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

被引：64
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
相关论文
共 25 条
[1]   Cathepsin D produces antimicrobial peptide parasin I from histone H2A in the skin mucosa of fish [J].
Cho, JH ;
Park, IY ;
Kim, HS ;
Lee, WT ;
Kim, MS ;
Kim, SC .
FASEB JOURNAL, 2002, 16 (01) :429-+
[2]   Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder [J].
Cole, AM ;
Weis, P ;
Diamond, G .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (18) :12008-12013
[3]   Innate host defense mechanisms of fish against viruses and bacteria [J].
Ellis, AE .
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY, 2001, 25 (8-9) :827-839
[4]   Diversity of antimicrobial peptides and their mechanisms of action [J].
Epand, RM ;
Vogel, HJ .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 1999, 1462 (1-2) :11-28
[5]   Paneth cell trypsin is the processing enzyme for human defensin-5 [J].
Ghosh, D ;
Porter, E ;
Shen, B ;
Lee, SK ;
Wilk, D ;
Drazba, J ;
Yadav, SP ;
Crabb, JW ;
Ganz, T ;
Bevins, CL .
NATURE IMMUNOLOGY, 2002, 3 (06) :583-590
[6]   The role of antimicrobial peptides in animal defenses [J].
Hancock, REW ;
Scott, MG .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (16) :8856-8861
[7]   Cationic peptides: a new source of antibiotics [J].
Hancock, REW ;
Lehrer, R .
TRENDS IN BIOTECHNOLOGY, 1998, 16 (02) :82-88
[8]   Characterization and functional analysis of 12 naturally occurring reactive site variants of serpin-1 from Manduca sexta [J].
Jiang, HB ;
Kanost, MR .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (02) :1082-1087
[9]   Pepsin-mediated processing of the cytoplasmic histone H2A to strong antimicrobial peptide buforin I [J].
Kim, HS ;
Yoon, H ;
Minn, I ;
Park, CB ;
Lee, WT ;
Zasloff, M ;
Kim, SC .
JOURNAL OF IMMUNOLOGY, 2000, 165 (06) :3268-3274
[10]   Discovery and characterization of two Isoforms of moronecidin, a novel antimicrobial peptide from hybrid striped bass [J].
Lauth, X ;
Shike, H ;
Burns, JC ;
Westerman, ME ;
Ostland, VE ;
Carlberg, JM ;
Van Olst, JC ;
Nizet, V ;
Taylor, SW ;
Shimizu, C ;
Bulet, P .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (07) :5030-5039
123