Matrix metalloproteinase 2 is involved in the regulation of the antimicrobial peptide parasin I production in catfish skin mucosa

被引：63
作者：
Cho, JH
Park, IY
Kim, MS
Kim, SC
机构：
[1] Korea Adv Inst Sci & Technol, Dept Biol Sci, Yusong Gu, Taejon 305701, South Korea
[2] Korea Inst Energy Res, Biomass Team, Taejon 305343, South Korea
来源：
FEBS LETTERS | 2002年 / 531卷 / 03期
关键词：
antimicrobial peptide; cathepsin D; historic H2A; matrix metalloproteinase 2; parasin I;
D O I：
10.1016/S0014-5793(02)03584-6
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 19-residue antimicrobial peptide parasin I is generated from histone H2A in the skin mucus of catfish by the action of cathepsin D activated by a procathepsin D-processing enzyme induced upon epidermal injury. Here we report the isolation and characterization of the procathepsin D-processing enzyme in the mucus of wounded catfish. Sequence analysis of the cDNA identified the purified procathepsin D-processing enzyme as matrix metalloproteinase 2 (MMP 2). By acting as a procathepsin D convertase upon epidermal injury, MMP 2 is involved in the regulation of parasin I production in catfish skin mucosa. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码：459 / 463
页数：5
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