Identification and characterization of a hormonally regulated form of phospholipase A2 in rat renal mesangial cells.
作者： J H Gronich , J V Bonventre , R A Nemenoff
DOI: 10.1016/S0021-9258(18)37439-8
关键词:
摘要: The activity of phospholipase A2 (PLA2), the regulatory enzyme in arachidonic acid release and prostaglandin synthesis, was measured cell-free extracts rat renal mesangial cells. Arginine vasopressin (AVP) phorbol myristate acetate (PMA) both stimulated PLA2 as assayed by free from exogenously added [14C]arachidonyl-phosphatidylcholine. This represents a direct vitro demonstration hormone-induced changes activity. recovered following fractionation DEAE-cellulose anion exchange FPLC Superose 12 gel filtration. Stimulated AVP- PMA-treated cells comigrated single peak, suggesting that these agents are stimulating form enzyme. molecular weight this hormonally regulated is approximately 60,000. has an obligate requirement for Ca2+, having no presence EGTA, pH optimum alkaline range. Following cell disruption chelators, high speed supernatant. However, it appears can bind to crude membrane fraction Ca2+-dependent manner, similar other Ca2+-phospholipid binding proteins. observed stable modification AVP PMA suggests phosphorylation or modulators protein kinase C.
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