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Endothelin-stimulated phosphoinositide turnover and protein kinase C translocation in rat synaptosomes
R E Catalan1, A M Martinez, M D Aragones
1Departamento de Biologia Molecular, Centro de Biologia Molecular, Universidad Autonoma de Madrid, Spain.
Biochemistry and Molecular Biology International
|February 1, 1996
Abstract:
The action of endothelin-1 (ET-1) on phosphoinositide metabolism was studied in rat synaptosomes. ET-1 caused an early and transitory decrease of 32P incorporation into phosphoinositides, concomitantly with an increase into phosphatidic acid (PA). This effect was time-dependent and was not found in the absence of exogenous calcium. Furthermore, ET-1 caused an increase in the generation of inositol phosphates and diacylglycerol (DAG). In addition, the peptide provoked a translocation of protein kinase C from the cytosol to membrane.