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XB-ART-16089
FEBS Lett 1997 Aug 18;4132:323-6.
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Role of protein kinase C and carboxyl-terminal region in acute desensitization of vasopressin V1a receptor.

Ancellin N , Preisser L , Corman B , Morel A .


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The role of protein kinase C activation and carboxyl-terminal region in rapid desensitization of the vasopressin V1a receptor was investigated in Xenopus oocytes. Preincubation of the oocytes with vasopressin or with the diacylglycerol analog 1-oleoyl-2-acetyl-sn-glycerol (OAG), or direct injection of active protein kinase C, all blunted the calcium response of the V1a receptor. Truncation of the 51 terminal amino acids (S374STOP) modified neither the intracellular calcium response to vasopressin nor its desensitization by vasopressin or OAG. These data suggest that desensitization of the V1a receptor is mediated by PKC activation and that its carboxyl-terminal domain is not required for signal transduction and rapid desensitization.

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Species referenced: Xenopus laevis
Genes referenced: atp6v1a avp