Matrix metalloproteinase interactions with collagen and elastin.
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ABSTRACT:
SUBMITTER: Van Doren SR
PROVIDER: S-EPMC4466143 | biostudies-literature | 2015 May-Jul
REPOSITORIES: biostudies-literature
Publications
Matrix metalloproteinase interactions with collagen and elastin.
Matrix biology : journal of the International Society for Matrix Biology 20150117
Most abundant in the extracellular matrix are collagens, joined by elastin that confers elastic recoil to the lung, aorta, and skin. These fibrils are highly resistant to proteolysis but can succumb to a minority of the matrix metalloproteinases (MMPs). Considerable inroads to understanding how such MMPs move to the susceptible sites in collagen and then unwind the triple helix of collagen monomers have been gained. The essential role in unwinding of the hemopexin-like domain of interstitial col ...[more]
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