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Isolation and characterization of a high molecular weight type IV collagenase isolated from human carcinoma tissue
Author(s) -
Tsuda Tomi T.,
Kodama Akira,
Yamamura Masaichi,
Matsuzaki Shohei,
Tsuda Michio
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80032-p
Subject(s) - collagenase , gelatinase , matrix metalloproteinase , gelatinase a , trypsin , chemistry , enzyme , metalloproteinase , microbiology and biotechnology , biochemistry , type i collagen , interstitial collagenase , biology , endocrinology
A proform of high molecular weight type IV collagenase was isolated and purified 1230‐fold from human metastatic carcinoma tissue. Like matrix metalloproteinases (MMPs), the enzyme was activated by trypsin and degraded type IV collagen and gelatin at a neutral pH, the activity was inhibited by EDTA and o ‐phenanthroline. However, the molecular weight was much higher than MMPs which degraded type IV collagen, gelatinase A (MMP‐2; 72 kDa gelatinase/type IV collagenase) (EC 3.4.24.24), gelatinase B (MMP‐9; 92 kDa gelatinase/type IV collagenase) (EC 3.4.24.35), stromelysin‐1 (MMP‐3; 57 kDa) (EC 3.4.24.17) and stromelysin‐2 (MMP‐10; 57 kDa) (EC 3.4.24.22). The other significant difference from MMPs was that the enzyme was not activated by 4‐aminophenylmercuric acetate nor inhibited by TIMP. Taking together these results, this high molecular weight type IV collagenase might be a newly found enzyme different from MMPs or might have the same configuration as MMPs already reported.