Matrix metalloproteinase 2 is involved in the regulation of the antimicrobial peptide parasin I production in catfish skin mucosa
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.
- Publisher
- ELSEVIER SCIENCE BV
- Issue Date
- 2002-11
- Language
- English
- Article Type
- Article
- Keywords
INNATE HOST-DEFENSE; HISTONE H2A; PLEUROCIDIN; ACTIVATION; FLOUNDER
- Citation
FEBS LETTERS, v.531, no.3, pp.459 - 463
- ISSN
- 0014-5793
- Appears in Collection
- BS-Journal Papers(저널논문)
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