Mechanical Load Induces a 100-Fold Increase in the Rate of Collagen Proteolysis by MMP-1

被引：95

作者：

Adhikari, Arjun S. ^{[1
]}

Chai, Jack ^{[1
]}

Dunn, Alexander R. ^{[1
]}

机构：

[1] Stanford Univ, Dept Chem Engn, Stanford, CA 94305 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2011年 / 133卷 / 06期

基金：

美国国家卫生研究院;

关键词：

TRIPLE-HELICAL COLLAGEN; PEPTIDE-BOND HYDROLYSIS; MATRIX-METALLOPROTEINASE; TUMOR MICROENVIRONMENT; ENZYMATIC DEGRADATION; EXTRACELLULAR-MATRIX; CRYSTAL-STRUCTURE; IN-VITRO; FIBRONECTIN; STABILITY;

D O I：

10.1021/ja109972p

中图分类号：

O6 [化学];

学科分类号：

070301 [无机化学];

摘要：

Although mechanical stress is known to profoundly influence the composition and structure of the extracellular matrix (ECM), the mechanisms by which this regulation occurs remain poorly understood. We used a single-molecule magnetic tweezers assay to study the effect of force on collagen proteolysis by matrix metalloproteinase-1 (MMP-1). Here we show that the application of similar to 10 pN in extensional force causes an similar to 100-fold increase in proteolysis rates. Our results support a mechanistic model in which the collagen triple helix unwinds prior to proteolysis. The data and resulting model predict that biologically relevant forces may increase localized ECM proteolysis, suggesting a possible role for mechanical force in the regulation of ECM remodeling.

引用

页码：1686 / 1689

页数：4

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