Single-molecule tracking of collagenase on native type I collagen fibrils reveals degradation mechanism.

ABSTRACT:

Background

Collagen, the most abundant human protein, is the principal component of the extracellular matrix and plays important roles in maintaining tissue and organ integrity. Highly resistant to proteolysis, fibrillar collagen is degraded by specific matrix metalloproteases (MMPs). Degradation of fibrillar collagen underlies processes including tissue remodeling, wound healing, and cancer metastasis. However, the mechanism of native collagen fibril degradation remains poorly understood.

Results

Here we present the results of high-resolution tracking of individual MMPs degrading type I collagen fibrils. MMP1 exhibits cleavage-dependent biased and hindered diffusion but spends 90% ± 3% of the time in one of at least two distinct pause states. One class of exponentially dist

SUBMITTER: Sarkar SK 

PROVIDER: S-EPMC3382001 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature