,"VI":1375},"Molecular cloning and expression of novel alternatively spliced cytochrome P450 2E1 mRNAs in humans","Nhân bản phân tử và biểu hiện của các mRNA ghép nối thay thế mới của cytochrome P450 2E1 ở người",{"VOID":1377},"Lieber CS: Cytochrome P-4502E1: its physiological and pathological role. Physiol Rev 77: 517–544, 1997\nCoon MJ, Koop DR: Alcohol-inducible cytochrome P-450 (P-450ALC). Arch Toxicol 60: 16–21, 1987\nYang CS, Yoo JSH, Ishizaki H, Hong J: Cytochrome P450IIE1: role in nitrosamine metabolism and mechanisms of regulation. Drug Metab Rev 22: 147–159, 1990\nCarriere V, Berthou F, Baird S, Belloc C, Beaune P, de Waziers I: Human cytochrome P450 2E1 (CYP2E1): from genotype to phenotype. Pharmacogenetics 6: 203–211, 1996\nCederbaum Al, Wu D, Mari M, Bai J: CYP2E1-dependent toxicity and oxidative stress in HepG2 cells. Free Radic Biol Med 31: 1539–1543, 2001\nTan W, Song N, Wang GQ, Liu Q, Tang HJ, Kadlubar FF, Lin DX: Impact of genetic polymorphisms in cytochrome P450 2E1 and glutathione S-transferase M1, T1, and P1 on susceptibility to esophageal cancer among high-risk individuals in China. Cancer Epidemiol Biomarker Prev 9: 551–556, 2000\nDupont I, Lucas D, Clot P, Menez C, Albano E: Cytochrome P4502E1 inducibility and hydroxyethyl radical formation among alcoholics. J Hepatol 28: 564–571, 1998\nO'Shea D, Davis SN, Kim RB, Wilkinson GR: Effect of fasting and obesity in humans on the 6-hydroxylation of chlorzoxazone: a putative probe of CYP2E1 activity. Clin Pharmacol Ther 56: 359–367, 1994\nHan XM, Zhou HH: Polymorphism of CYP450 and cancer susceptibility. Acta Pharmacol Sin 21: 673–679, 2000\nSnawder JE, Lipscomb JC: Interindividual variance of cytochrome P450 forms in human hepatic microsomes: correlation of individual forms with xenobiotic metabolism and implications in risk assessment. Regul Toxicol Pharmacol 32: 200–209, 2000\nStephens EA, Taylor JA, Kaplan N, Yang CH, Hsieh LL, Lucier GW, Bell DA: Ethnic variation in the CYP2E1 gene polymorphism analysis of 695 African-Americans, European-Americans and Taiwanese. Pharmacogenetics 4: 185–192, 1994\nPersson I, Johansson I, Bergling H, Dahl ML, Seidegard J, Rylander R, Rannug A, Hogberg J, Sundberg MI: Genetic polymorphism of cytochrome P4502E1 in a Swedish population: Relationship to incidence of lung cancer. FEBS Lett 319: 207–211, 1993\nHildesheim A, Anderson LM, Chen CJ, Cheng YJ, Brinton LA, Daly AK, Reed CD, Chen IH, Caporaso NE, Hsu MM, Chen JY, Idle JR, Hoover RN, Yang CS, Chabra SK: CYP2E1 genetic polymorphisms and risk of nasopharyngeal carcinoma in Taiwan. J Natl Cancer Inst 89: 1207–1212, 1997\nItoga S, Nomura F, Makino Y, Tomonaga T, Shimada H, Ochiai T, Iizasa T, Baba M, Fujisawa T, Harada S: Tandem repeat polymorphism of the CYP2E1 gene: an association study with esophageal cancer and lung cancer. Alcohol Clin Exp Res 26: 15S–19S, 2002\nLeMarchand L, Donlon T, Seifried A, Wilkens LR: Red meat intake, CYP2E1 genetic polymorphisms, and colorectal cancer risk. Cancer Epidemiol Biomarker Prev 11: 1019–1024, 2002\nUmeno M, McBride OW, Yang CS, Gelboin HV, Gonzales FJ: Human ethanol-inducible P450IIE1: complete gene sequence, promoter characterization, chromosome mapping, and cDNA-directed expression. Biochemistry 27: 9006–9013, 1988\nGonzales FJ, Ueno T, Umeno M, Song BJ, Veech RL, Gelboin HV: Microsomal ethanol oxidazing system: transcriptional and post-transcriptional regulation of cytochrome P450 CYP2E1. Alcohol Alcohol Suppl 1: 97–101, 1991\nAbdel-Razzak Z, Garlatti M, Aggerbeck M, Barouki R: Determination of interleukin-4-responsive region in the human cytochrome P450 2E1 gene promoter. Biochem Pharmacol 68: 1371–1381, 2004\nLagadic-Gossmann D, Lerche C, Rissel M, Joannard F, Galisteo M, Guillouzo A, Corcos L: The induction of the human hepatic CYP2E1 gene by interleukin 4 is transcriptional and regulated by protein kinase C. Cell Biol Toxicol 16: 221–233, 2000\nGonzalez FJ, Ueno T, Umeno M, Song BJ, Veech RL, Gelboin HV: Microsomal ethanol oxidizing system: transcriptional and posttranscriptional regulation of cytochrome P450 CYP2E1. Alcohol Alcohol Suppl 1: 97–101, 1991\nSong BJ, Matsunaga T, Hardwick JP, Park SS, Veech RL, Yang CS, Gelboin HV Gonzalez FJ: Stabilization of cytochrome P450j messenger ribonucleic acid in the diabetic rat. Mol Endocrinol 1: 542–547, 1987\nPeng HM, Coon MJ: Regulation of rabbit cytochrome P450 2E1 expression in HepG2 cells by insulin and thyroid hormone. Mol Pharmacol 54: 740–747, 1998\nAbdel Razzak Z, Loyer P, Fautrel A, Gautier JC, Corcos L, Turlin B, Beaune P, Guillouzo A: Cytokines down-regulate expression of major cytochrome P-450 enzymes in adult human hepatocytes in primary culture. Mol Pharmacol 44: 707–715, 1993\nChoi JY, Lee KM, Cho SH, Kim SW, Choi HY, Lee SY, Im HJ, Yoon KJ, Choi H, Choi I, Hirvonen A, Hayes RB, Kang D: CYP2E1 and NQO1 genotypes, smoking and bladder cancer. Pharmacogenetics 13: 349–355, 2003\nPiao YF, Li JT, Shi Y: Relationship between genetic polymorphism of cytochrome P450IIE1 and fatty liver. World J Gastroenterol 9: 2612–2615, 2003\nHoward LA, Ahluwalia JS, Lin SK, Sellers EM, Tyndale RF: CYP2E1∗1D regulatory polymorphism: Association with alcohol and nicotine dependence. Pharmacogenetics 13: 321–328, 2003\nKongruttanachok N, Sukdikul S, Setavarin S, Kerekhjanarong V, Supiyaphun P, Voravud N, Poovorawan Y, Mutirangura A: Cytochrome P450 2E1 polymorphism and nasopharyngeal carcinoma development in Thailand: a correlative study. BMC Cancer 1: 4, 2001\nHanioka N, Kimura S, Meyer UA, Gonzalez FJ: The human CYP2D locus associated with a common genetic defect in drug oxidation: a G1934 – A base change in intron 3 of a mutant CYP2D6 allele results in an aberrant 3′ splice recognition site. Am J Hum Genet 47: 994–1001, 1990\nMurata M, Watanabe M, Yamanaka M, Kubota Y, Ito H, Nagao M, Katoh T, Kamataki T, Kawamura J, Yatani R, Shiraishi T: Genetic polymorphisms in cytochrome P450 (CYP) 1A1, CYP1A2, CYP2E1, glutathione S-transferase (GST) M1 and GSTT1 and susceptibility to prostate cancer in the Japanese population. Cancer Lett 165(2): 171–177, 2001",{"VOID":1379},"10.1007\u002Fs11010-005-0169-x","2025-01-05T17:47:11.273+00:00",[134],"https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs11010-005-0169-x",[1384,1399,1412,1427],{"id":1385,"sortIndex":19,"researcher":18,"roles":1386,"affiliations":1387,"properties":1396,"displayName":1398,"givenName":18,"familyName":18},"0013b23c-262a-4f1d-9dbb-76ae51cd120a",[273],[1388],{"id":1389,"sortIndex":19,"affiliation":1390,"properties":18},"6e0b9279-9925-4841-963c-dcf73387c0cc",{"id":1389,"createTime":18,"updateTime":18,"relativeEntities":1391,"slug":18,"properties":1392,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":1395,"statistic":18},[],{"title":1393},{"VI":1394},"Department of Human Exposure Research and Epidemiology, UFZ – Centre for Environmental Research Leipzig-Halle, Leipzig, Germany",[],{"title":1397},{"VI":1398},"Mario 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demonstrate that TR2 orphan receptor (TR2) may induce transactivation activities via an AGGTCA-like-direct-repeat-4 consensus thyroid hormone response element (DR4-TRE) system. TR2 showed a slightly greater binding affinity than thyroid hormone receptor α1 (TRα1)\u002Fretinoid X receptor α (RXRα) heterodimer with Kds 0.5 nM and 2.3 nM, respectively. These receptors, TR2 and TRα1\u002FRXRα heterodimer, competed with each other on binding to limited amounts of DR4-TRE. TR2 canceled the suppression effect of unliganded-TRα1 on CAT reporter activity in a dose-dependent fashion. Estrogen receptor (ER) and 2P2 (a mutated TR2 with P box sequence of androgen receptor) failed not only to bind to DR4-TRE but also to recover this inhibitory effect of unliganded TRα1. However, when T3 was supplemented, estradiol-ER competed for a full CAT activity while TR2 showed an additive effect on the transcriptional activation. These results indicate that DNA binding is essential for TR2 to take action and fully functional liganded TRa1 may rely on common factors shared with ER but not TR2.",{"EN":1512,"VI":1513},"Thyroid hormone direct repeat 4 response element is a positive regulatory element for the human TR2 orphan receptor, a member of steroid receptor superfamily","Yếu tố đáp ứng hormone tuyến giáp lặp lại trực tiếp 4 là một yếu tố điều hòa dương tính cho thụ thể mồ côi TR2 ở người, một thành viên của siêu họ thụ thể steroid",{"VOID":1515},"Carson‐Jurica MA, Schrader WT, O'Malley BW: Steroid receptor family: Structure and functions. Endocrine Rev 11: 201–220, 1990\nEvans RM: The steroid and thyroid hormone receptor superfamily. Science 240: 889–895, 1988\nGlass CK, Holloway JM, Devary OV, Rosenfeld MG: The thyroid hormone receptor binds with opposite transcriptional effects to a common sequence motif in thyroid hormone and estrogen response elements. Cell 54: 313–323, 1988\nBrent GA, Harney JW, Chen Y, Warne RL, Moore DD, Larsen PR: Mutation of the rat growth hormone promoter which increase and decrease response to thyroid hormone define a consensus thyroid hormone response element. Mol Endocrinol 3: 1996–2004, 1989\nde Verneuil H, Metzger D: The lack of transcriptional activation of the v‐erbA oncogene is in part due to a mutation present in the DNA binding domain of the protein. Nucleic Acids Res 18: 4489–4497, 1990\nChang C, Kokontis J, Acakpo‐Satchivi L, Liao S, Takeda H, Chang Y: Molecular cloning of new TR2 receptors: A class of steroid receptor with multiple ligand‐binding domains. Biochem Biophys Res Commun 165: 735–741, 1989\nChang C, Kokontis J: Identification of a new member of the steroid receptor super‐family by cloning and sequence analysis. Biochem Biophys Res Commun 155: 971‐977, 1988\nLin T‐M, Young W‐J, Chang C: Multiple functions of the TR2‐11 orphan receptor in modulating activation of two key cis‐acting elements involved in the retinoic acid signal transduction system. J Biol Chem 270: 30121–30128, 1995\nLee H‐J, Chang C: Identification of human TR2 orphan receptor response element in the transcriptional initiation site of the simian virus 40 major late promoter. J Biol Chem 270: 5434–5440, 1995\nPetty KJ, Desverge B, Mitsuhashi T, Nikodem VM: Identification of a thyroid hormone response element in the malic enzyme gene. J Biol Chem 265: 7395–7400, 1990\nCooney AJ, Tsai SY, O'Malley BW, Tsai MJ: Chicken ovalbumin upstream promoter transcription factor (COUP‐TF) dimers bind to different GGTCA response elements, allowing COUP‐TF to repress hormonal inductin of the vitamin D3, thyroid hormone, and retinoic acid receptors. Mol Cell Biol 12: 4153–4163, 1992\nChen C, Okayama H: High‐efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 7: 2745–2752, 1987\nDamm K, Thompson CC, Evans RM: Protein encoded by v‐erbA functions as a thyroid‐hormone receptor antagonist. Nature 339: 593–597, 1989\nSap J, Munoz A, Schmitt J, Stunnenberg H, Vennstrom B: Repressin of transcription mediated at a thyroid hormone response element by the v‐erb‐A oncogene product. Nature 340: 242–244, 1989\nBaniahmad A, Steiner C, Kohne A.C, Renkawitz R: Modular structure of a chicken lysozyme silencer: involvement of an unusual thyroid hormone receptor binding site. Cell 61: 505–514, 1990\nHorlein AJ, Naar AM, Heinzel T, Torchia J, Gloss B, Kurokawa R, Ryan A, Kamei Y, Soderstrom M, Glass CK, Rosenfeld MG: Ligandindependent repression by the thyroid hormone receptor mediated by a nuclear receptor co‐repressor. Nature 377: 397–404, 1995\nKurokawa R, Soderstrom M, Horlein A, Halachmi S, Brown M, Rosenfeld MG, Glass CK: Polarity‐specific activities of retinoic acid receptors determined by a co‐repressor. Nature 377: 451–454, 1995\nZhu YS, Yen PM, Chin WW, Pfaff DW: Estrogen and thyroid hormone interaction on regulation of gene expression. Proc Natl Acad Sci USA 93: 12587–12592, 1996\nDellovade TL, Zhu YS, Krey L, Pfaff DW: Thyroid hormone and estrogen interact to regulate behavior. Proc Natl Acad Sci USA 93: 12581–12586, 1996",{"VOID":1517},"10.1023\u002FA:1006918402474","2024-12-17T15:54:17.205+00:00",[134],"https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1023\u002FA:1006918402474",[1522,1537],{"id":1523,"sortIndex":19,"researcher":18,"roles":1524,"affiliations":1525,"properties":1534,"displayName":1536,"givenName":18,"familyName":18},"edc7a9c1-a4ed-4676-a386-fde82b42c570",[273],[1526],{"id":1527,"sortIndex":19,"affiliation":1528,"properties":18},"bedcfd7a-515f-4fb7-8134-ab306ffb2cba",{"id":1527,"createTime":18,"updateTime":18,"relativeEntities":1529,"slug":18,"properties":1530,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":1533,"statistic":18},[],{"title":1531},{"VI":1532},"Departments of Pathology, Biochemistry, Urology, and Cancer Center, University of Rochester, George Whipple Laboratory for Cancer Research, Rochester, USA",[],{"title":1535},{"VI":1536},"Chawnshang Chang",{"id":1538,"sortIndex":102,"researcher":18,"roles":1539,"affiliations":1540,"properties":1547,"displayName":1549,"givenName":18,"familyName":18},"c0b8392a-466d-4655-852e-ffdab7515c98",[273],[1541],{"id":1527,"sortIndex":19,"affiliation":1542,"properties":18},{"id":1527,"createTime":18,"updateTime":18,"relativeEntities":1543,"slug":18,"properties":1544,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":1546,"statistic":18},[],{"title":1545},{"VI":1532},[],{"title":1548},{"VI":1549},"Huei-Ju Pan",{"url":1520,"publisher":1551,"properties":1604},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1552,"slug":10,"properties":1553,"entityType":16,"verifyStatus":17,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":19,"subjectFields":1556,"manageAffiliations":1573,"indexDatabases":1584,"url":18,"thumbnailPath":18,"statistic":1599,"gsStatistic":18,"type":105,"analyzePriority":18},[],{"issn":1554,"title":1555},{"VOID":13},{"EN":15},[1557,1561,1565,1569],{"id":22,"createTime":18,"updateTime":18,"relativeEntities":1558,"label":1559,"description":1560,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":25},{},{"id":28,"createTime":18,"updateTime":18,"relativeEntities":1562,"label":1563,"description":1564,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":31},{},{"id":34,"createTime":18,"updateTime":18,"relativeEntities":1566,"label":1567,"description":1568,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":37},{},{"id":40,"createTime":18,"updateTime":18,"relativeEntities":1570,"label":1571,"description":1572,"parentId":18,"standard":18,"scholarHubFieldId":18},[],{"EN":43},{},[1574,1579],{"id":47,"createTime":18,"updateTime":18,"relativeEntities":1575,"slug":18,"properties":1576,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":1578,"statistic":18},[],{"title":1577},{"EN":51},[],{"id":54,"createTime":18,"updateTime":18,"relativeEntities":1580,"slug":18,"properties":1581,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":1583,"statistic":18},[],{"title":1582},{"EN":58},[60],[1585,1592],{"id":63,"indexDatabase":1586,"url":74,"indexYears":75,"academicFieldIds":1591,"indexDatabaseRanking":81},{"id":65,"createTime":18,"updateTime":18,"relativeEntities":1587,"label":1588,"description":1589,"key":71,"publicationTags":1590,"standard":18},[],{"EN":68,"VI":68},{"EN":68,"VI":70},[73],[77,78,79,80],{"id":83,"indexDatabase":1593,"url":18,"indexYears":18,"academicFieldIds":1598,"indexDatabaseRanking":18},{"id":85,"createTime":18,"updateTime":18,"relativeEntities":1594,"label":1595,"description":1596,"key":92,"publicationTags":1597,"standard":18},[],{"EN":88,"VI":88},{"EN":90,"VI":91},[94,95],[97],{"impactFactor":19,"impactFactorByYear":1600,"i10Index":19,"i10IndexLast5Year":19,"totalPublication":100,"totalPublicationByYear":1601,"totalCitation":19,"totalCitationByYear":1602,"totalCitationPerPublication":19,"totalCitationPerPublicationByYear":1603,"hindexLast5Year":19,"hindex":19},{},{"1999":102,"2000":102,"2001":102,"2002":102,"2004":102,"2012":102,"2019":102},{},{},{"pages":1605,"volume":1607},{"VOID":1606},"195-200",{"VOID":1608},"189","1998-12-01",1998,[94,81]]