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Volume 270, Number 15, Issue of April 14, pp. 8996-9001, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.

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Growth Factor-induced Phosphorylation and Activation of Aortic Smooth Muscle Na/CaExchanger

Takahiro Iwamoto , Shigeo Wakabayashi , Munekazu Shigekawa

Although the Na/Caexchanger is one of the major Caextrusion systems in excitable tissues, little is known about its regulation via protein phosphorylation. We now present evidence that the Na/Caexchanger is phosphorylated in quiescent and growth factor-stimulated cultured aortic smooth muscle cells. The Na/Caexchanger was isolated from P-labeled cells by immunoprecipitation with a specific polyclonal antibody. Phosphorylation of the exchanger was increased by up to 1.7-fold in response to platelet-derived growth factor-BB (PDGF-BB), -thrombin, or phorbol 12-myristate 13-acetate (PMA). However, angiotensin II did not enhance the phosphorylation significantly. The extent of phosphorylation appeared to correlate with the growth factor-induced increase in cell 1,2-diacylglycerol. At least four phosphopeptides (P1 to P4) were detected by tryptic phosphopeptide map analysis of the phosphorylated exchanger, suggesting that phosphorylation occurred at multiple sites. PDGF-BB and PMA increased phosphorylation of the same phosphopeptides (in particular P1). Phosphorylated amino acids were exclusively serine residues in both quiescent and stimulated cells. We found that growth factors enhanced Na/Caexchange activity and that there was a good correlation between the growth factor-induced stimulations of phosphorylation and exchange activity. PDGF-BB-induced activation of the exchanger was abolished by prior long treatment of cells with PMA. These results suggest that the Na/Caexchanger is activated by protein kinase C-dependent phosphorylation in response to growth factors in vascular smooth muscle cells.

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