Panagia V, Michiel D F, Dhalla K S, Nijjar M S, Dhalla N S
Biochim Biophys Acta. 1981 Sep 4;676(3):395-400. doi: 10.1016/0304-4165(81)90176-8.
The adenylate cyclase activity and phospholipid composition were determined in rat heart sarcolemma after treating the membranes with a phosphatidylinositol-specific phospholipase C. Complete hydrolysis of phosphatidylinositol in sarcolemma was associated with a marked loss of the basal adenylate cyclase activity. The recombination of the supernatant with the phosphatidylinositol-depleted membranes was found to reactivate the adenylate cyclase activity. The soluble component(s) in the supernatant, which restored the adenylate cyclase activity, was thermolabile and precipitated by ammonium sulfate. Extensive hydrolysis of phosphatidylcholine, phosphatidylethanolamine and sphingomyelin in sarcolemma with a Clostridium welchii phospholipase C treatment did not affect the basal adenylate cyclase activity. These results suggest that phosphatidylinositol anchors component(s) essential for the expression of basal adenylate cyclase activity to the myocardial cell membrane.
在用磷脂酰肌醇特异性磷脂酶C处理大鼠心肌肌膜后，测定了腺苷酸环化酶活性和磷脂组成。肌膜中磷脂酰肌醇的完全水解与基础腺苷酸环化酶活性的显著丧失有关。发现上清液与磷脂酰肌醇耗尽的膜重组可重新激活腺苷酸环化酶活性。上清液中恢复腺苷酸环化酶活性的可溶性成分对热不稳定，可被硫酸铵沉淀。用产气荚膜梭菌磷脂酶C处理肌膜，使磷脂酰胆碱、磷脂酰乙醇胺和鞘磷脂大量水解，并不影响基础腺苷酸环化酶活性。这些结果表明，磷脂酰肌醇将对基础腺苷酸环化酶活性表达至关重要的成分锚定在心肌细胞膜上。
