Chambers T C, Eilon G
Department of Biological Chemistry, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.
Biochem Biophys Res Commun. 1988 Dec 15;157(2):507-14. doi: 10.1016/s0006-291x(88)80278-x.
Protein kinase C activity in the particulate fraction of the heart increases two-fold during mid-stage of disease in the cardiomyopathic hamster. No change in the corresponding enzyme activity occurs with aging in healthy control hamsters. In the solubilized particulate fraction of hearts from both myopathic and control animals, Ca++/phospholipid-dependent endogenous phosphorylation of proteins of Mr 26, 31, 45, 53, 69, 98, 105 and 126 kDa are observed. All of these proteins are more highly phosphorylated in the protein kinase C-enriched preparation from the myopathic heart compared to the control. No significant differences between myopathic and control hamsters are observed in the activities of protein kinase C or phosphoinositide-specific phospholipase C from heart cytosol.
在患心肌病的仓鼠疾病中期，心脏微粒部分中的蛋白激酶C活性增加两倍。在健康对照仓鼠中，相应的酶活性不会随衰老而发生变化。在患有肌病的动物和对照动物的心脏可溶性微粒部分中，观察到分子量为26、31、45、53、69、98、105和126 kDa的蛋白质发生Ca++/磷脂依赖性内源性磷酸化。与对照相比，在来自患肌病心脏的富含蛋白激酶C的制剂中，所有这些蛋白质的磷酸化程度更高。在患肌病的仓鼠和对照仓鼠之间，心脏胞质溶胶中的蛋白激酶C或磷酸肌醇特异性磷脂酶C的活性未观察到显著差异。
