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dc.creatorChaudhuri, Pinaki-
dc.creatorRosenbaum, Michael A.-
dc.creatorBirnbaumer, Lutz-
dc.creatorGraham, Linda M.-
dc.date2018-06-15T17:30:41Z-
dc.date2018-06-15T17:30:41Z-
dc.date2017-11-
dc.date2018-06-13T15:10:49Z-
dc.date.accessioned2019-04-29T15:54:27Z-
dc.date.available2019-04-29T15:54:27Z-
dc.identifierChaudhuri, Pinaki; Rosenbaum, Michael A.; Birnbaumer, Lutz; Graham, Linda M.; Integration of TRPC6 and NADPH oxidase activation in lysophosphatidylcholine-induced TRPC5 externalization; American Physiological Society; American Journal of Physiology-cell Physiology; 313; 5; 11-2017; 541-555-
dc.identifier0363-6143-
dc.identifierhttp://hdl.handle.net/11336/48812-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/305154-
dc.descriptionLipid oxidation products, including lysophosphatidylcholine (lysoPC), activate canonical transient receptor potential 6 (TRPC6) channels, and the subsequent increase in intracellular Ca2+ leads to TRPC5 activation. The goal of this study is to elucidate the steps in the pathway between TRPC6 activation and TRPC5 externalization. Following TRPC6 activation by lysoPC, extracellular regulated kinase (ERK) is phosphorylated. This leads to phosphorylation of p47phox and subsequent NADPH oxidase activation with increased production of reactive oxygen species. ERK activation requires TRPC6 opening and influx of Ca2+ as evidenced by the failure of lysoPC to induce ERK phosphorylation in TRPC6−/− endothelial cells. ERK siRNA blocks the lysoPC-induced activation of NADPH oxidase, demonstrating that ERK activation is upstream of NADPH oxidase. The reactive oxygen species produced by NADPH oxidase promote myosin light chain kinase (MLCK) activation with phosphorylation of MLC and TRPC5 externalization. Downregulation of ERK, NADPH oxidase, or MLCK with the relevant siRNA prevents TRPC5 externalization. Blocking MLCK activation prevents the prolonged rise in intracellular calcium levels and preserves endothelial migration in the presence of lysoPC.-
dc.descriptionFil: Chaudhuri, Pinaki. Cleveland Clinic; Estados Unidos-
dc.descriptionFil: Rosenbaum, Michael A.. Cleveland Clinic; Estados Unidos. Louis Stokes Cleveland Veterans Affairs Medical Center; Estados Unidos-
dc.descriptionFil: Birnbaumer, Lutz. Pontificia Universidad Católica Argentina "Santa María de los Buenos Aires". Instituto de Investigaciones Biomédicas. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones Biomédicas; Argentina. Research Triangle Park; Estados Unidos. Cleveland Clinic; Estados Unidos-
dc.descriptionFil: Graham, Linda M.. Cleveland Clinic; Estados Unidos-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherAmerican Physiological Society-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.physiology.org/doi/10.1152/ajpcell.00028.2017-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1152/ajpcell.00028.2017-
dc.rightsinfo:eu-repo/semantics/restrictedAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectTRPC6-
dc.subjectTRPC5-
dc.subjectNADPH-
dc.subjectOtras Ciencias Biológicas-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleIntegration of TRPC6 and NADPH oxidase activation in lysophosphatidylcholine-induced TRPC5 externalization-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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