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KMID : 0857020060210010293
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Kosin Medical Journal
2006 Volume.21 No. 1 p.293 ~ p.301
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Isolation and Characterization of Human 92-kD type Ⅳ Collagenase (Gelatinase B)
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Lee Dae-Heui
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Abstract
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Background : Human 92-kD type Ⅳ collagenase (gelatinase B), a family of matrix metalloproteinases (MMP), play important roles in the degradation of the basement membrane and the migration of leukocytes and metastatic tumor cells during inflammation and invasion, respectively.
Methods : To investigate the biochemical and enzymatic charicteristics of human neurtrophil type Ⅳ collagenase, the enzyme was extracted from human leukocytes and purified by a combination of Ultrogel AcA 54 and Bi0-Rex 70 chromatographies.
Results : The purified enzyme showed a single band of molecular weight: 92-kD on the sodium dodecyl sulfate-polyacryl amide gel electrophoresis (SDS-PAGE). Human neutrophil type Ⅳcollagenase degraded gelatin at the specific cleavage site, but did not affect intact typeⅠcollagen. Human 92-kD type Ⅳ collagenase was inhibited by EGTA, EDTA and tetracycline. These inhibitory effects may be related to the chelation effect of these agents since 92-kD type Ⅳ collagenase is a metalloenzyme.
Conclusion : Tetracycline showed the strongest inhibition effect on the gelatinolytic activity of the 92-kD type Ⅳ collagenase, and this strong effect of tetracycline among these agents might be associated with the amide group of tetracycline, besides the chelation effect of tetracycline. The carbonyl group of the amide group may be coordinated to the active site zinc atom as a fourth ligand in a way that blocks the active site.
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KEYWORD
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Gelatinase B, Ultrogel AcA 54, Bio-Rex 70, Metalloenzme, Tetracycline
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