Tetracyclines와 단백질분해효소 억제제에 의한 Human 92-kD type IV Collagenase (Gelatinase B)의 활성도 억제 = Inhibition of Human 92-kD type IV Collagenase (Gelatinase B) Activity by Tetracyclines and Proteinase Inhibitors

다국어 초록 (Multilingual Abstract)

Background : Human 92-kD type IV collagenase(gelatinase B), a family of matrix metalloproteinases(MMP), is involved in the remodeling of connective tissue as well as in disease states associated with acute and chronic inflammation or tumoral metastatic processes.
Methods : To investigate the pharmacological and enzymatic characteristics of human neutrophil type IV collagenase, the enzyme was extracted from human neutrophils and purified by a combination of Ultrogel AcA 54 gel filtration and Bio-Rex 70 ion exchange 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 IV collagenase degraded gelatin at the specific cleavage site, but did not affect intact type I collagen. Human 92-kD type IV collagenase was activated by aminophenylmercuric acetate and molecular conformation was changed at the disulfide bond finger site.
Conclusion : Human 92-kD type IV collagenase was inhibited by tetracycline, de-dimethylaminotetracycline and pepstatin A, an inhibitor of aspartic proteinase,
E-64, an inhibitor of cysteine proteinase and leupeptin, an inhibitor of cystein and serine proteinase had no inhibitory effect on human 92-kD type IV collagenase activity.

목차 (Table of Contents)

• 서론
• 재료 및 방법
• 1. 재료
• 2. 방법
• 결과
• 1. human 92-kD type IV collagenase의 분자량 측정
• 2. APMA에 의해 활성화된 human 92-kD type IV collagenase의 분자 구조의 변화
• 3. 효소 활성화 및 활성도 억제 효과
• 고찰
• 결론
• 참고문헌

참고문헌 (Reference)

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