A NEW METALLOENDOPEPTIDASE FROM HUMAN NEUROBLASTOMA NB-OK-1 CELLS WHICH INACTIVATES ATRIAL-NATRIURETIC-PEPTIDE BY SELECTIVE CLEAVAGE AT THE SER123-PHE124 BOND

被引：13

作者：

DELPORTE, C ^{[1
]}

CARVALHO, KD ^{[1
]}

LESENEY, AM ^{[1
]}

WINAND, J ^{[1
]}

CHRISTOPHE, J ^{[1
]}

COHEN, P ^{[1
]}

机构：

[1] UNIV PARIS 06,CNRS,UA 554,NEUROBIOCHIM CELLULAIRE & MOLEC GRP,F-75006 PARIS,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 182卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)80125-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A novel metallo-endopeptidase from human neuroblastoma NB-OK-1 cells was partially purified and characterized. This enzyme activity was detected in the culture medium and could be detached from intact cells by gentle washing, suggesting a peripheral localization of the enzyme. This endopeptidase inactivated Atrial Natriuretic Peptide (ANP) by a unique and selective cleavage of the Ser123-Phe124 bond. It also produced hydrolysis at the Xaa-Phe, Xaa-Leu, or Xaa-Ile bonds of other peptide hormones such as bradykinin, somatostatin 14, litorin, substance P, neuromedin C and angiotensin II. The substrate selectivity and inhibition profile of the enzyme showed obvious similarities with the peptide hormone inactivating endopeptidase (PHIE) recently purified from Xenopus laevis skin secretions and indicated a thermolysin-like activity distinct from neutral endopeptidase (EC 3.4.24.11) and from angiotensin converting enzyme (EC 3.4.15.1). © 1992 Academic Press, Inc.

引用

页码：158 / 164

页数：7

共 12 条

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