2',3'-cyclic nucleotide 3'-phosphodiesterase, an oligodendrocyte-Schwann cell and myelin-associated enzyme of the nervous system.
2',3'-cyclic nucleotide 3'-phosphodiesterase, an oligodendrocyte-Schwann cell and myelin-associated enzyme of the nervous system.
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发表时间：
1989
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Sprinkle Tj
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作者：
Sprinkle Tj
2‘，3’-环核苷酸3‘-磷酸水解酶(E.C.3.1.4.37；CNPase)是一种髓鞘结合酶。在中枢和外周神经系统组织中，该酶几乎只定位于形成髓鞘的两种细胞类型，分别是少突胶质细胞和雪旺细胞。CNPase的非神经来源也被描述过，但它们的活性都比在大脑中发现的要低得多。新分离的脑酶在SDS-PAGE上显示为约46 kDa和48 kDa的紧密间隔的双联体。初级序列在这两种蛋白之间高度保守，命名为CNP1和CNP2。这两种蛋白质之间的主要结构差异很可能是由于酶本身的翻译后修饰(当然是磷酸化，也可能是其他)或选择性剪接。大鼠和牛脑CNPase的初级序列已经从cDNA序列中推导出来，这些酶似乎是独一无二的。目前的研究表明，CNPase参与了早期少突胶质细胞膜生物发生和可能的维持过程中髓鞘膜的快速生长。CNPase的绝对水解性，从2‘，3’-环底物产生2‘-单核苷酸，强烈地表明CNPase是一种核酸酶，可能与RNA代谢有关。
2',3'-Cyclic nucleotide 3'-phosphohydrolase (E.C. 3.1.4.37; CNPase) is a myelin-associated enzyme. In central and peripheral nervous system tissues, the enzyme is localized almost exclusively in the two cell types that elaborate myelin, the oligodendrocyte and the Schwann cell, respectively. Nonneural sources of CNPase have also been described, but they all have much lower activities than those found in brain. The freshly isolated brain enzymes appear as closely spaced doublets at approximately 46 and 48 kDa on SDS-PAGE. The primary sequence appears highly conserved between these two proteins, designated CNP1 and CNP2. Major structural differences between these two proteins are most likely due to posttranslational modifications of the enzyme itself (certainly phosphorylation, possibly others) or to alternative splicing. The primary sequences of rat and bovine brain CNPase have now been deduced from the cDNA sequences and the enzymes appear to be unique. Current research suggests that CNPase is involved in the very rapid growth of myelin membrane during early oligodendrocyte membrane biogenesis and possibly maintenance. The absolute hydrolysis specificity, yielding 2'-mononucleotides from 2',3'-cyclic substrates, strongly suggests that CNPase is a nucleic acid enzyme, possibly related to RNA metabolism.