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The inhibitory effect of externally applied aminoglycosides on P2X2 receptor currents was examined after heterologous expression in Xenopus laevis oocytes using the two-electrode voltage-clamp technique. All of the aminoglycosides tested inhibited the ATP-evoked responses with potencies ranging from 71 μM to 2 mM (IC50 values). The ranked order of potency was streptomycin > gentamicin > neomycin > paromomycin > kanamycin. The inhibition of P2X receptor currents was independent of the ATP concentration used for the activation, which is compatible with a noncompetitive mechanism. The inhibition was voltage-dependent and was reduced at more positive membrane potentials. To examine whether the current block was dependent on the receptor conformation, the aminoglycoside effect on a non-desensitizing P2X2-X1 receptor chimera was analyzed. The results from these measurements suggest that inhibition is caused by an open pore block that locks the P2X receptor chimera in an open nonconducting state from which the agonist dissociation is slow. We also demonstrate that the P2X2-X1 chimera can serve as a tool to directly test whether an antagonist acts competitively or not.",{"EN":188},"Aminoglycoside block of P2X2 receptors heterologously expressed in Xenopus laevis oocytes",{"VOID":190},"[\"6876926827764029581\"]",{"VOID":192},"Nicke A, Bäumert HG, Rettinger J et al (1998) P2X1 and P2X3 receptors form stable trimers: a novel structural motif of ligand-gated ion channels. EMBO J 17:3016–3028\nAschrafi A, Sadtler S, Niculescu C et al (2004) Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes. J Mol Biol 342:333–343\nJasti J, Furukawa H, Gonzales EB et al (2007) Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH. Nature 449:316–323\nKawate T, Michel JC, Birdsong WT et al (2009) Crystal structure of the ATP-gated P2X4 ion channel in the closed state. Nature 460:592–598\nJarvis MF (2010) The neural–glial purinergic receptor ensemble in chronic pain states. Trends Neurosci 33:48–57\nCao L, Broomhead HE, Young MT et al (2009) Polar residues in the second transmembrane domain of the rat P2X2 receptor that affect spontaneous gating, unitary conductance, and rectification. J Neurosci 29:14257–14264\nKracun S, Chaptal V, Abramson J et al (2010) Gated access to the pore of a P2X receptor: structural implications for closed–open transitions. J Biol Chem 285:10110–10121\nJiang R, Martz A, Gonin S et al (2010) A putative extracellular salt bridge at the subunit interface contributes to the ion channel function of the ATP-gated P2X2 receptor. J Biol Chem 285:15805–15815\nKeceli B, Kubo Y (2009) Functional and structural identification of amino acid residues of the P2X2 receptor channel critical for the voltage- and [ATP]-dependent gating. J Physiol 587:5801–5818\nWildman SS, King BF, Burnstock G (1999) Modulatory activity of extracellular H+ and Zn2+ on ATP-responses at rP2X1 and rP2X3 receptors. Br J Pharmacol 128:486–492\nVirginio C, Church D, North RA et al (1997) Effects of divalent cations, protons and calmidazolium at the rat P2X7 receptor. Neuropharmacology 36:1285–1294\nKhakh BS, Proctor WR, Dunwiddie TV et al (1999) Allosteric control of gating and kinetics at P2X4 receptor channels. J Neurosci 19:7289–7299\nMiller KJ, Michel AD, Chessell IP et al (1998) Cibacron blue allosterically modulates the rat P2X4 receptor. Neuropharmacology 37:1579–1586\nNorth RA (2002) Molecular physiology of P2X receptors. Physiol Rev 82:1013–1067\nSchatz A, Bugie E, Waksman SA (2005) Streptomycin, a substance exhibiting antibiotic activity against gram-positive and gram-negative bacteria. 1944. Clin Orthop Relat Res 437:3–6\nRybak LP, Whitworth CA (2005) Ototoxicity: therapeutic opportunities. Drug Discov Today 10:1313–1321\nSelimoglu E (2007) Aminoglycoside-induced ototoxicity. Curr Pharm Des 13:119–126\nBlanchet C, Erostegui C, Sugasawa M et al (2000) Gentamicin blocks ACh-evoked K+ current in guinea-pig outer hair cells by impairing Ca2+ entry at the cholinergic receptor. J Physiol 525(Pt 3):641–654\nSchacht J (1993) Biochemical basis of aminoglycoside ototoxicity. Otolaryngol Clin North Am 26:845–856\nVital BO, Prado-Franceschi J (1969) The nature of neuromuscular block produced by neomycin and gentamicin. Arch Int Pharmacodyn Thér 179:78–85\nOhmori H (1985) Mechano-electrical transduction currents in isolated vestibular hair cells of the chick. J Physiol 359:189–217\nWinegar BD, Haws CM, Lansman JB (1996) Subconductance block of single mechanosensitive ion channels in skeletal muscle fibers by aminoglycoside antibiotics. J Gen Physiol 107:433–443\nOkamoto T, Sumikawa K (1991) Antibiotics cause changes in the desensitization of ACh receptors expressed in Xenopus oocytes. Brain Res Mol Brain Res 9:165–168\nAmici M, Eusebi F, Miledi R (2005) Effects of the antibiotic gentamicin on nicotinic acetylcholine receptors. Neuropharmacology 49:627–637\nRaisinghani M, Premkumar LS (2005) Block of native and cloned vanilloid receptor 1 (TRPV1) by aminoglycoside antibiotics. Pain 113:123–133\nMasuko T, Kuno T, Kashiwagi K et al (1999) Stimulatory and inhibitory properties of aminoglycoside antibiotics at N-methyl-d-aspartate receptors. J Pharmacol Exp Ther 290:1026–1033\nLin X, Hume RI, Nuttall AL (1993) Voltage-dependent block by neomycin of the ATP-induced whole cell current of guinea-pig outer hair cells. J Neurophysiol 70:1593–1605\nIto K, Dulon D (2010) Purinergic signaling in cochleovestibular hair cells and afferent neurons. Purinergic Signal 6:201–209\nTelang RS, Paramananthasivam V, Vlajkovic SM et al (2010) Reduced P2x(2) receptor-mediated regulation of endocochlear potential in the ageing mouse cochlea. Purinergic Signal 6:263–272\nHousley GD, Greenwood D, Ashmore JF (1992) Localization of cholinergic and purinergic receptors on outer hair cells isolated from the guinea-pig cochlea. Proc Biol Sci 249:265–273\nSzucs A, Szappanos H, Toth A et al (2004) Differential expression of purinergic receptor subtypes in the outer hair cells of the guinea pig. Hear Res 196:2–7\nZhao HB, Yu N, Fleming CR (2005) Gap junctional hemichannel-mediated ATP release and hearing controls in the inner ear. Proc Natl Acad Sci USA 102:18724–18729\nWerner P, Seward EP, Buell GN et al (1996) Domains of P2X receptors involved in desensitization. Proc Natl Acad Sci USA 93:15485–15490\nRettinger J, Schmalzing G (2004) Desensitization masks nanomolar potency of ATP at the P2X1 receptor. J Biol Chem 279:6426–6433\nMiledi R, Parker I, Woodward RM (1989) Membrane currents elicited by divalent cations in Xenopus oocytes. J Physiol 417:173–195\nWeber WM (1999) Endogenous ion channels in oocytes of Xenopus laevis: recent developments. J Membr Biol 170:1–12\nEvans RJ, Lewis C, Buell G et al (1995) Pharmacological characterization of heterologously expressed ATP-gated cation channels (P2x purinoceptors). Mol Pharmacol 48:178–183\nDing S, Sachs F (2000) Inactivation of P2X2 purinoceptors by divalent cations. J Physiol 522:199–214\nRettinger J, Schmalzing G (2003) Activation and desensitization of the recombinant P2X1 receptor at nanomolar ATP concentrations. J Gen Physiol 121:451–461\nInternational Union of Pharmacology, Khakh BS, Burnstock G, Kennedy C et al (2001) XXIV. Current status of the nomenclature and properties of P2X receptors and their subunits. Pharmacol Rev 53:107–118\nRettinger J, Braun K, Hochmann H et al (2005) Profiling at recombinant homomeric and heteromeric rat P2X receptors identifies the suramin analogue NF449 as a highly potent P2X1 receptor antagonist. Neuropharmacology 48:461–468\nGrosman C, Auerbach A (2001) The dissociation of acetylcholine from open nicotinic receptor channels. Proc Natl Acad Sci USA 98:14102–14107\nHausmann R, Rettinger J, Gerevich Z et al (2006) The suramin analog 4, 4′, 4″, 4‴-(carbonylbis(imino-5,1,3-benzenetriylbis (carbonylimino)))tetra-kis-benzenesulfonic acid (NF110) potently blocks P2X3 receptors: subtype selectivity is determined by location of sulfonic acid groups. 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evidence supports the idea that cancer stem cells (CSCs) are those with the capacity to initiate tumors, generate phenotypical diversity, sustain growth, confer drug resistance, and orchestrate the spread of tumor cells. It is still controversial whether CSCs originate from normal stem cells residing in the tissue or cancer cells from the tumor bulk that have dedifferentiated to acquire stem-like characteristics. Although CSCs have been pointed out as key drivers in cancer, knowledge regarding their physiology is still blurry; thus, research focusing on CSCs is essential to designing novel and more effective therapeutics. The purinergic system has emerged as an important autocrine-paracrine messenger system with a prominent role at multiple levels of the tumor microenvironment, where it regulates cellular aspects of the tumors themselves and the stromal and immune systems. Recent findings have shown that purinergic signaling also participates in regulating the CSC phenotype. Here, we discuss updated information regarding CSCs in the purinergic system and present evidence supporting the idea that elements of the purinergic system expressed by this subpopulation of the tumor represent attractive pharmacological targets for proposing innovative anti-cancer therapies.\u003C\u002Fjats:p>",{"EN":321},"Purinergic system in cancer stem cells",{"VOID":323},"[\"16260697181700505115\"]",{"VOID":325},"37966629",{"VOID":327},"10.1007\u002Fs11302-023-09976-5","2024-06-23T09:06:53.848+00:00",[330],"EN","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs11302-023-09976-5",[333,352,373,392,411],{"id":334,"sortIndex":21,"researcher":20,"roles":335,"affiliations":336,"properties":345,"displayName":347,"givenName":20,"familyName":20},"e6f111c8-8911-4790-902e-2f0b54d65f2a",[],[337],{"id":338,"sortIndex":21,"affiliation":339,"properties":20},"77ce6e21-3af4-4a28-bd0c-de6b71903945",{"id":338,"createTime":20,"updateTime":20,"relativeEntities":340,"slug":20,"properties":341,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":344,"statistic":20},[],{"title":342},{"EN":343},"Departamento de Neurobiología Celular y Molecular, Instituto de Neurobiología, Universidad Nacional Autónoma de México (UNAM), Boulevard Juriquilla #3001, Juriquilla Querétaro, Querétaro, CP 76230, México",[],{"title":346,"gsAuthor":348,"openalex":350},{"EN":347},"José David Núñez-Ríos",{"VOID":349},"[\"-lYucEQAAAAJ\"]",{"VOID":351},"A5093268181",{"id":353,"sortIndex":219,"researcher":20,"roles":354,"affiliations":355,"properties":364,"displayName":368,"givenName":20,"familyName":20},"45cdc298-8d8f-4d96-bf86-c9bb4f3e4e4a",[],[356],{"id":357,"sortIndex":21,"affiliation":358,"properties":20},"98d8ff6b-a166-4453-879d-927545bedcbf",{"id":357,"createTime":20,"updateTime":20,"relativeEntities":359,"slug":20,"properties":360,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":363,"statistic":20},[],{"title":361},{"VI":362},"Department of Biochemistry, Chemistry Institute, University of São Paulo (USP), São Paulo, Brazil",[],{"orcid":365,"title":367,"gsAuthor":369,"openalex":371},{"VOID":366},"https:\u002F\u002Forcid.org\u002F0000-0002-2114-3815",{"EN":368},"Henning Ulrich",{"VOID":370},"[\"gA_t84YAAAAJ\"]",{"VOID":372},"A5067506959",{"id":374,"sortIndex":233,"researcher":20,"roles":375,"affiliations":376,"properties":383,"displayName":387,"givenName":20,"familyName":20},"0b582598-6578-4c6a-b78d-a802dedaaccb",[],[377],{"id":338,"sortIndex":21,"affiliation":378,"properties":20},{"id":338,"createTime":20,"updateTime":20,"relativeEntities":379,"slug":20,"properties":380,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":382,"statistic":20},[],{"title":381},{"EN":343},[],{"orcid":384,"title":386,"gsAuthor":388,"openalex":390},{"VOID":385},"https:\u002F\u002Forcid.org\u002F0000-0002-9019-8246",{"EN":387},"Mauricio Dı́az-Muñoz",{"VOID":389},"[\"NrnEqS4AAAAJ\"]",{"VOID":391},"A5003722780",{"id":393,"sortIndex":149,"researcher":20,"roles":394,"affiliations":395,"properties":402,"displayName":406,"givenName":20,"familyName":20},"f5299607-a336-4eaf-bcd7-5f9690498f1b",[],[396],{"id":357,"sortIndex":21,"affiliation":397,"properties":20},{"id":357,"createTime":20,"updateTime":20,"relativeEntities":398,"slug":20,"properties":399,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":401,"statistic":20},[],{"title":400},{"VI":362},[],{"orcid":403,"title":405,"gsAuthor":407,"openalex":409},{"VOID":404},"https:\u002F\u002Forcid.org\u002F0000-0002-6874-5864",{"EN":406},"Claudiana Lameu",{"VOID":408},"[\"iucu_iMAAAAJ\"]",{"VOID":410},"A5071070052",{"id":412,"sortIndex":413,"researcher":20,"roles":414,"affiliations":415,"properties":422,"displayName":426,"givenName":20,"familyName":20},"7e9b1220-3bc3-4c91-b456-c223f90ef9a8",4,[],[416],{"id":338,"sortIndex":21,"affiliation":417,"properties":20},{"id":338,"createTime":20,"updateTime":20,"relativeEntities":418,"slug":20,"properties":419,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":421,"statistic":20},[],{"title":420},{"EN":343},[],{"orcid":423,"title":425,"openalex":427},{"VOID":424},"https:\u002F\u002Forcid.org\u002F0000-0002-8248-332X",{"EN":426},"Francisco G. 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When sperm were pre-incubated in the presence of the K+ channel inhibitor tetra-ethylammonium, the 17βE2 induced plasma membrane hyperpolarization was blunted suggesting the involvement of K+ channels in the hyperpolarizing effects of 17βE2. Extracellular ATP induced a rapid plasma membrane depolarization followed by acrosome reaction. Sperm pre-incubation with 17βE2 inhibited the effects of extracellular ATP on sperm plasma membrane potential variations and acrosome reaction. The effects of 17βE2 were specific since its inactive steroisomer 17αE2 was inactive. 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medial calcification (AMC) has been associated with phenotypic changes in vascular smooth muscle cells (VSMCs) that reportedly makes them more osteoblast-like. Previous work has shown that ATP\u002FUTP can inhibit AMC directly via P2 receptors and indirectly by NPP1-mediated hydrolysis to produce the mineralisation inhibitor, pyrophosphate (PPi). This study investigated the role of P2X receptors in the inhibitory effects of extracellular nucleotides on VSMC calcification. We found that Bz-ATP, α,β-meATP and β,γ-meATP inhibited calcification by up to 100%. Culture in a high-phosphate medium (2 mM) was associated with increased VSMC death and apoptosis; treatment with Bz-ATP, α,β-meATP and β,γ-meATP reduced apoptosis to levels seen in non-calcifying cells. Calcification was also associated with alterations in the protein levels of VSMC (e.g. SM22α and SMA) and osteoblast-associated (e.g. Runx2 and osteopontin) markers; Bz-ATP, α,β-meATP and β,γ-meATP attenuated these changes in protein expression. Long-term culture with Bz-ATP, α,β-meATP and β,γ-meATP resulted in lower extracellular ATP levels and an increased rate of ATP breakdown. P2X receptor antagonists failed to prevent the inhibitory effects of these analogues suggesting that they act via P2X receptor-independent mechanisms. In agreement, the breakdown products of α,β-meATP and β,γ-meATP (α,β-meADP and methylene diphosphonate, respectively) also dose-dependently inhibited VSMC calcification. Furthermore, the actions of Bz-ATP, α,β-meATP and β,γ-meATP were unchanged in VSMCs isolated from NPP1-knockout mice, suggesting that the functional effects of these compounds do not involve NPP1-mediated generation of PPi. Together, these results indicate that the inhibitory effects of ATP analogues on VSMC calcification and apoptosis in vitro may be mediated, at least in part, by mechanisms that are independent of purinergic signalling and PPi.",{"EN":1692},"Inhibition of vascular smooth muscle cell calcification by ATP analogues",{"VOID":1694},"[\"9487030904171936074\"]",{"VOID":1696},"citation_journal_title=Front Endocrinol (Lausanne); citation_title=Mechanisms and clinical consequences of vascular calcification; citation_author=D Zhu, NC Mackenzie, C Farquharson, VE Macrae; citation_volume=3; citation_publication_date=2012; citation_pages=95; citation_doi=10.3389\u002Ffendo.2012.00095; citation_id=CR1\ncitation_journal_title=Circ Res; citation_title=Apoptosis regulates human vascular calcification in vitro: evidence for initiation of vascular calcification by apoptotic bodies; citation_author=D Proudfoot, JN Skepper, L Hegyi, MR Bennett, CM Shanahan; citation_volume=87; 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Plasma membrane expression of P2X4 is regulated by dynamin-dependent endocytosis, and this study identifies a Rab5-dependent pathway of receptor internalisation. Expression of Rab5 constructs altered the distribution of P2X4 in HEK-293 cells, and both constitutive internalisation and agonist-induced desensitisation of P2X4 were increased by co-expression of wild-type Rab5 or constitutively active Rab5 (Q79L). Expression of inactive dynamin K44A and Rab5 S34N constructs abolished agonist-induced desensitisation, suggesting internalisation as the underlying mechanism. Blocking P2X4 internalisation in this way also abolished potentiation of ATP-induced currents by the allosteric modulator ivermectin. This suggests that the dynamin-Rab5 internalisation pathway is essential for the ivermectin potentiation effect. In agreement with this hypothesis, the co-expression of wild-type dynamin, wild-type Rab5 or active Rab5 (Q79L) could increase the potentiation of the ATP-induced P2X4 response by ivermectin. These findings highlight Rab5 GTPase as a key regulator of P2X4 receptor cell surface expression and internalisation.",{"EN":1890},"Rab5 regulates internalisation of P2X4 receptors and potentiation by ivermectin",{"VOID":1892},"North RA (2002) Molecular physiology of P2X receptors. Physiol Rev 82(4):1013–1067\nSurprenant A, North RA (2009) Signaling at purinergic P2X receptors. Annu Rev Physiol 71:333–359\nYamamoto K, Sokabe T, Matsumoto T, Yoshimura K, Shibata M, Ohura N, Fukuda T, Sato T, Sekine K, Kato S, Isshiki M, Fujita T, Kobayashi M, Kawamura K, Masuda H, Kamiya A, Ando J (2006) Impaired flow-dependent control of vascular tone and remodeling in P2X4-deficient mice. Nat Med 12(1):133–137\nSim JA (2006) Altered hippocampal synaptic potentiation in P2X4 knock-out mice. J Neurosci 26(35):9006–9009\nUlmann L, Hatcher J, Hughes J, Chaumont S, Green P, Conquet F, Buell G, Reeve A, Chessell I, Rassendren F (2008) Up-regulation of P2X4 receptors in spinal microglia after peripheral nerve injury mediates BDNF release and neuropathic pain. J Neurosci 28(44):11263–11268\nKhakh BS, Proctor WR, Dunwiddie TV, Labarca C, Lester HA (1999) Allosteric control of gating and kinetics at P2X(4) receptor channels. J Neurosci 19(17):7289–7299\nDawson GR, Wafford KA, Smith AV, Marshall GR, Bayley PJ, Schaeffer JM, Meinke PT, McKernan RM (2000) Anticonvulsant and adverse effects of avermectin analogs in mice are mediated through the gamma-aminobutyric acid(A) receptor. J Pharmacol Exp Ther 295(3):1051–1060\nShan Q (2001) Ivermectin, an unconventional agonist of the glycine receptor chloride channel. J Biol Chem 276(16):12556–12564\nToulmé E, Soto F, Garret M, Boué-Grabot E (2006) Functional properties of internalization-deficient P2X4 receptors reveal a novel mechanism of ligand-gated channel facilitation by ivermectin. Mol Pharmacol 69(2):576–587\nSilberberg S, Li M, Swartz K (2007) Ivermectin interaction with transmembrane helices reveals widespread rearrangements during opening of P2X receptor channels. Neuron 54(2):263–274\nRoyle SJ, Qureshi OS, Bobanović LK, Evans PR, Owen DJ, Murrell-Lagnado RD (2005) Non-canonical YXXGPhi endocytic motifs: recognition by AP2 and preferential utilization in P2X4 receptors. J Cell Sci 118:3073–3080\nRoyle SJ, Murrell-Lagnado RD (2002) Constitutive cycling: a general mechanism to regulate cell surface proteins. Bioessays 25(1):39–46\nStokes L, Surprenant A (2009) Dynamic regulation of the P2X 4receptor in alveolar macrophages by phagocytosis and classical activation. Eur J Immunol 39(4):986–995\nQureshi OS, Paramasivam A, Yu JCH, Murrell-Lagnado RD (2007) Regulation of P2X4 receptors by lysosomal targeting, glycan protection and exocytosis. J Cell Sci 120(21):3838–3849\nSchafer DA (2004) Regulating actin dynamics at membranes: a focus on dynamin. Traffic 5(7):463–469\nZerial M, McBride H (2001) Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2(2):107–117\nBucci C, Parton RG, Mather IH, Stunnenberg H, Simons K, Hoflack B, Zerial M (1992) The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 70(5):715–728\nLakadamyali M, Rust MJ, Zhuang X (2006) Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes. Cell 124(5):997–1009\nDinneen J (2004) Expression of dominant negative rab5 in HeLa cells regulates endocytic trafficking distal from the plasma membrane. Exp Cell Res 294(2):509–522\nHunker CM, Kruk I, Hall J, Giambini H, Veisaga ML, Barbieri MA (2006) Role of Rab5 in insulin receptor-mediated endocytosis and signaling. Arch Biochem Biophys 449(1–2):130–142\nZadeh AD, Xu H, Loewen ME, Noble GP, Steele DF, Fedida D (2008) Internalized Kv1.5 traffics via Rab-dependent pathways. J Physiol 586:4793–4813\nBrown TC, Tran IC, Backos DS, Esteban JA (2005) NMDA receptor-dependent activation of the small GTPase Rab5 drives the removal of synaptic AMPA receptors during hippocampal LTD. Neuron 45(1):81–94\nBobanovic LK, Royle SJ, Murrell-Lagnado RD (2002) P2X receptor trafficking in neurons is subunit specific. J Neurosci 22(12):4814–4824\nFountain SJ, North RA (2006) A C-terminal lysine that controls human P2X4 receptor desensitization. J Biol Chem 281(22):15044–15049\nGold ES, Underhill DM, Morrissette NS, Guo J, McNiven MA, Aderem A (1999) Dynamin 2 is required for phagocytosis in macrophages. J Exp Med 190(12):1849–1856\nKitano M, Nakaya M, Nakamura T, Nagata S, Matsuda M (2008) Imaging of Rab5 activity identifies essential regulators for phagosome maturation. Nature 453(7192):241–245\nHerskovits JS, Burgess CC, Obar RA, Vallee RB (1993) Effects of mutant rat dynamin on endocytosis. J Cell Biol 122(3):565–578\nBowler JW, Bailey RJ, North RA, Surprenant A (2003) P2X4, P2Y1 and P2Y2 receptors on rat alveolar macrophages. Br J Pharmacol 140(3):567–575\nPataki G, Czopf L, Jilling T, Marczin N, Catravas J, Matalon S (1995) Regulation of fluid-phase endocytosis in alveolar macrophages. Am J Physiology 269(4 Pt 1):L520–L526\nUlmann L, Hirbec H, Rassendren F (2010) P2X4 receptors mediate PGE2 release by tissue-resident macrophages and initiate inflammatory pain. EMBO J 29(14):2290–2300\nSoto F, Garcia-Guzman M, Gomez-Hernandez JM, Hollmann M, Karschin C, Stühmer W (1996) P2X4: an ATP-activated ionotropic receptor cloned from rat brain. Proc Natl Acad Sci USA 93(8):3684–3688",{"VOID":1894},"10.1007\u002Fs11302-012-9336-1","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs11302-012-9336-1",[1897],{"id":1898,"sortIndex":21,"researcher":20,"roles":1899,"affiliations":1900,"properties":1918,"displayName":1920,"givenName":20,"familyName":20},"0a731d29-21ef-40ee-b1a3-5e40514bac89",[204],[1901,1909],{"id":1902,"sortIndex":21,"affiliation":1903,"properties":20},"4199f011-6b74-4d97-b5c5-5fa75a6affcb",{"id":1902,"createTime":20,"updateTime":20,"relativeEntities":1904,"slug":20,"properties":1905,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1908,"statistic":20},[],{"title":1906},{"VI":1907},"Department of Biomedical Science, University of Sheffield, Sheffield, UK",[],{"id":1910,"sortIndex":219,"affiliation":1911,"properties":1917},"f01a1749-abfb-4a8d-aab8-b9e7a1823978",{"id":1910,"createTime":20,"updateTime":20,"relativeEntities":1912,"slug":20,"properties":1913,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1916,"statistic":20},[],{"title":1914},{"VI":1915},"Sydney Medical School Nepean, University of Sydney, Penrith, Australia",[],{},{"title":1919},{"VI":1920},"Leanne Stokes",{"url":1895,"publisher":1922,"properties":1972},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":1923,"slug":10,"properties":1924,"entityType":18,"verifyStatus":19,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":21,"subjectFields":1928,"manageAffiliations":1941,"indexDatabases":1952,"url":94,"thumbnailPath":20,"statistic":1967,"gsStatistic":20,"type":173,"analyzePriority":20},[],{"issn":1925,"title":1926,"eissn":1927},{"VOID":13},{"EN":15},{"VOID":17},[1929,1933,1937],{"id":24,"createTime":20,"updateTime":20,"relativeEntities":1930,"label":1931,"description":1932,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":27},{},{"id":30,"createTime":20,"updateTime":20,"relativeEntities":1934,"label":1935,"description":1936,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":33},{},{"id":36,"createTime":20,"updateTime":20,"relativeEntities":1938,"label":1939,"description":1940,"parentId":20,"standard":20,"scholarHubFieldId":20},[],{"EN":39},{},[1942,1947],{"id":43,"createTime":20,"updateTime":20,"relativeEntities":1943,"slug":20,"properties":1944,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1946,"statistic":20},[],{"title":1945},{"EN":47},[],{"id":50,"createTime":20,"updateTime":20,"relativeEntities":1948,"slug":20,"properties":1949,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":1951,"statistic":20},[],{"title":1950},{"EN":54},[56],[1953,1960],{"id":76,"indexDatabase":1954,"url":87,"indexYears":88,"academicFieldIds":1959,"indexDatabaseRanking":93},{"id":78,"createTime":20,"updateTime":20,"relativeEntities":1955,"label":1956,"description":1957,"key":84,"publicationTags":1958,"standard":20},[],{"EN":81,"VI":81},{"EN":81,"VI":83},[86],[90,91,92],{"id":59,"indexDatabase":1961,"url":72,"indexYears":20,"academicFieldIds":1966,"indexDatabaseRanking":20},{"id":61,"createTime":20,"updateTime":20,"relativeEntities":1962,"label":1963,"description":1964,"key":68,"publicationTags":1965,"standard":20},[],{"EN":64,"VI":64},{"EN":66,"VI":67},[70,71],[74],{"impactFactor":21,"impactFactorByYear":1968,"i10Index":109,"i10IndexLast5Year":110,"totalPublication":111,"totalPublicationByYear":1969,"totalCitation":128,"totalCitationByYear":1970,"totalCitationPerPublication":150,"totalCitationPerPublicationByYear":1971,"hindexLast5Year":172,"hindex":172},{"2012":97,"2013":98,"2014":99,"2015":100,"2016":101,"2017":102,"2018":103,"2019":104,"2020":105,"2021":106,"2022":107,"2023":108},{"2004":113,"2005":114,"2006":115,"2007":116,"2008":117,"2009":118,"2010":114,"2011":119,"2012":120,"2013":121,"2014":122,"2015":118,"2016":123,"2017":118,"2018":115,"2019":115,"2020":124,"2021":124,"2022":125,"2023":126,"2024":127},{"2004":117,"2005":130,"2006":131,"2007":132,"2008":133,"2009":134,"2010":135,"2011":136,"2012":137,"2013":138,"2014":139,"2015":140,"2016":141,"2017":142,"2018":143,"2019":144,"2020":145,"2021":146,"2022":147,"2023":148,"2024":149},{"2004":152,"2005":153,"2006":154,"2007":155,"2008":156,"2009":150,"2010":157,"2011":158,"2012":159,"2013":160,"2014":161,"2015":162,"2016":163,"2017":164,"2018":165,"2019":166,"2020":167,"2021":168,"2022":169,"2023":170,"2024":171},{"pages":1973,"volume":1975},{"VOID":1974},"113-121",{"VOID":1976},"9","2012-10-21",2012,[93,70],{"id":1981,"createTime":1982,"updateTime":1983,"relativeEntities":1984,"slug":1985,"properties":1986,"entityType":195,"verifyStatus":196,"verifyTime":1983,"verifyNote":198,"languages":20,"translateLanguages":20,"viewCount":21,"primaryUrl":1995,"fullTextUrl":20,"authors":1996,"publicationType":247,"publisherRelationship":2212,"citationCount":20,"citationInfo":20,"publishDate":2268,"publishYear":2269,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":2270,"openAccess":20,"references":20,"isForceReanalyzing":308},"0f851293-f91b-42f6-bf9b-042af7e71d92","2024-01-10T01:12:23.525+00:00","2025-02-26T16:22:43.045+00:00",[],"Overexpression-of-NTPDase2-in-gliomas-promotes-systemic-inflammation-and-pulmonary-injury",{"abstract":1987,"title":1989,"references":1991,"doi":1993},{"EN":1988},"Gliomas are the most common and devastating type of primary brain tumor. Many non-neoplastic cells, including immune cells, comprise the tumor microenvironment where they create a milieu that appears to dictate cancer development. ATP and the phosphohydrolytic products ADP and adenosine by activating P2 and P1 receptors may participate in these interactions among malignant and immune cells. Purinergic receptor-mediated cell communication is closely regulated by ectonucleotidases, such as by members of the ectonucleoside triphosphate diphosphohydrolase (E-NTPDase) family, which hydrolyze extracellular nucleotides. We have shown that gliomas, unlike astrocytes, exhibit low NTPDase activity. Furthermore, ATP induces glioma cell proliferation and the co-administration of apyrase decreases progression of injected cells in vivo. We have previously shown that NTPDase2 reconstitution dramatically increases tumor growth in vivo. Here we evaluated whether NTPDase2 reconstitution to gliomas modulates systemic inflammatory responses. We observed that NTPDase2 overexpression modulated pro-inflammatory cytokine production and platelet reactivity. Additionally, pathological alterations in the lungs were observed in rats bearing these tumors. Our results suggest that disruption of purinergic signaling via ADP accumulation creates an inflammatory state that may promote tumor spread and dictate clinical progression.",{"EN":1990},"Overexpression of NTPDase2 in gliomas promotes systemic inflammation and pulmonary injury",{"VOID":1992},"Davis FG, McCarthy BJ (2001) Current epidemiological trends and surveillance issues in brain tumors. Expert Rev Anticancer Ther 1:395–401\nMantovani A (2009) Inflaming metastasis. Nature 457:36–37\nWatters JJ, Schartner JM, Badie B (2005) Microglia function in brain tumors. J Neurosci Res 81:447–455\nMantovani A, Allavena P, Sica A, Balkwill F (2008) Cancer-related inflammation. Nature 454:436–444\nBours MJ, Swennen EL, Di Virgilio F, Cronstein BN, Dagnelie PC (2006) Adenosine 5′-triphosphate and adenosine as endogenous signaling molecules in immunity and inflammation. Pharmacol Ther 112(2):358–404\nFerrari D, Stroh C, Schulze-Osthoff K (1999) P2X7\u002FP2Z purinoreceptor-mediated activation of transcription factor NFAT in microglial cells. J Biol Chem 274:13205–13210\nDi Virgilio F (2007) Liaisons dangereuses: P2X7 and the inflammasome. Trends Pharmacol Sci 28:465–472\nSuzuki T, Hide I, Ido K, Kohsaka S, Inoue K, Nakata Y (2004) Production and release of neuroprotective tumor necrosis factor by P2X7 receptor-activated microglia. J Neurosci 24:1–7\nSprague DL, Sowa JM, Elzey BD, Ratliff TL (2007) The role of platelet CD154 in the modulation in adaptive immunity. Immunol Res 39:185–193\nSierko E, Wojtukiewicz MZ (2007) Inhibition of platelet function: does it offer a chance of better cancer progression control? Semin Thromb Hemost 33:712–721\nPinedo HM, Verheul HM, D’Amato RJ, Folkman J (1998) Involvement of platelets in tumour angiogenesis? Lancet 352:1775–1777\nMelani A, De Micheli E, Pinna G, Alfieri A, Corte LD, Pedata F (2003) Adenosine extracellular levels in human brain gliomas: an intraoperative microdialysis study. Neurosci Lett 31(1–2):93–96, 346\nSpychala J (2000) Tumor promoting functions of adenosine. Pharmacol Ther 87:161–173\nOhta A, Gorelik E, Prasad SJ, Ronchese F, Lukashev D, Wong MK, Huang X, Caldwell S, Liu K, Smith P, Chen JF, Jackson EK, Apasov S, Abrams S, Sitkovsky M (2006) A2A adenosine receptor protects tumors from antitumor T cells. Proc Natl Acad Sci U S A 29(35):13132–13137, 103\nRobson SC, Sévigny J, Zimmermann H (2006) The E-NTPDase family of ectonucleotidases: structure function relationship and pathophysiological significance. Purinergic Signal 2:409–430\nKnowles AF (2011) The GDA1_CD39 superfamily: NTPDases with diverse functions. Purinergic Signal 7:21–45\nYegutkin GG (2008) Nucleotide- and nucleoside-converting ectoenzymes: important modulators of purinergic signalling cascade. BBA 1783:673–694\nGrobben B, Anciaux K, Roymans D, Stefan C, Bollen M, Esmans EL, Slegers H (1999) An ecto-nucleotide pyrophosphatase is one of the main enzymes involved in the extracellular metabolism of ATP in rat C6 glioma. J Neurochem 72:826–834\nPellegatti P, Raffaghello L, Bianchi G, Piccardi F, Pistoia V, Di Virgilio F (2008) Increased level of extracellular ATP at tumor sites: in vivo imaging with plasma membrane luciferase. PLoS One 3(7):e2599\nWink MR, Lenz G, Braganhol E, Tamajusuku AS, Schwartsmann G, Sarkis JJ, Battastini AM (2003) Altered extracellular ATP, ADP and AMP catabolism in glioma cell lines. 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FASEB J 15:1963–1970",{"doi":2576},"10.1096\u002Ffj.01-0169com",{"id":2578,"createTime":2579,"updateTime":2580,"relativeEntities":2581,"slug":2582,"properties":2583,"entityType":195,"verifyStatus":196,"verifyTime":2580,"verifyNote":198,"languages":20,"translateLanguages":20,"viewCount":219,"primaryUrl":2592,"fullTextUrl":20,"authors":2593,"publicationType":247,"publisherRelationship":2704,"citationCount":20,"citationInfo":20,"publishDate":2760,"publishYear":2761,"citationAnalyzeStatus":19,"lastCitationAnalyze":20,"indexDatabases":2762,"openAccess":20,"references":20,"isForceReanalyzing":308},"1fe08ce1-052d-4ee1-b506-71f9b2513c8d","2024-02-16T15:35:13.575+00:00","2025-02-26T15:37:47.830+00:00",[],"Fetal-bovine-serum-contains-biologically-available-ATP",{"abstract":2584,"title":2586,"references":2588,"doi":2590},{"EN":2585},"ATP is a ubiquitous extracellular messenger released in a wide number of pathophysiological conditions. ATP is known to be present in minute amounts in the extracellular space in healthy tissues and in the blood, and to modulate a multiplicity of cell responses. Cell culture systems are widely used to explore purinergic signaling. We show here that currently used fetal bovine sera contain ATP in the 300–1300 pmol\u002FL range. Serum ATP is associated with albumin as well as with microparticle\u002Fmicrovesicle fraction. Serum microparticles\u002Fmicrovesicles affect in vitro cell responses due to their content of miRNAs, growth factors, and other bioactive molecules. ATP is likely to be one of these bioactive factors found in a variable amount in sera of different commercial sources. ATP in serum supports ATP-dependent biochemical reactions such as the hexokinase-dependent phosphorylation of glucose to glucose 6-phosphate, and affects purinergic signaling. These findings show that cells growing in vitro in serum-supplemented media are exposed to varying levels of extracellular ATP, and thus to varying degrees of purinergic stimulation.\n",{"EN":2587},"Fetal bovine serum contains biologically available ATP",{"VOID":2589},"Jochems CE, van der Valk JB, Stafleu FR, Baumans V (2002) The use of fetal bovine serum: ethical or scientific problem? Altern Lab Anim 30(2):219–227. https:\u002F\u002Fdoi.org\u002F10.1177\u002F026119290203000208\nNeubert E, Senger-Sander SN, Manzke VS, Busse J, Polo E, Scheidmann SEF, Schon MP, Kruss S, Erpenbeck L (2019) Serum and serum albumin inhibit in vitro formation of neutrophil extracellular traps (NETs). Front Immunol 10:12. https:\u002F\u002Fdoi.org\u002F10.3389\u002Ffimmu.2019.00012\nBernardini C, Algieri C, Mantia D, Zannoni A, Salaroli R, Trombetti F, Forni M, Pagliarani A, Nesci S (2021) Relationship between serum concentration, functional parameters and cell bioenergetics in IPEC-J2 cell line. Histochem Cell Biol 156(1):59–67. https:\u002F\u002Fdoi.org\u002F10.1007\u002Fs00418-021-01981-2\nLehrich BM, Liang Y, Fiandaca MS (2021) Foetal bovine serum influence on in vitro extracellular vesicle analyses. J Extracell Vesicles 10(3):e12061. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fjev2.12061\nThery C, Witwer KW, Aikawa E, Alcaraz MJ, Anderson JD, Andriantsitohaina R et al (2018) Minimal information for studies of extracellular vesicles 2018 (MISEV2018): a position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines. J Extracell Vesicles 7(1):1535750. https:\u002F\u002Fdoi.org\u002F10.1080\u002F20013078.2018.1535750\nAswad H, Jalabert A, Rome S (2016) Depleting extracellular vesicles from fetal bovine serum alters proliferation and differentiation of skeletal muscle cells in vitro. BMC Biotechnol 16:32. https:\u002F\u002Fdoi.org\u002F10.1186\u002Fs12896-016-0262-0\nOchieng J, Pratap S, Khatua AK, Sakwe AM (2009) Anchorage-independent growth of breast carcinoma cells is mediated by serum exosomes. Exp Cell Res 315(11):1875–1888. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.yexcr.2009.03.010\nShelke GV, Lasser C, Gho YS, Lotvall J (2014) Importance of exosome depletion protocols to eliminate functional and RNA-containing extracellular vesicles from fetal bovine serum. J Extracell Vesicles 3:24783. https:\u002F\u002Fdoi.org\u002F10.3402\u002Fjev.v3.24783\nZhou Q, Xie F, Zhou B, Li C, Kang Y, Wu B, Li L, Dai R (2020) Fetal bovine serum-derived exosomes regulate the adipogenic differentiation of human bone marrow mesenchymal stromal cells in a cross-species manner. Differentiation 115:11–21. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.diff.2020.06.004\nVultaggio-Poma V, Falzoni S, Chiozzi P, Sarti AC, Adinolfi E, Giuliani AL, Sanchez-Melgar A, Boldrini P, Zanoni M, Tesei A, Pinton P, Di Virgilio F (2022) Extracellular ATP is increased by release of ATP-loaded microparticles triggered by nutrient deprivation. Theranostics 12(2):859–874. https:\u002F\u002Fdoi.org\u002F10.7150\u002Fthno.66274\nBauer M, Baumann J, Trommer WE (1992) ATP binding to bovine serum albumin. FEBS Lett 313(3):288–290. https:\u002F\u002Fdoi.org\u002F10.1016\u002F0014-5793(92)81211-4\nTakeda S, Miyauchi S, Nakayama H, Kamo N (1997) Adenosine 5′-triphosphate binding to bovine serum albumin. Biophys Chem 69(2–3):175–183. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fs0301-4622(97)00084-7\nMichel AD, Xing M, Humphrey PP (2001) Serum constituents can affect 2′-& 3′-O-(4-benzoylbenzoyl)-ATP potency at P2X(7) receptors. Br J Pharmacol 132(7):1501–1508. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fsj.bjp.0703968\nGaevskaia VA, Azhitskii G (1978) [Isoelectric fractions of healthy human serum albumin and their ability to bind bilirubin]. Ukr Biokhim Zh 50(6):735–738\nBurnstock G (2018) Purine and purinergic receptors. Brain Neurosci Adv 2:2398212818817494. https:\u002F\u002Fdoi.org\u002F10.1177\u002F2398212818817494\nGiuliani AL, Sarti AC, Di Virgilio F (2019) Extracellular nucleotides and nucleosides as signalling molecules. Immunol Lett 205:16–24. https:\u002F\u002Fdoi.org\u002F10.1016\u002Fj.imlet.2018.11.006\nAbbracchio MP, Burnstock G, Boeynaems JM, Barnard EA, Boyer JL, Kennedy C, Knight GE, Fumagalli M, Gachet C, Jacobson KA, Weisman GA (2006) International Union of Pharmacology LVIII: update on the P2Y G protein-coupled nucleotide receptors: from molecular mechanisms and pathophysiology to therapy. Pharmacol Rev 58(3):281–341. https:\u002F\u002Fdoi.org\u002F10.1124\u002Fpr.58.3.3\nIlles P, Muller CE, Jacobson KA, Grutter T, Nicke A, Fountain SJ, Kennedy C, Schmalzing G, Jarvis MF, Stojilkovic SS, King BF, Di Virgilio F (2021) Update of P2X receptor properties and their pharmacology: IUPHAR Review 30. Br J Pharmacol 178(3):489–514. https:\u002F\u002Fdoi.org\u002F10.1111\u002Fbph.15299\nvan der Pol E, Boing AN, Harrison P, Sturk A, Nieuwland R (2012) Classification, functions, and clinical relevance of extracellular vesicles. Pharmacol Rev 64(3):676–705. https:\u002F\u002Fdoi.org\u002F10.1124\u002Fpr.112.005983",{"VOID":2591},"10.1007\u002Fs11302-023-09941-2","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs11302-023-09941-2",[2594,2609,2622,2635,2648,2661,2676,2691],{"id":2595,"sortIndex":21,"researcher":20,"roles":2596,"affiliations":2597,"properties":2606,"displayName":2608,"givenName":20,"familyName":20},"36a4a9fc-1ec5-4c3a-8b3b-ef854e7e852c",[204],[2598],{"id":2599,"sortIndex":21,"affiliation":2600,"properties":20},"1eb76c1b-2a17-4234-a68d-f41cad297325",{"id":2599,"createTime":20,"updateTime":20,"relativeEntities":2601,"slug":20,"properties":2602,"entityType":20,"verifyStatus":20,"verifyTime":20,"verifyNote":20,"languages":20,"translateLanguages":20,"viewCount":20,"url":20,"parentIds":2605,"statistic":20},[],{"title":2603},{"VI":2604},"Department of Medical Sciences, University of Ferrara, Ferrara, Italy",[],{"title":2607},{"VI":2608},"Valentina 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