| pubmed-article:15069188 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15069188 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:15069188 | lifeskim:mentions | umls-concept:C1425224 | lld:lifeskim |
| pubmed-article:15069188 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15069188 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:15069188 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15069188 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:15069188 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:15069188 | lifeskim:mentions | umls-concept:C0205227 | lld:lifeskim |
| pubmed-article:15069188 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:15069188 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:15069188 | pubmed:dateCreated | 2004-4-21 | lld:pubmed |
| pubmed-article:15069188 | pubmed:abstractText | TRPM7 is a ubiquitously expressed and constitutively active divalent cation-selective ion channel, whose basal activity is regulated by intracellular levels of Mg(2+) and Mg.ATP. We have investigated receptor-mediated mechanisms that may actively regulate TRPM7 activity. We here report that TRPM7 currents are suppressed by intracellular GTPgammaS, suggesting the involvement of heterotrimeric G proteins. TRPM7 currents are also inhibited by stimulating endogenous muscarinic receptors, which is mediated by G(i) because the inhibitory effect is blunted by pertussis toxin. Conversely, stimulation of endogenous G(s)-coupled beta-adrenergic receptors potentiates TRPM7 currents, whereas G(q)-coupled thrombin receptors have little effect. Consistent with the involvement of G(s)/G(i) in controlling adenylyl cyclase activity, elevations of intracellular cAMP levels enhance TRPM7 activity and prevent receptor-mediated modulation of TRPM7 activity by muscarinic and adrenergic agonists. This cAMP-dependent effect requires the functional integrity of both protein kinase A (PKA) and the endogenous kinase domain of TRPM7 because cAMP-mediated effects are abolished when treating cells with the PKA inhibitors H89 or KT5720 as well as in cells expressing phosphotransferase-deficient TRPM7 constructs. These mutant channels are also much less susceptible to GTPgammaS-mediated inhibition, suggesting that the main regulatory effect occurs through G(i)- and G(s)-mediated changes in cAMP. Taken together, our results demonstrate that TRPM7 activity is up- and down-regulated through its endogenous kinase in a cAMP- and PKA-dependent manner. | lld:pubmed |
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| pubmed-article:15069188 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15069188 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15069188 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15069188 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15069188 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:15069188 | pubmed:author | pubmed-author:ScharenbergAn... | lld:pubmed |
| pubmed-article:15069188 | pubmed:author | pubmed-author:PennerReinhol... | lld:pubmed |
| pubmed-article:15069188 | pubmed:author | pubmed-author:FleigAndreaA | lld:pubmed |
| pubmed-article:15069188 | pubmed:author | pubmed-author:TakezawaRyuic... | lld:pubmed |
| pubmed-article:15069188 | pubmed:author | pubmed-author:SchmitzCarste... | lld:pubmed |
| pubmed-article:15069188 | pubmed:author | pubmed-author:DemeusePhilip... | lld:pubmed |
| pubmed-article:15069188 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15069188 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:15069188 | pubmed:volume | 101 | lld:pubmed |
| pubmed-article:15069188 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15069188 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15069188 | pubmed:pagination | 6009-14 | lld:pubmed |
| pubmed-article:15069188 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15069188 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15069188 | pubmed:articleTitle | Receptor-mediated regulation of the TRPM7 channel through its endogenous protein kinase domain. | lld:pubmed |
| pubmed-article:15069188 | pubmed:affiliation | Laboratory of Cell and Molecular Signaling, Center for Biomedical Research, The Queen's Medical Center and John A. Burns School of Medicine, University of Hawaii, Honolulu, HI 96813, USA. | lld:pubmed |
| pubmed-article:15069188 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15069188 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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