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Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/54937
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dc.contributor.authorGomis, Ana-
dc.contributor.authorQuirce, Susana-
dc.contributor.authorViana, Félix-
dc.contributor.authorBelmonte, Carlos-
dc.contributor.authorPlanells-Cases, Rosa-
dc.date.accessioned2012-08-22T12:11:15Z-
dc.date.available2012-08-22T12:11:15Z-
dc.date.issued2011-05-
dc.identifier.citationFASEB Journal - Federation of American Societies for Experimental Biology 25(5): 1628-1640 (2011)es_ES
dc.identifier.issn0892-6638-
dc.identifier.urihttp://hdl.handle.net/10261/54937-
dc.descriptionAna Gomis, [et al.]. 13 p., 7 figures, 1 table and referenceses_ES
dc.description.abstractThe transient receptor potential vanilloid 1 (TRPV1) channel is a thermosensory receptor implicated in diverse physiological and pathological processes. The TRP domain, a highly conserved region in the C terminus adjacent to the internal channel gate, is critical for subunit tetramerization and channel gating. Here, we show that cell-penetrating, membrane-anchored peptides patterned after this protein domain are moderate and selective TRPV1 antagonists both in vitro and in vivo, blocking receptor activity in intact rat primary sensory neurons and their peripheral axons with mean decline time of 30 min. The most potent lipopeptide, TRP-p5, blocked all modes of TRPV1 gating with micromolar efficacy (IC 50<10 μM), without significantly affecting other thermoTRP channels. In contrast, its retrosequence or the corresponding sequences of other TRPV channels did not alter TRPV1 channel activity (IC 50>100 μM). TRP-p5 did not affect the capsaicin sensitivity of the vanilloid receptor. Our data suggest that TRP-p5 interferes with protein-protein interactions at the level of the TRP domain that are essential for the "conformational" change that leads to gate opening. Therefore, these palmitoylated peptides, which we termed TRPducins, are noncompetitive, voltage-independent, sequence-specific TRPV1 blockers. Our findings indicate that TRPducin-like peptides may embody a novel molecular strategy that can be exploited to generate a selective pharmacological arsenal for the TRP superfamily of ion channels.es_ES
dc.description.sponsorshipThis work was supported by Spain Ministry of Science and Innovation grants BFU2009-08346 to A.F.-M., BFU2008-0062 to J.M.G.R., SAF2007-63193 to R.P.-C., BFU2009- 07835 to A.G., BFU2007-61855 to F.V., and BFU2008-04425 to C.B.; Consolider-Ingenio 2010 CSD2008-00005 to A.F.-M., J.M.G.-R., and R.P.-C., and CSD2007-00002 to A.G., F.V., and C.B.; la Generalitat Valenciana Prometeo/2010/046 to A.F.-M., F.V., and C.B.; and Intramural (Consejo Superior de Investigaciones Cientificas) Ref. 2009-20I098 to A.G.es_ES
dc.language.isoenges_ES
dc.publisherFederation of American Societies for Experimental Biologyes_ES
dc.rightsclosedAccesses_ES
dc.subjectPaines_ES
dc.subjectIonotropic receptorses_ES
dc.subjectPepducines_ES
dc.subjectAnalgesiaes_ES
dc.subjectInflammationes_ES
dc.titleMembrane-tethered peptides patterned after the TRP domain (TRPducins) selectively inhibit TRPV1 channel activityes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1096/fj.10-174433-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1096/fj.10-174433es_ES
dc.identifier.e-issn1530-6860-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.grantfulltextnone-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.languageiso639-1en-
item.fulltextNo Fulltext-
item.openairetypeartículo-
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