Journal
MATRIX BIOLOGY
Volume 44-46, Issue -, Pages 224-231Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.matbio.2015.01.005
Keywords
Collagen triple helix; Elastin; Exosite; Matrix metalloproteinases
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Funding
- National Institute of General Medical Sciences of the NIH [R01GM057289]
- National Cancer Institute of the NIH [R01CA098799]
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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 collagenases or the collagen binding domain of gelatinases is highlighted. Elastolysis is also facilitated by the collagen binding domain in the cases of MMP-2 and MMP-9, and remote exosites of the catalytic domain in the case of MMP-12. (C) 2015 Published by Elsevier
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