Kishikawa T
Central Institute for Electron Microscopic Research, Tokyo, Japan.
J Submicrosc Cytol Pathol. 1990 Oct;22(4):507-13.
Rat lung surfactants including lamellar body, common myelin and tubular myelin were evaluated for enzyme activities of phospholipase A and phospholipase C using [14C] phosphatidylcholine as the substrate. The metabolic profiles of phosphatidylcholine were correlated with ultrastructural changes of each fraction in vitro incubation to elucidate whether any of these enzymes has a role in the morphological change. Lamellar body showed phospholipase A and phospholipase C activities at neutral pH. Electron microscopic observation showed that although these enzymes had no direct role in change of integration of the lamellar body to lattice tubule, phospholipase C had a role in modulation of the lamellar body to loose lamellae, and phospholipase A had a role in degradation of lattice integration.
以[14C]磷脂酰胆碱为底物,对包括板层小体、普通髓鞘和管状髓鞘在内的大鼠肺表面活性物质进行磷脂酶A和磷脂酶C的酶活性评估。在体外孵育过程中,将磷脂酰胆碱的代谢谱与各组分的超微结构变化相关联,以阐明这些酶中是否有任何一种在形态变化中起作用。板层小体在中性pH值下表现出磷脂酶A和磷脂酶C活性。电子显微镜观察表明,虽然这些酶在板层小体整合为晶格小管的变化中没有直接作用,但磷脂酶C在板层小体向松散薄片的调节中起作用,而磷脂酶A在晶格整合的降解中起作用。