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B16 cells exposed in vitro to TNF-alpha had an increased H-2 expression and were more metastatic than untreated cells. The simultaneous treatment with TNF-alpha and IFN-gamma amplified the enhancement of experimental metastasis and all other effects obtained with TNF-alpha alone. The B16 clone B78H1, selectively resistant to H-2 induction and to enhancement of metastatic ability by IFN-gamma, was not affected by treatment with TNF-alpha and with TNF-alpha + IFN-gamma. 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International Journal of Cancer, 32, 113–120.\nGopas, J., Segal, S., Hammerling, G., Bar-Eli, M., and Rager-Zisman, B., 1988, Influence of H-2K transfection on susceptibility of fibrosarcoma tumor cells to natural killer (NK) cells. Immunology Letters, 17, 261–266.\nGraf, L. H., Kaplan, P., and Silagi, S., 1984, Efficient DNA-mediated transfer of selectable genes and unselected sequences into differentiated and undifferentiated mouse melanoma clones. Somatic Cell and Molecular Genetics, 10, 139–151.\nHanna, N., and Burton, R. C., 1981, Definitive evidence that natural killer (NK) cells inhibit experimental tumor metastasis in vivo. Journal of Immunology, 127, 1754–1758.\nKawano, Y.-I., Taniguchi, K., Toshitani, A., and Nomoto, K., 1986, Synergistic defense system by cooperative natural effectors against metastasis of B16 melanoma cells in H-2-associated control: different behavior of H-2+ and H-2− cells in metastatic processes. Journal of Immunology, 136, 4729–4734.\nLollini, P.-L., De Giovanni, C., Del Re, B., Nicoletti, G., Prodi, G., and Nanni, P., 1987, Interferon-mediated enhancement of metastasis. Are MHC antigens involved? Clinical and Experimental Metastasis, 5, 277–287.\nLollini, P.-L., De Giovanni, C., Del Re, B., Nicoletti, G., Prodi, G., Scotlandi, K., and Nanni, P., 1988, Interferon-mediated modulation of metastasis and MHC antigens. Cancer Metastasis—Biological and biochemical mechanisms and clinical aspects, edited by G.Prodi, L. A. Liotta, P.-L. Lollini, S. Garbisa, S. Gorini, and K. Hellmann (New York: Plenum Press), pp. 129–140.\nMcMillan, T.J., Rao, J., Everett, C. A., and Hart, I. R., 1987, Interferon-induced alterations in metastatic capacity, class- I antigen expression and natural killer sensitivity of melanoma cells. International Journal of Cancer, 40, 659–663.\nNanni, P., Colombo, M. P., De Giovanni, C., Lollini, P.-L., Nicoletti, G., Parmiani, G., and Prodi, G., 1983, Impaired H-2 expression in B16 melanoma variants. Journal of Immunogenetics, 10, 361–370.\nPfizenmaier, K., Scheurich, P., Schlueter, C., and Kroenke, M., 1987, Tumor necrosis factor enhances HLA-A, B, C and HLA-DR gene expression in human tumor cells. Journal of Immunology, 138, 975–980.\nRager-Zisman, B., Gopas, J., Bar-Eli, M., Har-Vardi, I., Hammerling, G. J., and Segal, S., 1988, NK sensitivity, H-2, c-K-ras proto-oncogene expression and metastases: analysis of the metastatic potential of H-2 gene transfected fibrosarcoma cells. Cancer Metastasis—Biological and biochemical mechanisms and clinical aspects, edited by G. Prodi, L. A. Liotta, P.-L. Lollini, S. Garbisa, S. Gorini, and K. Hellmann (New York: Plenum Press), pp. 151–160.\nRamani, P., and Balkwill, F. R., 1987, Enhanced metastasis of a mouse carcinoma after in vitro treatment with murine interferon-gamma. International Journal of Cancer, 40, 830–834.\nSugarman, R. J., Aggarwal, B. B., Hass, P. E., Figari, I. S., Palladino, M. A. J., and Shepard, H. M., 1985, Recombinant human tumor necrosis factor-alpha: effects on proliferation of normal and transformed cells in vitro. Science, 230, 943–945.\nTalmadge, J. E., Tribble, H. R., Pennington, R. W., Phillips, H., and Wiltrout, R. H., 1987, Immunomodulatory and immuno therapeutic properties of recombinant gamma-interferon and recombinant tumor necrosis factor in mice. Cancer Research, 47, 2563–2570.\nTaniguchi, K., Karre, K., and Klein, G., 1985, Lung colonization and metastasis by disseminated B16 melanoma cells. H-2 associated control at the level of the host and the tumor cell. International Journal of Cancer, 36, 503–510.\nTaniguchi, K., Petersson, M., Hoglund, P., Kiessling, R., Klein, G., and Karre, K., 1987, Interferon-gamma induces lung colonization by intravenously inoculated B16 melanoma cells in parallel with enhanced expression of class I major histocompatibility complex antigens. Proceedings of the National Academy of Sciences, U.S.A., 84, 3405–3409.\nWexler, H., 1966, Accurate identification of experimental pulmonary metastases. Journal of the National Cancer Institute, 36, 641–645.\nWiltrout, R. H., Herberman, R. B., Zhang, S.-R., Chirigos, M. A., Ortaldo, J. R., Green, K. M. Jr, and Talmadge, J. E., 1985, Role of organ-associated NK cells in decreased formation of experimental metastases in lung and liver. Journal of Immunology, 134, 4267–4275.\nWong, G. H. W., and Goeddel, D. V., 1986, Tumor necrosis factors alpha and beta inhibit virus replication and synergise with interferons. Nature, 323, 819–822.\nZoeller, M., Strubel, A., Haemmerling, G., Andrighetto, G., Raz, A., and Benze'ev, A., 1988, Interferon-gamma treatment of B16 melanoma cells: opposing effects for non-adaptive and adaptive immune defense and its reflection by metastatic spread. 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RMCCA-1 cells expressed multiple forms of 25, 40, 75 and 115\u002F135 kDa NGAL which were detected in the conditioned medium, whereas only the 25 kDa form was detected in the cell lysates. NGAL expression was induced by serum deprivation. NGAL downregulation by siRNA suppressed NGAL mRNA and protein expression by about 70–80%, concommittant with a significant reduction of in vitro invasiveness, migration and pro-MMP-9 activity, but not cell proliferation. Suppression of pro-MMP-9 activity paralleled a reduction of NGAL\u002FMMP-9 complex in the conditioned medium, although MMP-9 mRNA expression was unaffected. Our data suggest that NGAL promotes the invasiveness of the cholangiocarcinoma cells by forming complex with MMP-9, stabilizing its activity and rendering the cancer cells to be more invasive.",{"EN":445,"VI":446},"NGAL knockdown by siRNA in human cholangiocarcinoma cells suppressed invasion by reducing NGAL\u002FMMP-9 complex formation","Knockdown NGAL bằng siRNA trong các tế bào ung thư đường mật ở người ức chế sự xâm lấn bằng cách làm giảm hình thành phức hợp NGAL\u002FMMP-9",{"VOID":448},"Anderson CD, Pinson CW, Berlin J et al (2004) Diagnosis and treatment of cholangiocarcinoma. Oncologist 9(1):43–57\nGores GJ (2003) Cholangiocarcinoma: current concepts and insights. Hepatology 37(5):961–969\nSirica AE (2005) Cholangiocarcinoma: molecular targeting strategies for chemoprevention and therapy. Hepatology 41(1):5–15\nFlower DR (1996) The lipocalin protein family: structure and function. Biochem J 318(Pt 1):1–14\nGoetz DH, Holmes MA, Borregaard N et al (2002) The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol Cell 10(5):1033–1043\nFriedl A, Stoesz SP, Buckley P et al (1999) Neutrophil gelatinase-associated lipocalin in normal and neoplastic human tissues. Cell type-specific pattern of expression. Histochem J 31(7):433–441\nNielsen BS, Borregaard N, Bundgaard JR et al (1996) Induction of NGAL synthesis in epithelial cells of human colorectal neoplasia and inflammatory bowel diseases. Gut 38(3):414–420\nTong Z, Wu X, Ovcharenko D et al (2005) Neutrophil gelatinase-associated lipocalin as a survival factor. Biochem J 391(Pt 2):441–448\nLee HJ, Lee EK, Lee KJ et al (2006) Ectopic expression of neutrophil gelatinase-associated lipocalin suppresses the invasion and liver metastasis of colon cancer cells. Int J Cancer 118(10):2490–2497\nStoesz SP, Friedl A, Haag JD et al (1998) Heterogeneous expression of the lipocalin NGAL in primary breast cancers. Int J Cancer 79(6):565–572\nGruvberger S, Ringner M, Chen Y et al (2001) Estrogen receptor status in breast cancer is associated with remarkably distinct gene expression patterns. Cancer Res 61(16):5979–5984\nBartsch S, Tschesche H (1995) Cloning and expression of human neutrophil lipocalin cDNA derived from bone marrow and ovarian cancer cells. FEBS Lett 357(3):255–259\nMoniaux N, Chakraborty S, Yalniz M et al (2008) Early diagnosis of pancreatic cancer: neutrophil gelatinase-associated lipocalin as a marker of pancreatic intraepithelial neoplasia. Br J Cancer 98(9):1540–1547\nTong Z, Kunnumakkara AB, Wang H et al (2008) Neutrophil gelatinase-associated lipocalin: a novel suppressor of invasion and angiogenesis in pancreatic cancer. Cancer Res 68(15):6100–6108\nShi H, Gu Y, Yang J et al (2008) Lipocalin 2 promotes lung metastasis of murine breast cancer cells. J Exp Clin Cancer Res 27:83\nFernandez CA, Yan L, Louis G et al (2005) The matrix metalloproteinase-9\u002Fneutrophil gelatinase-associated lipocalin complex plays a role in breast tumor growth and is present in the urine of breast cancer patients. Clin Cancer Res 11(15):5390–5395\nRattanasinganchan P, Leelawat K, Treepongkaruna SA et al (2006) Establishment and characterization of a cholangiocarcinoma cell line (RMCCA-1) from a Thai patient. World J Gastroenterol 12(40):6500–6506\nSripa B, Leungwattanawanit S, Nitta T et al (2005) Establishment and characterization of an opisthorchiasis-associated cholangiocarcinoma cell line (KKU-100). World J Gastroenterol 11(22):3392–3397\nYan L, Borregaard N, Kjeldsen L et al (2001) The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B\u002FMMP-9 and neutrophil gelatinase-associated lipocalin (NGAL). Modulation of MMP-9 activity by NGAL. J Biol Chem 276(40):37258–37265\nJayaraman A, Roberts KA, Yoon J et al (2005) Identification of neutrophil gelatinase-associated lipocalin (NGAL) as a discriminatory marker of the hepatocyte-secreted protein response to IL-1beta: a proteomic analysis. Biotechnol Bioeng 91(4):502–515\nZhang J, Wu Y, Zhang Y et al (2008) The role of lipocalin 2 in the regulation of inflammation in adipocytes and macrophages. Mol Endocrinol 22(6):1416–1426\nMishra J, Mori K, Ma Q et al (2004) Amelioration of ischemic acute renal injury by neutrophil gelatinase-associated lipocalin. J Am Soc Nephrol 15(12):3073–3082\nYan QW, Yang Q, Mody N et al (2007) The adipokine lipocalin 2 is regulated by obesity and promotes insulin resistance. Diabetes 56(10):2533–2540\nLiu Q, Nilsen-Hamilton M (1995) Identification of a new acute phase protein. J Biol Chem 270(38):22565–22570\nLiu QS, Nilsen-Hamilton M, Xiong SD (2003) Synergistic regulation of the acute phase protein SIP24\u002F24p3 by glucocorticoid and pro-inflammatory cytokines. Sheng Li Xue Bao 55(5):525–529\nLin HH, Li WW, Lee YC et al (2007) Apoptosis induced by uterine 24p3 protein in endometrial carcinoma cell line. Toxicology 234(3):203–215\nGoncharova EI, Nadas A, Rossman TG (1996) Serum deprivation, but not inhibition of growth per se, induces a hypermutable state in Chinese hamster G12 cells. Cancer Res 56(4):752–756\nPandey S, Lopez C, Jammu A (2003) Oxidative stress and activation of proteasome protease during serum deprivation-induced apoptosis in rat hepatoma cells; inhibition of cell death by melatonin. Apoptosis 8(5):497–508\nJoshi MB, Philippova M, Ivanov D et al (2005) T-cadherin protects endothelial cells from oxidative stress-induced apoptosis. Faseb J 19(12):1737–1739\nGupta AK, Lee YJ, Galoforo SS et al (1997) Differential effect of glucose deprivation on MAPK activation in drug sensitive human breast carcinoma MCF-7 and multidrug resistant MCF-7\u002FADR cells. Mol Cell Biochem 170(1–2):23–30\nLiu X, Gupta AK, Corry PM et al (1997) Hypoglycemia-induced c-Jun phosphorylation is mediated by c-Jun N-terminal kinase 1 and Lyn kinase in drug-resistant human breast carcinoma MCF-7\u002FADR cells. J Biol Chem 272(18):11690–11693\nLee YJ, Galoforo SS, Berns CM et al (1998) Glucose deprivation-induced cytotoxicity and alterations in mitogen-activated protein kinase activation are mediated by oxidative stress in multidrug-resistant human breast carcinoma cells. J Biol Chem 273(9):5294–5299\nLi EM, Xu LY, Cai WJ et al (2003) Functions of neutrophil gelatinase-associated lipocalin in the esophageal carcinoma cell line SHEEC. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:247–254\nIannetti A, Pacifico F, Acquaviva R et al (2008) The neutrophil gelatinase-associated lipocalin (NGAL), a NF-kappa B-regulated gene, is a survival factor for thyroid neoplastic cells. Proc Natl Acad Sci USA 105(37):14058–14063\nDunn LL, Sekyere EO, Rahmanto YS et al (2006) The function of melanotransferrin: a role in melanoma cell proliferation and tumorigenesis. Carcinogenesis 27(11):2157–2169\nThelander L, Reichard P (1979) Reduction of ribonucleotides. Annu Rev Biochem 48:133–158\nHu L, Hittelman W, Lu T et al (2009) NGAL decreases E-cadherin-mediated cell-cell adhesion and increases cell motility and invasion through Rac1 in colon carcinoma cells. Lab Invest 89(5):531–548\nCharest PG, Firtel RA (2007) Big roles for small GTPases in the control of directed cell movement. Biochem J 401(2):377–390\nZhang H, Xu L, Xiao D et al (2007) Upregulation of neutrophil gelatinase-associated lipocalin in oesophageal squamous cell carcinoma: significant correlation with cell differentiation and tumour invasion. 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was first discovered as a metastasis suppressor, but also plays crucial roles in the onset of puberty. The KISS1 gene encodes a secreted protein of 145 amino acids that exhibits no sequence similarity with any known proteins. KISS1 protein is proteolytically processed to generate a number of so-called kisspeptins (KP), the most well characterized is known as KP-54 or metastin. KP-54 is carboxy-terminally amidated and binds to and activates the KISS1 receptor (KISS1R). The current studies were undertaken in order to determine structure of KP-54 using nuclear magnetic resonance and circular dichroism. KP-54 is mostly disordered both in water and in trifluoroethanol\u002Fwater mixed solvent, with no structural motifs. In sodium dodecyl sulfate micelles, KP-54 remains mostly disordered except for a small increase in helical propensity (from 3.7% in water to 9.9% in micelles). Despite this apparent lack of structure, KP-54 is biologically active. The intrinsic disorder of KP-54 may confer advantages in its ability to recognize and bind a wide range of target proteins.",{"EN":574},"Nuclear magnetic resonance and circular dichroism study of metastin (Kisspeptin-54) structure in solution",{"VOID":576},"[\"4698740297684737666\"]",{"VOID":578},"10.1007\u002Fs10585-009-9252-0","2024-05-03T18:55:09.226+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10585-009-9252-0",[582,597,644,661,674,694],{"id":583,"sortIndex":21,"researcher":20,"roles":584,"affiliations":585,"properties":594,"displayName":596,"givenName":20,"familyName":20},"e59c6036-f99a-49aa-b79a-bc37b3bbca07",[247],[586],{"id":587,"sortIndex":21,"affiliation":588,"properties":20},"542b4a37-3b46-4c33-9345-787f7a54b10b",{"id":587,"createTime":20,"updateTime":20,"relativeEntities":589,"slug":20,"properties":590,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":593,"statistic":20},[],{"title":591},{"VI":592},"Comprehensive Cancer Center, The University of Alabama at Birmingham, Birmingham, USA",[],{"title":595},{"VI":596},"Ronald Shin",{"id":598,"sortIndex":259,"researcher":20,"roles":599,"affiliations":600,"properties":639,"displayName":641,"givenName":20,"familyName":20},"b2b4f394-0498-4f81-bcec-c3ccabab83c4",[247],[601,607,615,623,631],{"id":587,"sortIndex":21,"affiliation":602,"properties":20},{"id":587,"createTime":20,"updateTime":20,"relativeEntities":603,"slug":20,"properties":604,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":606,"statistic":20},[],{"title":605},{"VI":592},[],{"id":608,"sortIndex":259,"affiliation":609,"properties":20},"3719e343-9a9c-411c-ba72-5087efb314b0",{"id":608,"createTime":20,"updateTime":20,"relativeEntities":610,"slug":20,"properties":611,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":614,"statistic":20},[],{"title":612},{"VI":613},"Departments of Pathology, The University of Alabama at Birmingham, Birmingham, USA",[],{"id":616,"sortIndex":285,"affiliation":617,"properties":20},"f6ea485f-0e65-40a9-bd93-2b5f2290447c",{"id":616,"createTime":20,"updateTime":20,"relativeEntities":618,"slug":20,"properties":619,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":622,"statistic":20},[],{"title":620},{"VI":621},"Department of Cell Biology, The University of Alabama at Birmingham, Birmingham, USA",[],{"id":624,"sortIndex":306,"affiliation":625,"properties":20},"55b18dda-c157-4ddb-8760-3aef189e8947",{"id":624,"createTime":20,"updateTime":20,"relativeEntities":626,"slug":20,"properties":627,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":630,"statistic":20},[],{"title":628},{"VI":629},"Department of Pharmacology & Toxicology, The University of Alabama at Birmingham, Birmingham, USA",[],{"id":632,"sortIndex":176,"affiliation":633,"properties":20},"a4741420-7701-4b9a-be39-47afdc87f7d6",{"id":632,"createTime":20,"updateTime":20,"relativeEntities":634,"slug":20,"properties":635,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":638,"statistic":20},[],{"title":636},{"VI":637},"National Foundation for Cancer Research – Center for Metastasis Research, The University of Alabama at Birmingham, Birmingham, USA",[],{"title":640,"gsAuthor":642},{"VI":641},"Danny R. 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Cancer Microenviron 1:1–11. doi:10.1007\u002Fs12307-008-0001-8","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs12307-008-0001-8",{"doi":786},"10.1007\u002Fs12307-008-0001-8",{"id":20,"text":788,"url":789,"identifiers":790},"Stafford LJ, Vaidya KS, Welch DR (2008) Metastasis suppressors genes in cancer. Int J Biochem Cell Biol 40:874–891. doi:10.1016\u002Fj.biocel.2007.12.016","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.biocel.2007.12.016",{"mag":791,"openalex":792,"pm":793,"doi":794},"2123808188","W2123808188","18280770","10.1016\u002Fj.biocel.2007.12.016",{"id":796,"text":797,"url":798,"identifiers":799},"cf396b03-2629-4abd-abac-f7af79a2d91e","Lee J-H, Miele ME, Hicks DJ et al (1996) KiSS-1, a novel human malignant melanoma metastasis-suppressor gene. J Natl Cancer Inst 88:1731–1737. doi:10.1093\u002Fjnci\u002F88.23.1731","https:\u002F\u002Facademic.oup.com\u002Fjnci\u002Farticle-lookup\u002Fdoi\u002F10.1093\u002Fjnci\u002F88.23.1731",{"doi":800},"10.1093\u002Fjnci\u002F88.23.1731",{"id":802,"text":803,"url":804,"identifiers":805},"cda79a35-8560-4a77-9cef-c9899b2277f9","West A, Vojta PJ, Welch DR, Weissman BE (1998) Chromosome localization and genomic structure of the KiSS-1 metastasis suppressor gene (KISS1). Genomics 54:145–148. doi:10.1006\u002Fgeno.1998.5566","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0888754398955665",{"doi":806},"10.1006\u002Fgeno.1998.5566",{"id":808,"text":809,"url":810,"identifiers":811},"4c68646b-0035-4279-8000-0006b275d4fa","Goldberg SF, Miele ME, Hatta N et al (2003) Melanoma metastasis suppression by chromosome 6: evidence for a pathway regulated by CRSP3 and TXNIP. Cancer Res 63:432–440","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10440-022-00541-7",{"doi":812},"10.1007\u002Fs10440-022-00541-7",{"id":20,"text":814,"url":815,"identifiers":816},"Lee J-H, Welch DR (1997) Identification of highly expressed genes in metastasis-suppressed chromosome 6\u002Fhuman malignant melanoma hybrid cells using subtractive hybridization and differential display. Int J Cancer 71:1035–1044. doi:10.1002\u002F(SICI)1097-0215(19970611)71:6\u003C1035::AID-IJC20>3.0.CO;2-B","https:\u002F\u002Fdoi.org\u002F10.1002\u002F(sici)1097-0215(19970611)71:6\u003C1035::aid-ijc20>3.0.co;2-b",{"mag":817,"openalex":818,"pm":819,"doi":820},"2085037998","W2085037998","9185708","10.1002\u002F(sici)1097-0215(19970611)71:6",{"id":808,"text":822,"url":810,"identifiers":823},"Lee J-H, Welch DR (1997) Suppression of metastasis in human breast carcinoma MDA-MB-435 cells after transfection with the metastasis suppressor gene, KiSS-1. Cancer Res 57:2384–2387",{"doi":812},{"id":825,"text":826,"url":827,"identifiers":828},"1c112224-07eb-4dfa-a0e5-6ed5978af4e9","Jiang Y, Berk M, Singh LS et al (2005) KiSS1 suppresses metastasis in human ovarian cancer via inhibition of protein kinase C alpha. Clin Exp Metastasis 22:369–376. doi:10.1007\u002Fs10585-005-8186-4","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10585-005-8186-4",{"doi":829},"10.1007\u002Fs10585-005-8186-4",{"id":20,"text":831,"url":832,"identifiers":833},"Kotani M, Detheux M, Vandenbogaerde A et al (2001) The metastasis suppressor gene KiSS-1 encodes kisspeptins, the natural ligands of the orphan G protein-coupled receptor GPR54. J Biol Chem 276:34631–34636. doi:10.1074\u002Fjbc.M104847200","https:\u002F\u002Fdoi.org\u002F10.1074\u002Fjbc.m104847200",{"mag":834,"openalex":835,"pm":836,"doi":837},"2111338104","W2111338104","11457843","10.1074\u002Fjbc.m104847200",{"id":20,"text":839,"url":840,"identifiers":841},"Muir AI, Chamberlain L, Elshourbagy NA et al (2001) AXOR12: a novel human G protein-coupled receptor, activated by the peptide KiSS-1. J Biol Chem 276:28969–28975. doi:10.1074\u002Fjbc.M102743200","https:\u002F\u002Fdoi.org\u002F10.1074\u002Fjbc.m102743200",{"mag":842,"openalex":843,"pm":844,"doi":845},"2151613225","W2151613225","11387329","10.1074\u002Fjbc.m102743200",{"id":847,"text":848,"url":849,"identifiers":850},"d9cd6a5f-6d7c-43de-84f8-6265217daa0d","Ohtaki T, Shintani Y, Honda S et al (2001) Metastasis suppressor gene KiSS1 encodes peptide ligand of a G-protein-coupled receptor. Nature 411:613–617. doi:10.1038\u002F35079135","https:\u002F\u002Fwww.nature.com\u002Farticles\u002F35079135",{"doi":851},"10.1038\u002F35079135",{"id":20,"text":853,"url":20,"identifiers":854},"Nash KT, Phadke PA, Navenot J-M et al (2007) KISS1 metastasis suppressor secretion, multiple organ metastasis suppression, and maintenance of tumor dormancy. J Natl Cancer Inst 99:309–321. doi:10.1093\u002Fjnci\u002Fdjk053",{"doi":855},"10.1093\u002Fjnci\u002Fdjk053",{"id":857,"text":858,"url":859,"identifiers":860},"c80f177a-8cf2-4313-8b9d-8bbee7d55461","Goldberg SF, Harms JF, Quon K, Welch DR (1999) Metastasis-suppressed C8161 melanoma cells arrest in lung but fail to proliferate. 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Proteins 42:460–470. doi:10.1002\u002F1097-0134(20010301)42:4\u003C460::AID-PROT50>3.0.CO;2-U","https:\u002F\u002Fdoi.org\u002F10.1002\u002F1097-0134(20010301)42:4\u003C460::aid-prot50>3.0.co;2-u",{"mag":896,"openalex":897,"pm":898,"doi":899},"2059402338","W2059402338","11170201","10.1002\u002F1097-0134(20010301)42:4",{"id":20,"text":901,"url":902,"identifiers":903},"Gianetti E, Seminara S (2008) Kisspeptin and KISS1R: a critical pathway in the reproductive system. Reproduction 136:295–301. doi:10.1530\u002FREP-08-0091","https:\u002F\u002Fdoi.org\u002F10.1530\u002Frep-08-0091",{"mag":904,"pmc":905,"openalex":906,"pm":907,"doi":908},"2054664043","2858313","W2054664043","18515314","10.1530\u002Frep-08-0091",{"id":20,"text":910,"url":911,"identifiers":912},"Ohkura S, Uenoyama Y, Yamada S et al (2009) Physiological role of metastin\u002Fkisspeptin in regulating gonadotropin-releasing hormone (GnRH) secretion in female rats. Peptides 30:49–56. doi:10.1016\u002Fj.peptides.2008.08.004","https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.peptides.2008.08.004",{"mag":913,"openalex":914,"pm":915,"doi":916},"1998983965","W1998983965","18775461","10.1016\u002Fj.peptides.2008.08.004",{"id":918,"text":919,"url":920,"identifiers":921},"8b151e4f-4c31-416c-bde5-95bb6d00bcfe","Arai AC (2009) The role of kisspeptin and GPR54 in the hippocampus. Peptides 30:16–25. doi:10.1016\u002Fj.peptides.2008.07.023","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS0196978108003306",{"doi":922},"10.1016\u002Fj.peptides.2008.07.023",{"id":20,"text":924,"url":925,"identifiers":926},"Tena-Sempere M (2008) Timeline: the role of kisspeptins in reproductive biology. Nat Med 14:1196. doi:10.1038\u002Fnm1108-1196","https:\u002F\u002Fdoi.org\u002F10.1038\u002Fnm1108-1196",{"mag":927,"openalex":928,"pm":929,"doi":930},"1990149191","W1990149191","18989306","10.1038\u002Fnm1108-1196",{"id":20,"text":932,"url":933,"identifiers":934},"Cheng J, Randall AZ, Sweredoski MJ, Baldi P (2005) SCRATCH: a protein structure and structural feature prediction server. Nucleic Acids Res 33:W72–W76. doi:10.1093\u002Fnar\u002Fgki396","https:\u002F\u002Fdoi.org\u002F10.1093\u002Fnar\u002Fgki396",{"mag":935,"pmc":936,"openalex":937,"pm":938,"doi":939},"2096495474","1160157","W2096495474","15980571","10.1093\u002Fnar\u002Fgki396",{"id":808,"text":941,"url":810,"identifiers":942},"Wuthrich K (1986) NMR of proteins and nucleic acids. Wiley, New York",{"doi":812},{"id":944,"text":945,"url":946,"identifiers":947},"4647bd8a-725d-4223-a350-29b1edda453e","Rastogi VK, Girvin ME (1999) 1H, 13C, and 15 N assignments and secondary structure of the high pH form of subunit c of the F1F0 ATP synthase. J Biomol NMR 13:91–92. doi:10.1023\u002FA:1008379624478","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1023\u002FA:1008379624478",{"doi":948},"10.1023\u002FA:1008379624478",{"id":950,"text":951,"url":952,"identifiers":953},"d6144be0-2bf6-4bff-8da4-036313faa195","Sickmeier M, Hamilton JA, LeGall T et al (2007) DisProt: the database of disordered proteins. NAR 35:D786–D793. doi:10.1093\u002Fnar\u002Fgkl893","https:\u002F\u002Facademic.oup.com\u002Fnar\u002Farticle-lookup\u002Fdoi\u002F10.1093\u002Fnar\u002Fgkl893",{"doi":954},"10.1093\u002Fnar\u002Fgkl893",{"id":20,"text":956,"url":957,"identifiers":958},"Gaiser OJ, Ball LJ, Schmieder P et al (2004) Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1. Biochemistry 43:15983–15995. doi:10.1021\u002Fbi049550q","https:\u002F\u002Fdoi.org\u002F10.1021\u002Fbi049550q",{"mag":959,"openalex":960,"pm":961,"doi":962},"2149806742","W2149806742","15609993","10.1021\u002Fbi049550q",{"id":20,"text":964,"url":965,"identifiers":966},"Sunde M, McGrath KCY, Young L et al (2004) TC-1 is a novel tumorigenic and natively disordered protein associated with thyroid cancer. Cancer Res 64:2766–2773. doi:10.1158\u002F0008-5472.CAN-03-2093","https:\u002F\u002Fdoi.org\u002F10.1158\u002F0008-5472.can-03-2093",{"mag":967,"openalex":968,"pm":969,"doi":970},"2135293703","W2135293703","15087392","10.1158\u002F0008-5472.can-03-2093",{"id":20,"text":972,"url":973,"identifiers":974},"Orsini MJ, Klein MA, Beavers MP, Connolly PJ, Middleton SA, Mayo KH (2007) Metastin (KiSS-1) mimetics identified from peptide structure-activity relationship-derived pharmacophores and directed small molecule database screening. J Med Chem 50:462–471. doi:10.1021\u002Fjm0609824","https:\u002F\u002Fdoi.org\u002F10.1021\u002Fjm0609824",{"mag":975,"openalex":976,"pm":977,"doi":978},"1991647807","W1991647807","17266198","10.1021\u002Fjm0609824",{"id":980,"createTime":981,"updateTime":982,"relativeEntities":983,"slug":984,"properties":985,"entityType":236,"verifyStatus":237,"verifyTime":996,"verifyNote":239,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":997,"fullTextUrl":20,"authors":998,"publicationType":374,"publisherRelationship":1092,"citationCount":20,"citationInfo":20,"publishDate":1148,"publishYear":1149,"citationAnalyzeStatus":1150,"lastCitationAnalyze":982,"indexDatabases":1151,"openAccess":20,"references":20,"isForceReanalyzing":434},"c6d97796-5554-49a9-8183-eb0ce2832d89","2024-02-18T01:01:57.152+00:00","2026-08-13T14:11:39.185+00:00",[],"NM23-deficiency-promotes-metastasis-in-a-UV-radiation-induced-mouse-model-of-human-melanoma",{"abstract":986,"title":988,"gsPaper":990,"references":992,"doi":994},{"EN":987},"Cutaneous malignant melanoma is the most lethal form of skin cancer, with 5-year survival rates of \u003C5 % for patients presenting with metastatic disease. Mechanisms underlying metastatic spread of UVR-induced melanoma are not well understood, in part due to a paucity of animal models that accurately recapitulate the disease in its advanced forms. We have employed a transgenic mouse strain harboring a tandem deletion of the nm23-m1 and nm23-m2 genes to assess the combined contribution of these genes to suppression of melanoma metastasis. Crossing of the nm23-h1\u002Fnm23-h2 knockout in hemizygous-null form ([m1m2]+\u002F−) to a transgenic mouse strain (hepatocyte growth factor\u002Fscatter factor-overexpressing, or HGF+ strain) vulnerable to poorly-metastatic, UVR-induced melanomas resulted in UVR-induced melanomas with high metastatic potential. Metastasis to draining lymph nodes was seen in almost all cases of back skin melanomas, while aggressive metastasis to lung, thoracic cavity, liver and bone also occurred. Interestingly, no differences were observed in the invasive characteristics of primary melanomas of HGF+ and HGF+ × [m1m2]+\u002F− strains, with both exhibiting invasion into the dermis and subcutis, indicating factors other than simple invasive activity were responsible for metastasis of HGF+ × [m1m2]+\u002F− melanomas. Stable cell lines were established from the primary and metastatic melanoma lesions from these mice, with HGF+ × [m1m2]+\u002F− lines exhibiting increased single cell migration and genomic instability. These studies demonstrate for the first time in vivo a potent metastasis suppressor activity of NM23 in UVR-induced melanoma, and have provided new tools for identifying molecular mechanisms that underlie melanoma metastasis.",{"EN":989},"NM23 deficiency promotes metastasis in a UV radiation-induced mouse model of human melanoma",{"VOID":991},"[]",{"VOID":993},"Linos K, Slominski A, Ross JS, Carlson JA (2011) Melanoma update: diagnostic and prognostic factors that can effectively shape and personalize management. Biomark Med 5(3):333–360\nGandini S, Autier P, Boniol M (2011) Reviews on sun exposure and artificial light and melanoma. Prog Biophys Mol Biol 107(3):362–366\nGreen AC, Wallingford SC, McBride P (2011) Childhood exposure to ultraviolet radiation and harmful skin effects: epidemiological evidence. 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Nat Immunol 17(4):364–8",{"doi":812},{"id":1338,"text":1339,"url":1340,"identifiers":1341},"5ca9f0d0-418c-47e9-85eb-14599a92dc9d","Pauken KE, Sammons MA, Odorizzi PM, Manne S, Godec J, Khan O et al (2016) Epigenetic stability of exhausted T cells limits durability of reinvigoration by PD-1 blockade. Science 354(6316):1160–5","https:\u002F\u002Fwww.science.org\u002Fdoi\u002F10.1126\u002Fscience.aaf2807",{"doi":1342},"10.1126\u002Fscience.aaf2807",{"id":808,"text":1344,"url":810,"identifiers":1345},"Haddad R, Saldanha-Araujo F (2014) Mechanisms of T-cell immunosuppression by mesenchymal stromal cells: what do we know so far? BioMed Res Int 2014:216806",{"doi":812},{"id":808,"text":1347,"url":810,"identifiers":1348},"Stromnes IM, Greenberg PD, Hingorani SR (2014 Oct 15) Molecular pathways: myeloid complicity in cancer. Clin Cancer Res Off J Am Assoc Cancer Res 20(20):5157–70",{"doi":812},{"id":808,"text":1350,"url":810,"identifiers":1351},"Chou CK, Schietinger A, Liggitt HD, Tan X, Funk S, Freeman GJ et al (2012) Cell-intrinsic abrogation of TGF-β signaling delays but does not prevent dysfunction of self\u002Ftumor-specific CD8 T cells in a murine model of autochthonous prostate cancer. J Immunol Baltim Md 1950 89(8):3936–3946",{"doi":812},{"id":1353,"text":1354,"url":1355,"identifiers":1356},"01dab8c0-5006-4091-8b71-1fa9f37758ef","Soliman H, Rawal B, Fulp J, Lee J-H, Lopez A, Bui MM et al (2013) Analysis of indoleamine 2–3 dioxygenase (IDO1) expression in breast cancer tissue by immunohistochemistry. Cancer Immunol Immunother CII 62(5):829–37","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs00262-013-1393-y",{"doi":1357},"10.1007\u002Fs00262-013-1393-y",{"id":808,"text":1359,"url":810,"identifiers":1360},"Kuol N, Stojanovska L, Apostolopoulos V, Nurgali K (2018 Feb) Crosstalk between cancer and the neuro-immune system. J Neuroimmunol 15(315):15–23",{"doi":812},{"id":808,"text":1362,"url":810,"identifiers":1363},"Gajewski TF, Schreiber H, Fu Y-X (2013) Innate and adaptive immune cells in the tumor microenvironment. Nat Immunol 14(10):1014–22",{"doi":812},{"id":808,"text":1365,"url":810,"identifiers":1366},"Whiteside TL (2008 Oct 6) The tumor microenvironment and its role in promoting tumor growth. Oncogene. 27(45):5904–12",{"doi":812},{"id":808,"text":1368,"url":810,"identifiers":1369},"Berger AC, Korkut A, Kanchi RS, Hegde AM, Lenoir W, Liu W et al (2018) A comprehensive pan-cancer molecular study of gynecologic and breast cancers. Cancer Cell 33(4):690-705.e9",{"doi":812},{"id":808,"text":1371,"url":810,"identifiers":1372},"Olivier M, Asmis R, Hawkins GA, Howard TD, Cox LA (2019 Sep 26) The need for multi-omics biomarker signatures in precision medicine. Int J Mol Sci 20(19):4781",{"doi":812},{"id":1374,"text":1375,"url":1376,"identifiers":1377},"141fc3f6-0d25-4db4-97bc-41790a8883a9","Mitri ZI, Parmar S, Johnson B, Kolodzie A, Keck JM, Morris M et al (2018) Implementing a comprehensive translational oncology platform: from molecular testing to actionability. J Transl Med 16(1):358","https:\u002F\u002Ftranslational-medicine.biomedcentral.com\u002Farticles\u002F10.1186\u002Fs12967-018-1733-y",{"doi":1378},"10.1186\u002Fs12967-018-1733-y",{"id":808,"text":1380,"url":810,"identifiers":1381},"Prasad V (2016) Perspective: the precision-oncology illusion. Nature 537(7619):S63",{"doi":812},{"id":808,"text":1383,"url":810,"identifiers":1384},"Meric-Bernstam F, Brusco L, Shaw K, Horombe C, Kopetz S, Davies MA et al (2015) Feasibility of large-scale genomic testing to facilitate enrollment onto genomically matched clinical trials. J Clin Oncol Off J Am Soc Clin Oncol 33(25):2753–62",{"doi":812},{"id":808,"text":1386,"url":810,"identifiers":1387},"Flaherty KT, Gray R, Chen A, Li S, Patton D, Hamilton SR et al (2020) The molecular analysis for therapy choice (NCI-MATCH) trial: lessons for genomic trial design. J Natl Cancer Inst 112(10):1021–9",{"doi":812},{"id":808,"text":1389,"url":810,"identifiers":1390},"Ng PK-S, Li J, Jeong KJ, Shao S, Chen H, Tsang YH et al (2018) Systematic functional annotation of somatic mutations in cancer. Cancer Cell 33(3):450–462",{"doi":812},{"id":808,"text":1392,"url":810,"identifiers":1393},"Tsang YH, Dogruluk T, Tedeschi PM, Wardwell-Ozgo J, Lu H, Espitia M et al (2016) Functional annotation of rare gene aberration drivers of pancreatic cancer. Nat Commun 25(7):10500",{"doi":812},{"id":808,"text":1395,"url":810,"identifiers":1396},"Ellsworth RE, Blackburn HL, Shriver CD, Soon-Shiong P, Ellsworth DL (2017) Molecular heterogeneity in breast cancer: State of the science and implications for patient care. Semin Cell Dev Biol 64:65–72",{"doi":812},{"id":808,"text":1398,"url":810,"identifiers":1399},"Turashvili G, Brogi E (2017) Tumor heterogeneity in breast cancer. Front Med 4:227",{"doi":812},{"id":808,"text":1401,"url":810,"identifiers":1402},"Pectasides E, Stachler MD, Derks S, Liu Y, Maron S, Islam M et al (2018) Genomic heterogeneity as a barrier to precision medicine in gastroesophageal adenocarcinoma. Cancer Discov 8(1):37–48",{"doi":812},{"id":808,"text":1404,"url":810,"identifiers":1405},"Ward HW (1973 Jan 6) Anti-oestrogen therapy for breast cancer: a trial of tamoxifen at two dose levels. Br Med J 1(5844):13–4",{"doi":812},{"id":808,"text":1407,"url":810,"identifiers":1408},"Lerner HJ, Band PR, Israel L, Leung BS (1976) Phase II study of tamoxifen: report of 74 patients with stage IV breast cancer. Cancer Treat Rep 60(10):1431–5",{"doi":812},{"id":1410,"createTime":1411,"updateTime":1412,"relativeEntities":1413,"slug":1414,"properties":1415,"entityType":236,"verifyStatus":237,"verifyTime":1426,"verifyNote":239,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1427,"fullTextUrl":20,"authors":1428,"publicationType":374,"publisherRelationship":1470,"citationCount":1526,"citationInfo":1527,"publishDate":1532,"publishYear":1528,"citationAnalyzeStatus":1277,"lastCitationAnalyze":1533,"indexDatabases":1534,"openAccess":20,"references":20,"isForceReanalyzing":434},"0ca7dad3-ad6a-4cd0-812c-ba25564401d0","2024-01-09T08:20:43.731+00:00","2026-07-25T19:05:12.846+00:00",[],"Osteopontin-OPN-may-facilitate-metastasis-by-protecting-cells-from-macrophage-NO-mediated-cytotoxicity-evidence-from-cell-lines-down-regulated-for-OPN-expression-by-a-targeted-ribozyme",{"abstract":1416,"title":1418,"gsPaper":1420,"references":1422,"doi":1424},{"EN":1417},"Osteopontin (OPN) is a GRGDS-containing phosphoglycoprotein that is capable of facilitating cell adhesion and modulating gene expression via integrin receptors. Three hammerhead ribozymes designed to target three different regions of OPN mRNA were shown to cleave the message catalyticallyin vitro. Plasmid vectors that had been engineered to express the ribozymes in mammalian cells were used to generate stably transfected T24 H-ras-transformed NIH3T3 cells that normally express OPN at high levels. Northern and Western blot analyses showed that OPN mRNA and protein expression were reduced in a subset of these anti-OPN ribozyme-expressing cell lines. Cells whose ability to produce OPN had been impaired exhibited greater sensitivity to the cytotoxic action of activated RAW264.7 macrophage-like cells; they were also less effective at suppressing macrophage NO production. In agreement with previous reports, they were also less tumorigenic and metastatic in an experimental metastasis assay. These results are consistent with the hypothesis that OPN serves as a defense against NO-mediated host cell cytotoxicity and thereby augments the metastatic phenotype.",{"EN":1419},"Osteopontin (OPN) may facilitate metastasis by protecting cells from macrophage NO-mediated cytotoxicity: evidence from cell lines down-regulated for OPN expression by a targeted ribozyme",{"VOID":1421},"[\"2285035706110033096\"]",{"VOID":1423},"Butler, WT, 1989, The nature and significance of osteopontin.Connect Tissue Res,23, 123–36.\nDenhardt, DT and Guo, X, 1993, Osteopontin: a protein with diverse functions.FASEB J,7, 1475–82.\nSenger, DR and Perruzzi, CA, 1985, Secreted phosphoprotein marks for neoplastic transformation of human epithelial and fibroblastic cells.Cancer Res,45, 5818–23.\nSenger, DR, Perruzzi, CA and Papadopoulos, A, 1989, Elevated expression of secreted phosphoprotein I (osteopontin, 2ar) as a consequence of neoplastic transformation.Anticancer Res,9, 1291–300.\nChambers, AF, Behrend, EI, Wilson, SM and Denhardt, DT, 1992, Induction of expression of osteopontin (opn; secreted phosphoprotein) in metastatic, ras-transformed NIH 3T3 cells.Anticancer Res,12, 43–8.\nSmith, JH and Denhardt, DT, 1989, Evidence for two pathways of protein kinase C induction of 2ar expression: Correlation with mitogenesis.J Cell Physiol,139, 189–95.\nCraig, AM, Smith, JH and Denhardt, DT, 1989, Osteopontin, a transformation-associated cell adhesion phosphoprotein, is induced by 12-O-tetradecanoylphorbol 13-acetate in mouse epidermis.J Biol Chem,264, 9682–9.\nCraig, AM, Bowden, GT, Chambers, AF,et al. 1990, Secreted phosphoprotein mRNA is induced during multi-stage carcinogenesis in mouse skin and correlates with the metastatic potential of murine fibroblasts.Int J Cancer,46, 133–7.\nTuck, AB, Wilson, SM, Sergovich, FR and Chambers, AF, 1991, Gene expression and metastasis of somatic cell hybrids between murine fibroblast cell lines of different malignant potential.Somatic Cell Molec Gen. 17, 337–89.\nPatarca, R, Freeman, GJ, Singh, RP,et al. 1989, Structural and functional studies of the early T lymphocyte activation gene 1(Eta-1) Gene.J Exp Med,170, 145–61.\nPatarca, R, Saavedra, RA and Cantor, H, 1993, Molecular and cellular basis of genetic resistance to bacterial infection: the role of the early T-lymphocyte activation-1\u002Fosteopontin gene.Crit Rev Immunol,13, 225–46.\nHwang, SM, Lopez, CA, Heck, DE,et al. 1994, Osteopontin inhibits induction of nitric oxide synthase gene expression by inflammatory mediators in mouse kidney epithelial cells.J Biol Chem,269, 711–715.\nHaseloff, J and Gerlach, WL, 1988, Simple RNA enzymes with new and highly specific endoribonuclease activities.Nature,334, 585–91.\nUhlenbeck, OC, 1987, A small catalytic oligonucleotide.Nature,328, 596–600.\nLarson, GP, Bertrand, E and Rossi, JJ, 1993, Designing and testing of ribozymes as therapeutic agents.Methods: A Companion to Methods in Enzymology,5, 19–27.\nBratty, J, Chartrand, P, Ferbeyre, G and Cedergren, R, 1993, The hammerhead RNA domain, a model ribozyme.Biochim Biophys Acta,1216, 345–59.\nKnowles, RG and Moncada, S, 1994, Nitric oxide synthases in mammals.Biochem J,298, 249–58.\nFidler, IJ, 1990, Critical factors in the biology of human cancer metastasis.Cancer Res,50, 6130–8.\nDong, Z, Staroselsky, AH, Qi, X, Keping, X and Fidler, IJ, 1994, Inverse correlation between expression of inducible nitric oxide synthase activity and production of metastasis in K-1735 murine melanoma cells.Cancer Res,54, 789–93.\nLi, L, Kilbourn, RG, Adams, J and Fidler, IJ, 1991, Role of nitric oxide in lysis of tumor cells by cytokineactivated endothelial cells.Cancer Res,51, 2531–5.\nLorsbach, RB, Murphy, WJ, Lowenstein, CJ, Snyder, SH and Russell, SW, 1993, Expression of the nitric oxide synthase gene in mouse macrophages activated for tumor cell killing.J Biol Chem,268, 1908–13.\nIsobe, KI and Nakashima, I, 1993, Abundant production of nitric oxide from murine macrophages by direct stimulation of tumor cells.Biochem Biophys Res Commun,192, 499–504.\nIoannidis, I and de Groot, H, 1993, Cytotoxicity of nitric oxide in Fu5 rat hepatoma cells: evidence for cooperative action with hydrogen peroxide.Biochem J,296, 341–5.\nHill, SA, Wilson, S and Chambers, AF, 1988, Clonal heterogeneity, experimental metastatic ability, and p21 expression in H-ras-transformed NIH 3T3 cells.J Natl Cancer Inst,80, 484–90.\nChambers, AF, Denhardt, GH and Wilson, SM, 1990,Ras-transformed NIH 3T3 cell lines, selected for metastatic ability in chick embryos, have increased proportions of p21-expressing cells and are metastatic in nude mice.Invasion Metastasis,10,.225–40.\nKhokha, R and Denhardt, DT, 1987, On the use of antisense-RNA: down-regulation of mRNA encoding a metalloproteinase inhibitor.Anticancer Res,7, 653–60.\nGunning, P, Leavitt, J, Muscat, G, Ng, SY and Kedes, L, 1987, A human β-actin expression vector system directs high-level accumulation of antisense transcripts.Proc Natl Acad Sci USA,84, 4831–5.\nSambrook, J, Fritsch, EF and Maniatis, T, 1989, Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.\nIgnarro, LJ, Fukuto, JM, Griscavage, JM, Rogers, NE and Byrns, RF, 1993, Oxidation of nitric oxide in aqueous solution to nitrite but not nitrate: comparison with enzymatically formed nitric oxide froml-arginine.Proc Natl Acad Sci USA,90, 8103–7.\nBehrend, EI, Craig, AM, Wilson, SM, Denhardt, DT and Chambers, AF, 1994, Reduced malignancy ofras-transformed N1H3T3 cells expressing antisense osteopontin RNA.Cancer Res,54, 832–7.\nGardner, HAR, Berse, B and Senger, DR, 1994, Specific reduction in osteopontin synthesis by antisense RNA inhibits the tumorigenicity of transformed ratl fibroblasts.Oncogene,9, 2321–6.\nDenhardt, DT, Greenberg, AH, Egan, SE, Hamilton, RT and Wright, JA, 1987, Cysteine proteinase cathepsin L expression correlates closely with the metastatic potential of H-ras-transformed murine fibroblasts.Oncogene,2, 55–9.\nChambers, AF, Colella, R, Denhardt, DT and Wilson, SM, 1992, Increased activity of cathepsins L and B and decreased activity of their inhibitors in metastatic,ras-transformed NIH3T3 cells.Molec Carcin,5, 238–45.\nSarver, N, Cantin, EM, Chang, PS,et al. 1990, Ribozyme as potential anti-HIV-1 therapeutic agents.Science,247, 1222–5.\nCantor, GH, McElwain, TF, Birkebak, TA and Palmer, GH, 1993, Ribozyme cleaves rex\u002Ftar mRNA and inhibits bovine leukemia virus expression.Proc Natl Acad Sci USA,90, 10932–6.\nKashani-Sabet, M, Funato, T, Florenes, VA, Fodstad, O and Scanlon, KJ, 1994, Suppression of the neoplastic phenotypein vivo by an anti-ras ribozyme.Cancer Res,54, 900–2.\nBertrand, E, Pictet, R and Grange, T, 1994, Can hammerhead ribozymes be efficient tools to inactivate gene function?Nucleic Acids Res,22, 293–300.\nHendry, P, MaCall, MJ, Santiago, ITS and Jennings, PA, 1992, A ribozyme with DNA in the hybridising arms displays enhanced cleavage ability.Nucleic Acids Res,20, 5737–41.\nTaylor, NR, Kaplan, BE, Swiderski, P, Li, H and Rossi, JJ, 1992, Chimeric DNA-RNA hammerhead ribozymes have enhancedin vitro catalytic efficiency and increased stabilityin vivo.Nucleic Acids Res,20, 4559–65.\nEllis, J and Rogers, J, 1993, Design and specificity of hammerhead ribozymes against calretinin mRNA.Nucleic Acids Res,21, 5171–8.\nMateo, RB and Albina, JE, 1994, Is NO a necessary but not sufficient effector for macrophage tumor cytotoxicity?FASEB J (Abstract),8:A209.\nDenko, NC, Giaccia, AJ, Stringer, JR and Stambrook, PJ, 1994, The human Ha-ras oncogene induces genomic instability in murine fibroblasts within one cell cycle.Proc Natl Acad Sci USA,91, 5124–8.\nDenhardt, DT and Chambers, AF, 1994, Overcoming obstacles to metastasis — Defenses against host defenses: osteopontin (OPN) as a shield against attack by cytotoxic host cells.J Cell Biochem,56, 48–51.",{"VOID":1425},"10.1007\u002FBF00118184","2024-05-27T21:01:14.195+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002FBF00118184",[1429,1444,1457],{"id":1430,"sortIndex":21,"researcher":20,"roles":1431,"affiliations":1432,"properties":1441,"displayName":1443,"givenName":20,"familyName":20},"88b9d788-1a08-47b2-bd1b-50622d46deab",[247],[1433],{"id":1434,"sortIndex":21,"affiliation":1435,"properties":20},"0c96b1d4-7283-40ee-977a-f9701dba5ba2",{"id":1434,"createTime":20,"updateTime":20,"relativeEntities":1436,"slug":20,"properties":1437,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1440,"statistic":20},[],{"title":1438},{"VI":1439},"Department of Biological Sciences, Rutgers University, Piscataway, USA",[],{"title":1442},{"VI":1443},"Bo Feng",{"id":1445,"sortIndex":259,"researcher":20,"roles":1446,"affiliations":1447,"properties":1454,"displayName":1456,"givenName":20,"familyName":20},"11c0936c-1de0-4c55-a372-f926fecc6331",[247],[1448],{"id":1434,"sortIndex":21,"affiliation":1449,"properties":20},{"id":1434,"createTime":20,"updateTime":20,"relativeEntities":1450,"slug":20,"properties":1451,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1453,"statistic":20},[],{"title":1452},{"VI":1439},[],{"title":1455},{"VI":1456},"Ellen E. Rollo",{"id":1458,"sortIndex":285,"researcher":20,"roles":1459,"affiliations":1460,"properties":1467,"displayName":1469,"givenName":20,"familyName":20},"14db3ebd-9cf2-48c6-b24e-e2717dd0ceb0",[247],[1461],{"id":1434,"sortIndex":21,"affiliation":1462,"properties":20},{"id":1434,"createTime":20,"updateTime":20,"relativeEntities":1463,"slug":20,"properties":1464,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1466,"statistic":20},[],{"title":1465},{"VI":1439},[],{"title":1468},{"VI":1469},"David T. Denhardt",{"url":1427,"publisher":1471,"properties":1521},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1472,"slug":10,"properties":1473,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1477,"manageAffiliations":1490,"indexDatabases":1501,"url":20,"thumbnailPath":20,"statistic":1516,"gsStatistic":20,"type":20,"analyzePriority":20},[],{"issn":1474,"title":1475,"eissn":1476},{"VOID":13},{"EN":15},{"VOID":17},[1478,1482,1486],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":1479,"label":1480,"description":1481,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":1483,"label":1484,"description":1485,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":1487,"label":1488,"description":1489,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},[1491,1496],{"id":43,"createTime":20,"updateTime":20,"relativeEntities":1492,"slug":20,"properties":1493,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1495,"statistic":20},[],{"title":1494},{"EN":47},[49],{"id":51,"createTime":20,"updateTime":20,"relativeEntities":1497,"slug":20,"properties":1498,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1500,"statistic":20},[],{"title":1499},{"EN":55},[],[1502,1509],{"id":59,"indexDatabase":1503,"url":70,"indexYears":71,"academicFieldIds":1508,"indexDatabaseRanking":76},{"id":61,"createTime":20,"updateTime":20,"relativeEntities":1504,"label":1505,"description":1506,"key":67,"publicationTags":1507,"standard":20},[],{"EN":64,"VI":64},{"EN":64,"VI":66},[69],[73,74,75],{"id":78,"indexDatabase":1510,"url":91,"indexYears":20,"academicFieldIds":1515,"indexDatabaseRanking":20},{"id":80,"createTime":20,"updateTime":20,"relativeEntities":1511,"label":1512,"description":1513,"key":87,"publicationTags":1514,"standard":20},[],{"EN":83,"VI":83},{"EN":85,"VI":86},[89,90],[93],{"impactFactor":21,"impactFactorByYear":1517,"i10Index":108,"i10IndexLast5Year":109,"totalPublication":110,"totalPublicationByYear":1518,"totalCitation":144,"totalCitationByYear":1519,"totalCitationPerPublication":177,"totalCitationPerPublicationByYear":1520,"hindexLast5Year":215,"hindex":215},{"2012":96,"2013":97,"2014":98,"2015":99,"2016":100,"2017":101,"2018":102,"2019":103,"2020":104,"2021":105,"2022":106,"2023":107},{"1983":112,"1984":113,"1985":114,"1986":115,"1987":116,"1988":117,"1989":118,"1990":119,"1991":120,"1992":121,"1993":122,"1994":123,"1995":124,"1996":125,"1997":117,"1998":126,"1999":127,"2000":128,"2002":129,"2003":130,"2004":131,"2005":132,"2006":133,"2007":134,"2008":135,"2009":136,"2010":137,"2011":138,"2012":139,"2013":140,"2014":141,"2015":138,"2016":118,"2017":142,"2018":138,"2019":137,"2020":122,"2021":141,"2022":143,"2023":119,"2024":115},{"1983":146,"1984":147,"1985":126,"1986":143,"1987":142,"1988":148,"1989":149,"1990":123,"1991":150,"1992":151,"1993":152,"1994":153,"1995":154,"1996":155,"1998":156,"2003":157,"2004":158,"2005":159,"2006":160,"2007":161,"2008":162,"2009":163,"2010":164,"2011":165,"2012":166,"2013":167,"2014":168,"2015":169,"2016":153,"2017":170,"2018":171,"2019":172,"2020":173,"2021":174,"2022":175,"2023":176},{"1983":179,"1984":180,"1985":181,"1986":182,"1987":183,"1988":184,"1989":185,"1990":186,"1991":187,"1992":188,"1993":189,"1994":190,"1995":191,"1996":192,"1998":193,"2003":194,"2004":195,"2005":196,"2006":197,"2007":198,"2008":199,"2009":200,"2010":201,"2011":202,"2012":203,"2013":204,"2014":205,"2015":206,"2016":207,"2017":208,"2018":209,"2019":210,"2020":211,"2021":212,"2022":213,"2023":214},{"pages":1522,"volume":1524},{"VOID":1523},"453-462",{"VOID":1525},"13",93,{"total":1526,"publishYear":1528,"statisticByYear":1529},1995,{"1996":335,"1997":176,"1998":1530,"1999":335,"2000":349,"2001":772,"2002":1531,"2003":170,"2004":170,"2005":176,"2006":285,"2007":259,"2008":335,"2009":176,"2010":306,"2012":285,"2013":259,"2014":176,"2015":259,"2017":259,"2018":259,"2021":259,"2022":259,"2023":259},9,10,"1995-11-01","2026-07-25T19:05:12.845+00:00",[89,76],{"id":1536,"createTime":1537,"updateTime":1538,"relativeEntities":1539,"slug":1540,"properties":1541,"entityType":236,"verifyStatus":237,"verifyTime":1552,"verifyNote":239,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1553,"fullTextUrl":20,"authors":1554,"publicationType":374,"publisherRelationship":1626,"citationCount":1682,"citationInfo":1683,"publishDate":1689,"publishYear":1684,"citationAnalyzeStatus":1277,"lastCitationAnalyze":1690,"indexDatabases":1691,"openAccess":20,"references":20,"isForceReanalyzing":434},"a0d49894-d00e-43a9-8159-2bfe484cfb61","2024-01-15T14:02:50.009+00:00","2026-07-24T02:37:42.850+00:00",[],"Genetics-of-metastasis-melanoma-and-other-cancers",{"abstract":1542,"title":1544,"gsPaper":1546,"references":1548,"doi":1550},{"EN":1543},"Melanoma is a malignant neoplasm of melanocytes that accounts for the majority of skin cancer deaths despite comprising less than 5% of all cutaneous malignancies. Its incidence has increased faster than that of any other cancer over the past half-century and the annual costs of treatment in the United States alone have risen rapidly. Although the majority of primary melanomas are cured with local excision, metastatic melanoma historically carries a grim prognosis, with a median survival of 9 months and a long-term survival rate of 10%. Given the urgent need to develop treatment strategies for metastatic melanoma and the explosion of genetic technologies over the past 20 years, there has been extensive research into the genetic alterations that cause melanocytes to become malignant. More recently, efforts have focused on the genetic changes that drive melanoma metastasis. This review aims to summarize the current knowledge of the genetics of primary cutaneous and ocular melanoma, the genetic changes associated with metastasis in melanoma and other cancer types, and non-genetic factors that may contribute to metastasis.",{"EN":1545},"Genetics of metastasis: melanoma and other cancers",{"VOID":1547},"[\"136078841611540123\"]",{"VOID":1549},"Clark WH Jr, Elder DE, Van Horn M (1986) The biologic forms of malignant melanoma. Hum Pathol 17(5):443–450\nArrington JH 3rd et al (1977) Plantar lentiginous melanoma: a distinctive variant of human cutaneous malignant melanoma. Am J Surg Pathol 1(2):131–143\nPandiani C et al (2017) Focus on cutaneous and uveal melanoma specificities. Genes Dev 31(8):724–743\nVazquez Vde L et al (2016) Molecular profiling, including TERT promoter mutations, of acral lentiginous melanomas. 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Cell 144(5):646",{"VOID":1551},"10.1007\u002Fs10585-018-9893-y","2024-06-25T02:52:55.479+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10585-018-9893-y",[1555,1572,1587],{"id":1556,"sortIndex":21,"researcher":20,"roles":1557,"affiliations":1558,"properties":1567,"displayName":1569,"givenName":20,"familyName":20},"226b09d7-afd7-4523-bbd1-d5b3b3d340d1",[247],[1559],{"id":1560,"sortIndex":21,"affiliation":1561,"properties":20},"30e413ab-328d-4b30-8561-6ffc2911e0f6",{"id":1560,"createTime":20,"updateTime":20,"relativeEntities":1562,"slug":20,"properties":1563,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1566,"statistic":20},[],{"title":1564},{"VI":1565},"Department of Dermatology, Yale School of Medicine, New Haven, USA",[],{"title":1568,"gsAuthor":1570},{"VI":1569},"Noel 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"abstract":1699,"title":1701,"gsPaper":1703,"references":1705,"doi":1707},{"EN":1700},"Mena, an actin regulatory protein, functions at the convergence of motility pathways that drive breast cancer cell invasion and migration in vivo. The tumor microenvironment spontaneously induces both increased expression of the Mena invasive (MenaINV) and decreased expression of Mena11a isoforms in invasive and migratory tumor cells. Tumor cells with this Mena expression pattern participate with macrophages in migration and intravasation in mouse mammary tumors in vivo. Consistent with these findings, anatomical sites containing tumor cells with high levels of Mena expression associated with perivascular macrophages were identified in human invasive ductal breast carcinomas and called TMEM. The number of TMEM sites positively correlated with the development of distant metastasis in humans. Here we demonstrate that mouse mammary tumors generated from EGFP-MenaINV expressing tumor cells are significantly less cohesive and have discontinuous cell–cell contacts compared to Mena11a xenografts. Using the mouse PyMT model we show that metastatic mammary tumors express 8.7 fold more total Mena and 7.5 fold more MenaINV mRNA than early non-metastatic ones. Furthermore, MenaINV expression in fine needle aspiration biopsy (FNA) samples of human invasive ductal carcinomas correlate with TMEM score while Mena11a does not. These results suggest that MenaINV is the isoform associated with breast cancer cell discohesion, invasion and intravasation in mice and in humans. They also imply that MenaINV expression and TMEM score measure related aspects of a common tumor cell dissemination mechanism and provide new insight into metastatic risk.",{"EN":1702},"Mena invasive (MenaINV) and Mena11a isoforms play distinct roles in breast cancer cell cohesion and association with TMEM",{"VOID":1704},"[\"9223519236455256429\"]",{"VOID":1706},"Sahai E et al (2005) Simultaneous imaging of GFP, CFP and collagen in tumors in vivo using multiphoton microscopy. BMC Biotechnol 5:14\nCondeelis J, Singer RH, Segall JE (2005) The great escape: when cancer cells hijack the genes for chemotaxis and motility. Annu Rev Cell Dev Biol 21:695–718\nWang W et al (2004) Identification and testing of a gene expression signature of invasive carcinoma cells within primary mammary tumors. Cancer Res 64(23):8585–8594\nHeimann R et al (2000) Separating favorable from unfavorable prognostic markers in breast cancer: the role of E-cadherin. Cancer Res 60(2):298–304\nWeigelt B, Peterse JL, van ‘t Veer LJ (2005) Breast cancer metastasis: markers and models. Nat Rev Cancer 5(8):591–602\nDi Modugno F et al (2007) Molecular cloning of hMena (ENAH) and its splice variant hMena+11a: epidermal growth factor increases their expression and stimulates hMena+11a phosphorylation in breast cancer cell lines. Cancer Res 67(6):2657–2665\nGertler F, Condeelis J (2010) Metastasis: tumor cells becoming MENAcing. Trends Cell Biol 21(2):81–90\nGoswami S et al (2009) Identification of invasion specific splice variants of the cytoskeletal protein Mena present in mammary tumor cells during invasion in vivo. Clin Exp Metastasis 26(2):153–159\nRobinson BD et al (2009) Tumor microenvironment of metastasis in human breast carcinoma: a potential prognostic marker linked to hematogenous dissemination. Clin Cancer Res 15(7):2433–2441\nDi Modugno F et al (2006) The cytoskeleton regulatory protein hMena (ENAH) is overexpressed in human benign breast lesions with high risk of transformation and human epidermal growth factor receptor-2-positive\u002Fhormonal receptor-negative tumors. Clin Cancer Res 12(5):1470–1478\nGurzu S et al (2008) The expression of cytoskeleton regulatory protein Mena in colorectal lesions. Rom J Morphol Embryol 49(3):345–349\nGurzu S et al (2009) The immunohistochemical aspects of protein Mena in cervical lesions. Rom J Morphol Embryol 50(2):213–216\nGertler FB et al (1996) Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics. Cell 87(2):227–239\nBear JE et al (2000) Negative regulation of fibroblast motility by Ena\u002FVASP proteins. Cell 101(7):717–728\nDrees F, Gertler FB (2008) Ena\u002FVASP: proteins at the tip of the nervous system. Curr Opin Neurobiol 18(1):53–59\nNeel NF et al (2009) VASP is a CXCR2-interacting protein that regulates CXCR2-mediated polarization and chemotaxis. J Cell Sci 122(Pt 11):1882–1894\nPhilippar U et al (2008) A Mena invasion isoform potentiates EGF-induced carcinoma cell invasion and metastasis. Dev Cell 15(6):813–828\nUrbanelli L et al (2006) Characterization of human Enah gene. Biochim Biophys Acta 1759(1–2):99–107\nWelch DR, Neri A, Nicolson GL (1983) Comparison of ‘spontaneous’ and ‘experimental’ metastasis using rat 13762 mammary adenocarcinoma metastatic cell clones. Invasion Metastasis 3(2):65–80\nNeri A et al (1982) Development and biologic properties of malignant cell sublines and clones of a spontaneously metastasizing rat mammary adenocarcinoma. J Natl Cancer Inst 68(3):507–517\nRoussos ET, Balsamo M, Alford SK, Wyckoff JB, Gligorijevic B, Wang Y, Pozzuto M, Stobezki R, Goswami S, Segall JE, Lauffenburger DA, Bresnick AR, Gertler FB, Condeelis JS (2011) Mena invasive (MenaINV) promotes multicellular streaming motility and transendothelial migration in a mouse model of breast cancer. J Cell Sci. doi:10.1242\u002FJCS086231\nWyckoff J et al (2004) A paracrine loop between tumor cells and macrophages is required for tumor cell migration in mammary tumors. Cancer Res 64(19):7022–7029\nWang W et al (2002) Single cell behavior in metastatic primary mammary tumors correlated with gene expression patterns revealed by molecular profiling. Cancer Res 62(21):6278–6288\nWyckoff J et al (2010) High resolution multi-photon imaging of tumors in vivo. In: Goldman RD, Swedlow JR, Spector DL (eds) Live cell imaging; a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, pp 441–462\nZipfel WR, Williams RM, Webb WW (2003) Nonlinear magic: multiphoton microscopy in the biosciences. Nat Biotechnol 21(11):1369–1377\nGupta PK, Baloch ZW (2002) Intraoperative and on-site cytopathology consultation: utilization, limitations, and value. Semin Diagn Pathol 19(4):227–236\nMouneimne G et al (2004) Phospholipase C and cofilin are required for carcinoma cell directionality in response to EGF stimulation. J Cell Biol 166(5):697–708\nLoureiro JJ et al (2002) Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena\u002Fvasodilator-stimulated phosphoprotein (VASP) function during cell migration. Mol Biol Cell 13(7):2533–2546\nLebrand C et al (2004) Critical role of Ena\u002FVASP proteins for filopodia formation in neurons and in function downstream of netrin-1. Neuron 42(1):37–49\nPino MS et al (2008) Human Mena+11a isoform serves as a marker of epithelial phenotype and sensitivity to epidermal growth factor receptor inhibition in human pancreatic cancer cell lines. Clin Cancer Res 14(15):4943–4950\nLin EY et al (2003) Progression to malignancy in the polyoma middle T oncoprotein mouse breast cancer model provides a reliable model for human diseases. Am J Pathol 163(5):2113–2126\nSymmans WF et al (2003) Total RNA yield and microarray gene expression profiles from fine-needle aspiration biopsy and core-needle biopsy samples of breast carcinoma. Cancer 97(12):2960–2971\nDi Modugno F et al (2004) Human Mena protein, a serex-defined antigen overexpressed in breast cancer eliciting both humoral and CD8+ T-cell immune response. Int J Cancer 109(6):909–918\nGiampieri S et al (2009) Localized and reversible TGFbeta signalling switches breast cancer cells from cohesive to single cell motility. Nat Cell Biol 11(11):1287–1296\nZeineldin R et al (2006) Mesenchymal transformation in epithelial ovarian tumor cells expressing epidermal growth factor receptor variant III. Mol Carcinog 45(11):851–860\nGuy CT, Cardiff RD, Muller WJ (1992) Induction of mammary tumors by expression of polyomavirus middle T oncogene: a transgenic mouse model for metastatic disease. Mol Cell Biol 12(3):954–961\nLin EY et al (2001) Colony-stimulating factor 1 promotes progression of mammary tumors to malignancy. J Exp Med 193(6):727–740\nWyckoff JB et al (2000) A critical step in metastasis: in vivo analysis of intravasation at the primary tumor. Cancer Res 60(9):2504–2511\nWyckoff JB et al (2007) Direct visualization of macrophage-assisted tumor cell intravasation in mammary tumors. Cancer Res 67(6):2649–2656\nWang W et al (2005) Tumor cells caught in the act of invading: their strategy for enhanced cell motility. Trends Cell Biol 15(3):138–145\nWang W et al (2007) Coordinated regulation of pathways for enhanced cell motility and chemotaxis is conserved in rat and mouse mammary tumors. 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Cancer Research, 42, 1337?1342.",{},{"id":20,"text":2253,"url":20,"identifiers":2254},"Gasic GJ, Gasic TB and Stewart CC, 1968, Antimetastatic effects associated with platelet reduction. Proceedings of the National Academy of Sciences, USA, 61, 46?52.",{"doi":2255},"10.1073\u002Fpnas.61.1.46",{"id":20,"text":2257,"url":20,"identifiers":2258},"Diana HA and John D, 1978, Endotoxin-induced changes in human platelet membranes: morphologic evidence. Blood, 51, 487?495.",{"doi":2259},"10.1182\u002Fblood.V51.3.487.487",{"id":2261,"createTime":2262,"updateTime":2263,"relativeEntities":2264,"slug":2265,"properties":2266,"entityType":236,"verifyStatus":237,"verifyTime":2275,"verifyNote":239,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":2276,"fullTextUrl":20,"authors":2277,"publicationType":374,"publisherRelationship":2375,"citationCount":21,"citationInfo":2431,"publishDate":2434,"publishYear":2432,"citationAnalyzeStatus":1277,"lastCitationAnalyze":2435,"indexDatabases":2436,"openAccess":20,"references":2437,"isForceReanalyzing":434},"47194e54-4d7c-4427-8010-6907885da150","2024-02-09T09:10:48.672+00:00","2026-07-11T06:03:04.308+00:00",[],"CD4-FOXP3-T-regulatory-cells-decrease-and-CD3-CD8-T-cells-recruitment-in-TILs-from-melanoma-metastases-after-electrochemotherapy",{"abstract":2267,"title":2269,"gsPaper":2271,"doi":2273},{"EN":2268},"Electrochemotherapy (ECT) represents an effective local treatment for skin unresectable melanoma metastases with high overall objective response rate. ECT is based on the combination of anti-neoplastic drugs administration and cancer cells electroporation. Whether ECT can also activate the immune system is a matter of debate, however a significant recruitment of dendritic cells in melanoma treated metastases has been described. Herein we investigated immediate and late effects of ECT treatment on T cell subsets in ECT-treated lesions by fluorescent immunohistochemistry. Biopsies from melanoma patients (n = 10) were taken before ECT (t0), at d1 and d14 from treatment. At t0, CD3+CD4+ T cells were the most represented T cells, well detected in the perilesional dermis, particularly at tumour margin, while CD3+CD8+ T cells were less represented. CD4+FOXP3+ T regulatory (Treg) cells were present in the perilesional dermis and within the lesion. ECT induced a significant decrease of CD4+FOXP3+ Treg cells percentage in the perilesional dermis, observed at d1 and at d14 (p \u003C 0.001). CD3+CD8+ T cells frequency significantly increased at d14 from treatment in the perilesional dermis (p \u003C 0.001). Furthermore calreticulin translocation to the plasma membrane, a hallmark of immunogenic cell death, was observed in metastatic cells after ECT. The data reported here confirm that ECT induces a local response, with a lymphoid infiltrate characterized by CD4+FOXP3+ Treg cells decrease and CD3+CD8+ T cells recruitment in the treated lesions. These results might contribute to design novel combinational therapeutic approaches with ECT and immunotherapy in order to generate a systemic long-lasting anti-melanoma immunity.",{"EN":2270},"CD4+FOXP3+ T regulatory cells decrease and CD3+CD8+ T cells recruitment in TILs from melanoma metastases after electrochemotherapy",{"VOID":2272},"11709885191241664321",{"VOID":2274},"10.1007\u002Fs10585-016-9814-x","2024-04-29T01:14:37.070+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10585-016-9814-x",[2278,2293,2306,2321,2334,2347,2362],{"id":2279,"sortIndex":21,"researcher":20,"roles":2280,"affiliations":2281,"properties":2290,"displayName":2292,"givenName":20,"familyName":20},"3d9d67ac-3d5f-4203-b0e5-9242d306e2d3",[247],[2282],{"id":2283,"sortIndex":21,"affiliation":2284,"properties":20},"052c4217-3dae-4c42-b527-7b94900cab5d",{"id":2283,"createTime":20,"updateTime":20,"relativeEntities":2285,"slug":20,"properties":2286,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2289,"statistic":20},[],{"title":2287},{"VI":2288},"Plastic and Reconstructive Surgery Unit - Regional Melanoma Referral Center - Tuscan Tumour Institute (ITT), Santa Maria Annunziata Hospital, Florence, Italy",[],{"title":2291},{"VI":2292},"P. Di Gennaro",{"id":2294,"sortIndex":259,"researcher":20,"roles":2295,"affiliations":2296,"properties":2303,"displayName":2305,"givenName":20,"familyName":20},"70dbf779-3663-47d2-b2f9-4a6a951ee762",[247],[2297],{"id":2283,"sortIndex":21,"affiliation":2298,"properties":20},{"id":2283,"createTime":20,"updateTime":20,"relativeEntities":2299,"slug":20,"properties":2300,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2302,"statistic":20},[],{"title":2301},{"VI":2288},[],{"title":2304},{"VI":2305},"G. 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Eur J Cancer Suppl 4:3–13",{"doi":812},{"id":808,"text":2442,"url":810,"identifiers":2443},"Möller MG, Salwa S, Soden DM, O’Sullivan GC (2009) Electrochemotherapy as an adjunct or alternative to other treatments for unresectable or in-transit melanoma. Expert Rev Anticancer Ther 9:1611–1630",{"doi":812},{"id":808,"text":2445,"url":810,"identifiers":2446},"Cadossi R, Ronchetti M, Cadossi M (2014) Locally enhanced chemotherapy by electroporation: clinical experiences and perspective of use of electrochemotherapy. Future Oncol 10:877–890",{"doi":812},{"id":808,"text":2448,"url":810,"identifiers":2449},"Mir LM (2006) Basis and rationale of the electrochemotherapy. Eur J Cancer Suppl 4:38–44",{"doi":812},{"id":808,"text":2451,"url":810,"identifiers":2452},"Mir LM, Gehl J, Sersa G, Collins CG, Garbay J-R, Billard V, Geertsen PF, Rudolf Z, O’Sullivan GC, Marty M (2006) Standard operating procedures of the electrochemotherapy: instructions for the use of bleomycin or cisplatin administered either systemically or locally and electric pulses delivered by the cliniporator by means of invasive or non-invasive electrodes. Eur J Cancer Suppl 4:14–25",{"doi":812},{"id":2454,"text":2455,"url":2456,"identifiers":2457},"ee685b2d-6633-4425-9069-d4c0b3757fc9","Caracò C, Mozzillo N, Marone U, Simeone E, Benedetto L, Di Monta G, Di Cecilia ML, Botti G, Ascierto PA (2013) Long-lasting response to electrochemotherapy in melanoma patients with cutaneous metastasis. BMC Cancer 13:564–568","https:\u002F\u002Fbmccancer.biomedcentral.com\u002Farticles\u002F10.1186\u002F1471-2407-13-564",{"doi":2458},"10.1186\u002F1471-2407-13-564",{"id":808,"text":2460,"url":810,"identifiers":2461},"Campana LG, Testori A, Mozzillo N, Rossi CR (2014) Treatment of metastatic melanoma with electochemotherapy. J Surg Oncol 109:301–307",{"doi":812},{"id":2463,"text":2464,"url":2465,"identifiers":2466},"a53d0d99-edf2-48d9-aa1f-c4af614dab3a","Queirolo P, Marincola F, Spagnolo F (2014) Electrochemotherapy for the management of melanoma skin metastasis: a review of the literature and possible combinations with immunotherapy. Arch Dermatol Res 306:521–526","http:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs00403-014-1462-x",{"doi":2467},"10.1007\u002Fs00403-014-1462-x",{"id":808,"text":2469,"url":810,"identifiers":2470},"Ricotti F, Giuliodori K, Cataldi I, Campanati A, Ganzetti G, Ricotti G, Offidani A (2014) Electrochemotherapy: an effective local treatment of cutaneous and subcutaneous melanoma metastases. Dermatol Ther 27:148–152",{"doi":812},{"id":808,"text":2472,"url":810,"identifiers":2473},"Mekid H, Tounekti O, Spatz A, Cemazar M, El Kebir FZ, Mir LM (2003) In vivo evolution of tumour cells after the generation of double-strand DNA breaks. Br J Cancer 88:1763–1771",{"doi":812},{"id":808,"text":2475,"url":810,"identifiers":2476},"Roux S, Bernat C, Al-Sakere B, Ghiringhelli F, Opolon P, Carpentier AF, Zitvogel L, Mir LM, Robert C (2008) Tumour destruction using electrochemotherapy followed by CpG oligodeoxynucleotide injection induces distant tumour responses. Cancer Immunol Immunother 57:1291–1300",{"doi":812},{"id":808,"text":2478,"url":810,"identifiers":2479},"Calvet CY, Famin D, André FM, Mir LM (2014) Electrochemotherapy with bleomycin induces hallmarks of immunogenic cell death in murine colon cancer cells. Oncoimmunology 3:e28131",{"doi":812},{"id":808,"text":2481,"url":810,"identifiers":2482},"Kepp O, Senovilla L, Vitale I, Vacchelli E, Adjemian S, Agostinis P, Apetoh L, Aranda F, Barnaba V, Bloy N et al (2014) Consensus guidelines for the detection of immunogenic cell death. Oncoimmunology 3:e955691",{"doi":812},{"id":808,"text":2484,"url":810,"identifiers":2485},"Kroemer G, Galluzzi L, Kepp O, Zitvogel L (2013) Immunogenic cell death in cancer therapy. Annu Rev Immunol 31:51–72",{"doi":812},{"id":2487,"text":2488,"url":2489,"identifiers":2490},"65658dc3-356f-4114-8225-2072beee1ccd","Gerlini G, Sestini S, Di Gennaro P, Urso C, Pimpinelli N, Borgognoni L (2013) Dendritic cells recruitment in melanoma metastasis treated by electrochemotherapy. Clin Exp Metastasis 30:37–45","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs10585-012-9505-1",{"doi":2491},"10.1007\u002Fs10585-012-9505-1",{"id":808,"text":2493,"url":810,"identifiers":2494},"Gerlini G, Di Gennaro P, Borgognoni L (2012) Enhancing antimelanoma immunity by electrochemotherapy and in vivo dendritic-cell activation. Oncoimmunology 1:1655–1657",{"doi":812},{"id":808,"text":2496,"url":810,"identifiers":2497},"Schreiber RD, Old LJ, Smyth MJ (2011) Cancer immunoediting: integrating immunity’s roles in cancer suppression and promotion. 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