Goppelt-Struebe M, Rehfeldt W
Institute of Molecular Pharmacology, Medical School Hannover, Germany.
Biochim Biophys Acta. 1992 Jul 29;1127(2):163-7. doi: 10.1016/0005-2760(92)90273-x.
The cytosolic phospholipase A2 (PLA2) was characterized in the human epithelial carcinoma cell line HEp-2 by its apparent molecular mass (about 80 kDa); its in vitro activation by micromolar concentrations of calcium; and its calcium-dependent association with cellular membranes. The activity of this enzyme was induced by an overnight incubation with tumor necrosis factor alpha (TNF alpha). Glucocorticoids only moderately reduced PLA2 activity in control cells, but completely inhibited the TNF alpha-induced increase in the activity of the high-molecular-weight cytosolic PLA2.
通过其表观分子量(约80 kDa)、微摩尔浓度钙对其体外激活作用以及其与细胞膜的钙依赖性结合,对人上皮癌细胞系HEp-2中的胞质磷脂酶A2(PLA2)进行了表征。该酶的活性通过与肿瘤坏死因子α(TNFα)过夜孵育诱导产生。糖皮质激素仅适度降低对照细胞中的PLA2活性,但完全抑制了TNFα诱导的高分子量胞质PLA2活性增加。