Carboxypeptidase N: a pleiotropic regulator of inflammation

Carboxypeptidase N: a pleiotropic regulator of inflammation
复制标题

DOI:
10.1016/j.molimm.2003.10.002
复制
发表时间:
2004-01-01
影响因子:
3.6
通讯作者:
Wetsel, RA
Wetsel, RA
中科院分区:
医学3区
文献类型:
--
作者:
Matthews, KW;Mueller-Ortiz, SL;Wetsel, RA

文献摘要

被引文献

相似文献

羧基肽酶N (Carboxypeptidase N, CPN)是一种血浆锌金属蛋白酶,由两个具有酶活性的小亚基(CPN1)和两个保护蛋白不被降解的大亚基(CPN2)组成。CPN从血液中发现的肽如补体过敏毒素、肌酸激酶和肌酸激酶MM (CK-MM)中切割羧基端精氨酸和赖氨酸。通过去除一个氨基酸,CPN具有改变肽活性和受体结合的能力。CPN是一个更大的羧基肽酶家族的成员,其中许多也裂解精氨酸和赖氨酸。由于羧基肽酶高度保守的活性位点和可能的冗余功能,很难阐明CPN在疾病过程中的作用。未来使用基因消融技术可能是了解CPN在体内功能的最合适方法。(C) 2003 Elsevier Ltd.版权所有。
Carboxypeptidase N (CPN) is a plasma zinc metalloprotease, which consists of two enzymatically active small subunits (CPN1) and two large subunits (CPN2) that protect the protein from degradation. CPN cleaves carboxy-terminal arginines and lysines from peptides found in the bloodstream such as complement anaphylatoxins, kinins, and creatine kinase MM (CK-MM). By removing only one amino acid, CPN has the ability to change peptide activity and receptor binding. CPN is a member of a larger family of carboxypeptidases, many of which also cleave arginine and lysine. Because of the highly conserved active sites and the possible redundant functions of carboxypeptidases, it has been difficult to elucidate the role of CPN in disease processes. The future use of gene ablation technology may be the most appropriate way to understand the function of CPN in vivo. (C) 2003 Elsevier Ltd. All rights reserved.