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- W1932854671 abstract "It is generally believed that cAMP-dependent phosphorylation is the principle mechanism for activating cystic fibrosis transmembrane conductance regulator (CFTR) Cl − channels. However, we showed that activating G proteins in the sweat duct stimulated CFTR Cl − conductance ( G Cl ) in the presence of ATP alone without cAMP. The objective of this study was to test whether the G protein stimulation of CFTR G Cl is independent of protein kinase A. We activated G proteins and monitored CFTR G Cl in basolaterally permeabilized sweat duct. Activating G proteins with guanosine 5′- O-(3-thiotriphosphate) (10–100 μM) stimulated CFTR G Cl in the presence of 5 mM ATP alone without cAMP. G protein activation of CFTR G Cl required Mg 2+ and ATP hydrolysis (5′-adenylylimidodiphosphate could not substitute for ATP). G protein activation of CFTR G Cl was 1) sensitive to inhibition by the kinase inhibitor staurosporine (1 μM), indicating that the activation process requires phosphorylation; 2) insensitive to the adenylate cyclase (AC) inhibitors 2′,5′-dideoxyadenosine (1 mM) and SQ-22536 (100 μM); and 3) independent of Ca 2+ , suggesting that Ca 2+ -dependent protein kinase C and Ca 2+ /calmodulin-dependent kinase(s) are not involved in the activation process. Activating AC with 10 −6 M forskolin plus 10 −6 M IBMX (in the presence of 5 mM ATP) did not activate CFTR, indicating that cAMP cannot accumulate sufficiently to activate CFTR in permeabilized cells. We concluded that heterotrimeric G proteins activate CFTR G Cl endogenously via a cAMP-independent pathway in this native absorptive epithelium." @default.
- W1932854671 created "2016-06-24" @default.
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- W1932854671 date "2001-03-01" @default.
- W1932854671 modified "2023-09-25" @default.
- W1932854671 title "cAMP-independent phosphorylation activation of CFTR by G proteins in native human sweat duct" @default.
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- W1932854671 doi "https://doi.org/10.1152/ajpcell.2001.280.3.c604" @default.
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