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Deformation-Dependent Enzyme Cleavage of Collagen

[+] Author Affiliations
Karla E.-K. Wyatt

City College of New York, New York, NY

Jonathan W. Bourne

Cornell University, New York, NY

Peter A. Torzilli

Hospital for Special Surgery, New York, NY

Paper No. SBC2007-176502, pp. 785-786; 2 pages
doi:10.1115/SBC2007-176502
From:
  • ASME 2007 Summer Bioengineering Conference
  • ASME 2007 Summer Bioengineering Conference
  • Keystone, Colorado, USA, June 20–24, 2007
  • Conference Sponsors: Bioengineering Division
  • ISBN: 0-7918-4798-5
  • Copyright © 2007 by ASME

abstract

Collagen degradation is a mechanism for normal musculoskeletal development and extracellular matrix (ECM) maintenance, and in response to trauma, disease and inflammation. Matrix metalloproteinases (MMP-1, 8, and 13, the collagenases) are the primary enzymes that act to degrade collagen. These MMPs gain access to the collagen triple helix by binding to the enzyme’s attachment domain along the α-chains, followed by separation (unwinding) of the α-chains to expose the 3/4–1/4 cleavage site, and then cleavage of the α-chain by the enzyme’s catalytic domain [3, 5].

Copyright © 2007 by ASME
Topics: Deformation , Enzymes

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