Kunze H, Löffler B M, Schmidt M
Max-Planck-Institut für Experimentelle Medizin, Göttingen, FRG.
FEBS Lett. 1988 Aug 29;236(2):388-90. doi: 10.1016/0014-5793(88)80062-0.
Cultured rat hepatocytes exhibit acid phospholipase A activity. On the basis of product formation from stereospecifically radiolabeled phosphatidylethanolamine substrates, phospholipases A1 and A2 have been identified with optimal activities at pH 4.5. According to subcellular fractionation studies, the acid phospholipases in hepatocytes appear to be located in the lysosomal compartment. Application of specific inhibitors of the biosynthesis, glycosylation, and translocation of lysosomal enzymes in hepatocyte cultures suggests a half-life of approx. 1 day for the acid lysosomal phospholipase A1. About the same value for the half-life was obtained for the lysosomal marker enzymes, acid phosphatase and beta-N-acetyl-D-hexosaminidase.
培养的大鼠肝细胞表现出酸性磷脂酶A活性。根据立体特异性放射性标记的磷脂酰乙醇胺底物的产物形成情况,已鉴定出磷脂酶A1和A2在pH 4.5时具有最佳活性。根据亚细胞分级分离研究,肝细胞中的酸性磷脂酶似乎位于溶酶体区室。在肝细胞培养物中应用溶酶体酶生物合成、糖基化和转运的特异性抑制剂表明,酸性溶酶体磷脂酶A1的半衰期约为1天。溶酶体标记酶酸性磷酸酶和β-N-乙酰-D-己糖胺酶的半衰期也得到了大致相同的值。