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转化成纤维细胞中一种糜蛋白酶抑制素敏感的内肽酶的检测及部分特性分析

Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts.

作者信息

O'Donnell-Tormey J, Quigley J P

出版信息

Proc Natl Acad Sci U S A. 1983 Jan;80(2):344-8. doi: 10.1073/pnas.80.2.344.

DOI:10.1073/pnas.80.2.344
PMID:6300832
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC393373/
Abstract

A chymostatin-sensitive step in the release of plasminogen activator from transformed fibroblasts has been described recently. By using synthetic peptidyl substrates, we have detected and characterized a chymostatin-sensitive peptidase activity in chicken embryo fibroblasts transformed by Rous sarcoma virus. The activity represents a neutral endopeptidase that exhibits phenylalanine specificity and is inhibited by diisopropyl fluorophosphate. A detailed inhibitor profile of the enzyme activity shows that it is distinct from other chymotrypsin-like phenylalanine-preferring peptidases. The endopeptidase activity in transformed fibroblasts is increased over that of parallel cultures of normal fibroblasts. The mechanism of enzyme inhibition by chymostatin is indicated by these studies, and the possible role of the enzyme in modulating plasminogen activator secretion is discussed.

摘要

最近已描述了转化成纤维细胞中纤溶酶原激活物释放过程中对抑肽酶敏感的步骤。通过使用合成肽基底物，我们在经劳斯肉瘤病毒转化的鸡胚成纤维细胞中检测并鉴定了一种对抑肽酶敏感的肽酶活性。该活性代表一种中性内肽酶，具有苯丙氨酸特异性，并且被氟磷酸二异丙酯抑制。该酶活性的详细抑制剂谱表明它不同于其他类胰凝乳蛋白酶样的偏爱苯丙氨酸的肽酶。转化成纤维细胞中的内肽酶活性高于正常成纤维细胞平行培养物中的活性。这些研究表明了抑肽酶对酶的抑制机制，并讨论了该酶在调节纤溶酶原激活物分泌中的可能作用。

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本文引用的文献

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Cell. 1981 Nov;27(1 Pt 2):85-95. doi: 10.1016/0092-8674(81)90363-9.
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