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J. Biochem, 1990, Vol. 108, No. 2 222-229
© 1990 Japanese Biochemical Society

research-article

Protein Kinase-Dependent Phosphorylation of Cardiac Sarcolemmal Ca2+ as Studied with a Specific Monoclonal Antibody1

Tarou Ogurusu, Shigeo Wakabayashi, Ken-Ichi Furukawa, Yuko Tawada-Iwata, Toshiaki Imagawa and Munekazu Shigekawa

Department of Molecular Physiology, National Cardiovascular Center Research Institute Suito, Osaka 565

Phosphorylation of the Ca2+ ATPase of cadiac sarcolemmal vesicles by exogeneously added protein kineses was examined to elucidate the molecular basis for its regulation. The Ca2+-pump ATPase was isolated from protein kinase-treated sarcolemmal vesicles using a monoclonal antibody raised against the erythrocyte Ca2+ Protein kinase C (C-kinase) was found to phosphorylate the Ca2+ The stoichiometry of this phosphor ylation was about 1 mol per mol of the ATPase molecule. The C-kinase activation resulted in up to twofold acceleration of Ca2+ uptake by sarcolemmal vesicles due to its effect on the affinity of the Ca2+ pump for Ca2+ in both the presence and absence of calmodulin. Both the phosphorylation and stimulation of ATPase activity by C kinase were also observed with a highly-purified Ca2+ preparation isolated from cardiac sarcolemma with cal modulin-Sepharose and a high salt-washing procedure. Thus, C-klnase appears to stimu late the activity of the sarcolemmal Ca2+ pump through its direct phosphorylation. In contrast to these results, neither cAMP-dependent protein kinase, cGMP-dependent protein kinase nor Ca2+ protein kinase II phosphorylated the Ca2+ in the sarcoleinmal membrane or the purified enzyme preparation, and also they exerted virtually no effect on Ca2+ uptake by sarcolemmal vesicles.

1This study was supported in part by a Grant-in-Aid for Scientific Research on Priority Areas (62624515) from the Ministry of Educa tion, Science and Culture of Japan.


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