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ANP stimulates phospholipase C in cultured RIMCT cells: roles of protein kinases and G protein

ANP stimulates phospholipase C in cultured RIMCT cells: roles of protein kinases and G protein RIMCT cells: BERL, JULIE MANSOUR, AND ISAAC TEITELBAUM of Medicine, University of Colorado School of Medicine; Denver, Colorado 80262 BERL, TOMAS, JULIE MANSOUR, AND ISAAC TEITELBAUM. ANP stimulatesphospholipase in cultured RIMCT cells:roles C of protein kinasesand G protein. Am. J. Physiol. 260 (Renal Fluid Electrolyte Physiol. 29): F590-F595, 1991.-We examined the possibility that, in addition to stimulation of guanylate cyclase (GC), atria1 natriuretic peptide (ANP) also activates phospholipase (PLC) in cultured rat inner medullary collectC ing tubule (RIMCT) cells. ANP (10-l’ M) causesmarked release of inositol trisphosphate (IPa) at a concentration that doesnot stimulate GC. Concentrations of ANP that stimulate GC (rlO-10 M) result in attenuated IP3 release. Similarly, exogenous dibutyryl guanosine 3’,5’-cyclic monophosphate (10B6M) markedly inhibits the responseto 10-l' M ANP. Inhibition of cyclic nucleotide-dependentprotein kinase by H 8, but not inhibition of protein kinase C by H 7, restoresthe responseto 10m8 and 10B6M ANP. Therefore, activation of cyclic nucleotide-dependentprotein kinase inhibits ANP-stimulated PLC activity. Activation of protein kinase C by phorbol 12-my&ate-13.acetate (PMA) decreases ANP-stimulated IPs production. Pretreatment with H 7, but not H 8, prevents inhibition by PMA. To explore a potential role for G proteins, we examined the effect of guanine nucleotide analogueson ANP-stimulated http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Renal Physiology The American Physiological Society

ANP stimulates phospholipase C in cultured RIMCT cells: roles of protein kinases and G protein

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Publisher
The American Physiological Society
Copyright
Copyright © 1991 the American Physiological Society
ISSN
0363-6127
eISSN
1522-1466
Publisher site
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Abstract

RIMCT cells: BERL, JULIE MANSOUR, AND ISAAC TEITELBAUM of Medicine, University of Colorado School of Medicine; Denver, Colorado 80262 BERL, TOMAS, JULIE MANSOUR, AND ISAAC TEITELBAUM. ANP stimulatesphospholipase in cultured RIMCT cells:roles C of protein kinasesand G protein. Am. J. Physiol. 260 (Renal Fluid Electrolyte Physiol. 29): F590-F595, 1991.-We examined the possibility that, in addition to stimulation of guanylate cyclase (GC), atria1 natriuretic peptide (ANP) also activates phospholipase (PLC) in cultured rat inner medullary collectC ing tubule (RIMCT) cells. ANP (10-l’ M) causesmarked release of inositol trisphosphate (IPa) at a concentration that doesnot stimulate GC. Concentrations of ANP that stimulate GC (rlO-10 M) result in attenuated IP3 release. Similarly, exogenous dibutyryl guanosine 3’,5’-cyclic monophosphate (10B6M) markedly inhibits the responseto 10-l' M ANP. Inhibition of cyclic nucleotide-dependentprotein kinase by H 8, but not inhibition of protein kinase C by H 7, restoresthe responseto 10m8 and 10B6M ANP. Therefore, activation of cyclic nucleotide-dependentprotein kinase inhibits ANP-stimulated PLC activity. Activation of protein kinase C by phorbol 12-my&ate-13.acetate (PMA) decreases ANP-stimulated IPs production. Pretreatment with H 7, but not H 8, prevents inhibition by PMA. To explore a potential role for G proteins, we examined the effect of guanine nucleotide analogueson ANP-stimulated

Journal

AJP - Renal Physiology – The American Physiological Society

Published: Apr 1, 1991

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