Multiple forms of phosphoinositide-specific phospholipase C of different relative molecular masses in animal tissues. Evidence for modification of the platelet enzyme by Ca2+-dependent proteinase.
Multiple forms of phosphoinositide-specific phospholipase C of different relative molecular masses in animal tissues. Evidence for modification of the platelet enzyme by Ca2+-dependent proteinase.
复制标题
动物组织中多种形式的不同相对分子质量的磷酸肌醇特异性磷脂酶 C。
DOI：
10.1042/bj2210813
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
Weglicki,WB
中科院分区：
文献类型：
--
作者：
Low,MG;Carroll,RC;Weglicki,WB
用高效凝胶过滤色谱法分析了多种动物组织分离的上清液中磷酸肌苷特异性磷脂酶C的Mr分布。在大多数组织中，至少有四个活性峰被分解。然而，不同组织在这些峰值之间的活性分布表现出相当显著的差异。在大鼠心脏、肺和肾脏中，Mr约为主要形式。而在大脑中的主要形式，Mr约为。290000. 在肝脏中，Mr-90000形式占主导地位，但该组织也含有相对大量的Mr- 900000形式。150000. 在其他动物的这些组织中，磷脂酶C的活性在峰之间也有类似的分布。在白细胞活化素（0.5 mM）或EGTA （20 mM）存在下制备的血小板上清液中，Mr-290000形式占主导地位。然而，当从超声缓冲液中省略胰肽或EGTA （Ca2+依赖性蛋白酶抑制剂）时，Mr-290000形式似乎被Mr 100000形式所取代。Mr在其他组织中没有出现类似的变化。这些结果可能与磷脂酶C的细胞内调节有关，因为据报道，在血小板活化过程中会发生Ca2+依赖性蛋白水解。
The Mr distribution of phosphoinositide-specific phospholipase C in the supernatants isolated from a variety of animal tissues was analysed by high-performance gel-filtration chromatography. In most tissues, at least four peaks of activity were resolved. However, different tissues showed quite marked differences in the distribution of activity between these peaks. In rat heart, lung and kidney, the predominant form had Mr approx. 90000, whereas the predominant form in brain had Mr approx. 290000. In liver, the Mr-90000 form predominated, but this tissue also contained relatively large amounts of a form of Mr approx. 150000. Phospholipase C in these tissues from other animal species gave similar distributions of activity between the peaks. In supernatants prepared from platelets sonicated in the presence of leupeptin (0.5 mM) or EGTA (20 mM), the Mr-290000 form predominated. However, when leupeptin or EGTA (inhibitors of Ca2+-dependent proteinase) was omitted from the sonication buffer, the Mr-290000 form appeared to be replaced by a form of Mr 100000. Similar changes in Mr were not demonstrated with the other tissues. These results may be relevant to the intracellular regulation of phospholipase C, since Ca2+-dependent proteolysis has been reported to occur during platelet activation.