Wightman P D, Dahlgren M E, Davies P, Bonney R J
Biochem J. 1981 Nov 15;200(2):441-4. doi: 10.1042/bj2000441.
Resident mouse peritoneal macrophages have three phospholipase activities: a phospholipase A2 active at pH 4.5, a Ca2+-dependent phospholipase A2 active at pH 8.5 and a phosphatidylinositol-specific phospholipase C activity. When macrophages are exposed to zymosan in culture, the cellular activity of pH-4.5 phospholipase A2 is diminished in a manner dependent on zymosan concentration and time of exposure, whereas the cellular activities of pH-8.5 phospholipase A2 and phospholipase C remain unchanged. The depletion of pH-4.5 phospholipase A2 activity from the cell is paralleled by a quantitative recovery of this activity in the culture medium in a manner similar to the cellular depletion and extracellular recovery of two lysosomal enzymes. This release is specifically elicited by an inflammatory substance such as zymosan, since macrophages incubated with 6 micrometer latex spheres retain pH-4.5 phospholipase A2 activity and lysosomal enzyme activities intracellularly.
一种在pH 4.5时具有活性的磷脂酶A2、一种在pH 8.5时具有活性的Ca2+依赖性磷脂酶A2以及一种磷脂酰肌醇特异性磷脂酶C活性。当巨噬细胞在培养物中暴露于酵母聚糖时,pH 4.5磷脂酶A2的细胞活性以依赖于酵母聚糖浓度和暴露时间的方式降低,而pH 8.5磷脂酶A2和磷脂酶C的细胞活性保持不变。细胞中pH 4.5磷脂酶A2活性的消耗与该活性在培养基中的定量恢复相平行,其方式类似于两种溶酶体酶的细胞内消耗和细胞外恢复。这种释放是由诸如酵母聚糖等炎性物质特异性引发的,因为与6微米乳胶球一起孵育的巨噬细胞在细胞内保留了pH 4.5磷脂酶A2活性和溶酶体酶活性。