Characterization of a novel phospholipase A2 activity in human brain.
Characterization of a novel phospholipase A2 activity in human brain.
复制标题
人脑中新型磷脂酶 A2 活性的表征。
DOI：
10.1046/j.1471-4159.1995.64052213.x
复制
发表时间：
1995
影响因子：
4.7
通讯作者：
Kish,SJ
中科院分区：
文献类型：
--
作者：
Ross,BM;Kim,DK;Bonventre,JV;Kish,SJ
Phospholipases A2(PLA2) are a family of enzymes that catalyze the removal of fatty acid residues from phosphoglycerides. The enzyme is postulated to be involved in several human brain disorders, although little is known regarding the status of PLA2activity in human CNS. We therefore have characterized some aspects of the PLA2activity present in the temporal cortex of human brain. More PLA2activity was found in the membrane (particulate) fraction than in the cytosolic fraction. The enzyme could be solubilized from particulate material using 1Mpotassium chloride, and was capable of hydrolyzing choline phosphoglyceride (CPG) and ethanolamine phosphoglyceride (EPG), with a preference (approximately eightfold) for EPG over CPG. When the solubilized particulate enzyme was subjected to gel filtration chromatography, PLA2activity eluted in a high molecular mass fraction (∼180 kDa). PLA2activity was weakly stimulated by dithiothreitol, strongly stimulated by millimolar concentrations of calcium ions, and inhibited by brief heat treatment at 57°C, bromophenacyl bromide, the arachidonic acid derivative AACOCF3, γ‐linolenoyl amide, andN‐methyl γ‐linolenoyl amide. Thus, whereas the human brain enzyme(s) characterized in our study displays some of the characteristics of previously characterized PLA2s, it differs in several key features.
