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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Scharenberg, Andrew M. Penner, Reinhold Takezawa, Ryuichi Schmitz, Carsten Fleig, Andrea Demeuse, Philippe |
| Description | Author Affiliation: Takezawa R ( 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.); |
| Abstract | 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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 16 |
| Volume Number | 101 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2004-04-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Ion Channels Physiology Membrane Proteins Protein Kinases Metabolism Receptors, Cell Surface Calcium Cell Line Cyclic AMP GTP-Binding Proteins Patch-Clamp Techniques Pertussis Toxin Pharmacology Protein-Serine-Threonine Kinases TRPM Cation Channels Type C Phospholipases Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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