MOLECULAR-CLONING AND COMPLETE AMINO-ACID-SEQUENCE OF FORM-I PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE-C
MOLECULAR-CLONING AND COMPLETE AMINO-ACID-SEQUENCE OF FORM-I PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE-C
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DOI：
10.1038/334268a0
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发表时间：
1988-07-21
期刊：
影响因子：
64.8
通讯作者：
CROOKE, ST
中科院分区：
文献类型：
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作者：
BENNETT, CF;BALCAREK, JM;CROOKE, ST
我们报道了磷酸肌醇特异性磷脂酶C （PI-PLC）的分子克隆和序列，这种酶因其在细胞信号转导中的核心作用而引起特别关注。所讨论的信号是那些由激素传递到细胞表面受体的信号，这些受体通过鸟嘌呤核苷酸结合蛋白激活PI-PLC。酶的激活导致磷脂酰肌醇4,5-二磷酸水解为两个第二信使，1,2-二酰基甘油和1,4,5-三磷酸肌醇，后者最终动员内部的钙池1,2。至少有五种PI-PLC同工酶，其结构和功能的差异尚不清楚3 - 10。我们的重点是同工酶I，我们最近从豚鼠子宫中纯化并鉴定了它。我们现在已经确定了这个同工酶的全长互补DNA的序列。尽管该序列与其他唯一测序的PI-PLC同工酶几乎没有相似性11，但它与硫醇依赖氧化还原反应中的蛋白质辅助因子硫氧还毒素有着惊人的相似性12。
We report the molecular cloning and sequence of a phosphoinositide-specific phopspholipase C (PI-PLC), an enzyme that is of particular interest because of its central role in cell signal transduction. The signals in question are those delivered by hormones to their cell-surface receptors that activate PI-PLC by means of a guanine nucleotide binding protein. Activation of the enzyme leads to the hydrolysis of phosphatidylinositol 4,5-bisphosphate to two second messengers, 1,2-diacylglycerol and inositol 1,4,5-trisphos-phate, the second of which ultimately mobilizes internal pools of calcium1,2. There are at least five PI-PLC isoenzymes, whose differences in structure and function are unknown3–10. We have focused on isoenzyme I, which we have recently purified and characterized from guinea pig uterus8. We have now determined the sequence of a full length complementary DNA of this isoenzyme from the rat. Although the sequence has little similarity with the only other sequenced PI-PLC isoenzyme11, it has a surprising degree of similarity to thioredoxins, protein co-factors in thiol-dependent redox reactions12.