Kinetic analysis of matrix metalloproteinase activity using fluorogenic triple-helical substrates.

Journal article

Matrix metalloproteinase (MMP) family members are involved in the physiological remodeling of tissues and embryonic development as well as pathological destruction of extracellular matrix components. To study the mechanisms of MMP action on collagenous substrates, we have constructed homotrimeric, fluorogenic triple-helical peptide (THP) models of the MMP-1 cleavage site in type II collagen. The substrates were designed to incorporate the fluorophore/quencher pair of (7-methoxycoumarin-4-yl)a...

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Authors: Lauer-Fields, J; Broder, T; Sritharan, T; Chung, L; Nagase, H

• Publication status: Published
• Journal: Biochemistry
• Volume: 40
• Issue: 19
• Pages: 5795-5803
• Publication date: 2001-05-01
• DOI: 10.1021/bi0101190
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Matrix Metalloproteinases; Matrix Metalloproteinase 2; Collagenases; Molecular Sequence Data; Humans; Protein Structure, Secondary; Fluorescent Dyes; Matrix Metalloproteinase 3; Hydrolysis; Cells, Cultured; Collagen; Kinetics; Matrix Metalloproteinase 13; Substrate Specificity; Animals; Thermodynamics; Matrix Metalloproteinase 1; Rabbits; Amino Acid Sequence; Peptide Fragments