期刊
SCIENCE
卷 306, 期 5693, 页码 108-111出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1099179
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资金
- NIAMS NIH HHS [AR39472, AR40618] Funding Source: Medline
- NIGMS NIH HHS [GM-38838] Funding Source: Medline
We show that activated collagenase (MMP-1) moves processively on the collagen fibril. The mechanism of movement is a biased diffusion with the bias component dependent on the proteolysis of its substrate, not adenosine triphosphate (ATP) hydrolysis. inactivation of the enzyme by a single amino acid residue substitution in the active center eliminates the bias without noticeable effect on rate of diffusion. Monte Carlo simulations using a model similar to a burnt bridge Brownian ratchet accurately describe our experimental results and previous observations on kinetics of collagen digestion. The biological implications of MMP-1 acting as a molecular ratchet tethered to the cell surface suggest new mechanisms for its role in tissue remodeling and cell-matrix interaction.
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