人和兔中性粒细胞膜的钙离子激活的多磷酸肌醇磷酸二酯酶
The Ca2+-activated polyphosphoinositide phosphodiesterase of human and rabbit neutrophil membranes.
作者信息
Cockcroft S, Baldwin J M, Allan D
出版信息
Biochem J. 1984 Jul 15;221(2):477-82. doi: 10.1042/bj2210477.
Abstract
Addition of Ca2+ to a plasma-membrane fraction derived from human or rabbit neutrophils led to the specific breakdown of polyphosphoinositides. The degradation products were identified as diacylglycerol and inositol bis- and tris-phosphate, thus demonstrating the presence of a Ca2+-activated phospholipase C. The newly generated diacylglycerol resembled the polyphosphoinositides in its fatty acid composition, and in the presence of MgATP2- it was converted into phosphatidate. These results therefore demonstrate the presence in neutrophil plasma membranes not only of polyphosphoinositide phosphodiesterase but also of diacylglycerol kinase.
摘要
向源自人或兔中性粒细胞的质膜组分中添加钙离子会导致多磷酸肌醇的特异性分解。降解产物被鉴定为二酰基甘油以及肌醇二磷酸和肌醇三磷酸，从而证明存在钙离子激活的磷脂酶C。新生成的二酰基甘油在脂肪酸组成上与多磷酸肌醇相似，并且在存在MgATP2-的情况下会转化为磷脂酸。因此，这些结果证明中性粒细胞质膜中不仅存在多磷酸肌醇磷酸二酯酶，还存在二酰基甘油激酶。
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