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Characterization of a rainbow trout matrix metalloproteinase capable of degrading type I collagen

M Saito1, K Sato, N Kunisaki

  • 1Laboratory of Food Science, Kagawa Nutrition University, Komagome, Toshima, Tokyo, Japan. msaito@eiyo.ac.jp

European Journal of Biochemistry
|November 18, 2000
PubMed

Insights

Researchers identified a unique fish matrix metalloproteinase-13 (MMP-13) in rainbow trout. This fish MMP-13 effectively degrades type I collagen, marking a significant discovery in fish collagenase research.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Fish Biology

Background:

  • Matrix metalloproteinases (MMPs) are a large family of enzymes found in vertebrates.
  • MMP-13, also known as collagenase-3, is a key collagenase in higher vertebrates.
  • Understanding fish MMPs is crucial for comparative molecular biology.

Purpose of the Study:

  • To clone and characterize a fish homologue of human MMP-13.
  • To investigate the enzymatic activity of the identified fish MMP-13.
  • To establish the first report of a fish MMP capable of degrading type I collagen.

Main Methods:

  • Cloning of cDNA encoding rainbow trout MMP-13 from a fibroblast cDNA library.
  • Expression of the recombinant protein in Escherichia coli.
  • Degradation assays using gelatin, calf type I collagen, and rainbow trout type I and V collagen.

Main Results:

  • A unique rainbow trout MMP-13 cDNA (2.1 kb) encoding a 475-amino acid protein was isolated.
  • The recombinant fish MMP-13 showed 66% identity to human MMP-13 in the catalytic domain.
  • The enzyme degraded gelatin and type I collagen, with higher susceptibility observed for rainbow trout collagen.
  • Cleavage of nonhelical regions in rainbow trout muscle type V collagen was also observed.

Conclusions:

  • The cloned cDNA encodes a unique rainbow trout MMP-13.
  • This fish MMP-13 exhibits collagenase activity, particularly against its native type I collagen.
  • This study represents the first identification of a fish MMP with type I collagen degrading capabilities.

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