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Involvement of calmodulin and myosin light chain kinase in activation of mTRPC5 expressed in HEK cells

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dc.contributor.authorKim, Min Tae-
dc.contributor.authorKim, Byung Joo-
dc.contributor.authorLee, Jae Hwa-
dc.contributor.authorKwon, Seong Chun-
dc.contributor.authorYeon, Dong Soo-
dc.contributor.authorYang, Dong Ki-
dc.contributor.authorSo, Insuk-
dc.contributor.authorKim, Ki Whan-
dc.date.accessioned2010-01-04-
dc.date.available2010-01-04-
dc.date.issued2006-
dc.identifier.citationAm J Physiol Cell Physiol 290: C1031-C1040en
dc.identifier.issn0363-6143 (Print)-
dc.identifier.issn1522-1563 (Online)-
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16306123-
dc.identifier.urihttp://hdl.handle.net/10371/24796-
dc.description.abstractThe classic type of transient receptor potential channel (TRPC) is a molecular candidate for Ca(2+)-permeable cation channels in mammalian cells. Because TRPC channels have calmodulin (CaM) binding sites at their COOH termini, we investigated the effect of CaM on mTRPC5. TRPC5 was initially activated by muscarinic stimulation with 50 microM carbachol and then decayed rapidly even in the presence of carbachol. Intracellular CaM (150 microg/ml) increased the amplitude of mTRPC5 current activated by muscarinic stimulation. CaM antagonists (W-7 and calmidazolium) inhibited mTRPC5 currents when they were applied during the activation of mTRPC5. Pretreatment of W-7 and calmidazolium also inhibited the activation of mTRPC5 current. Inhibitors of myosin light chain kinase (MLCK) inhibited the activation of mTRPC5 currents, whereas inhibitors of CaM-dependent protein kinase II did not. Small interfering RNA against cardiac type MLCK also inhibited the activation of mTRPC5 currents. However, inhibitors of CaM or MLCK did not show any effect on GTPgammaS-induced currents. Application of both Rho kinase inhibitor and MLCK inhibitor inhibited GTPgammaS-induced currents. We conclude that CaM and MLCK modulates the activation process of mTRPC5.en
dc.language.isoenen
dc.publisherAmerican Physiological Societyen
dc.subjectAnimalsen
dc.subjectCalmodulin/genetics/*metabolismen
dc.subjectCarbachol/metabolismen
dc.subjectCell Lineen
dc.subjectCholinergic Agonists/metabolismen
dc.subjectEnzyme Inhibitors/metabolismen
dc.subjectGuanosine 5'-O-(3-Thiotriphosphate)/metabolismen
dc.subjectHumansen
dc.subjectKidney/cytology/embryologyen
dc.subjectMiceen
dc.subjectMyosin-Light-Chain Kinase/genetics/*metabolismen
dc.subjectPatch-Clamp Techniquesen
dc.subjectRNA, Small Interfering/genetics/metabolismen
dc.subjectTRPC Cation Channels/genetics/*metabolismen
dc.titleInvolvement of calmodulin and myosin light chain kinase in activation of mTRPC5 expressed in HEK cellsen
dc.typeArticleen
dc.contributor.AlternativeAuthor김민태-
dc.contributor.AlternativeAuthor김병주-
dc.contributor.AlternativeAuthor이재화-
dc.contributor.AlternativeAuthor권성춘-
dc.contributor.AlternativeAuthor연동수-
dc.contributor.AlternativeAuthor양동기-
dc.contributor.AlternativeAuthor서인석-
dc.contributor.AlternativeAuthor김기환-
dc.identifier.doi10.1152/ajpcell.00602.2004-
Appears in Collections:
College of Medicine/School of Medicine (의과대학/대학원)Dept. of Physiology (생리학교실)Journal Papers (저널논문_생리학교실)
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