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

作者信息

Cho Ju Hyun, Park In Yup, Kim Mi Sun, Kim Sun Chang

机构信息

Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 373-1 Kusong-dong Yusong-gu, 305-701, Taejon, South Korea.

出版信息

FEBS Lett. 2002 Nov 20;531(3):459-63. doi: 10.1016/s0014-5793(02)03584-6.

DOI:10.1016/s0014-5793(02)03584-6
PMID:12435593
Abstract

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.

摘要

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