IMR Press / FBL / Volume 11 / Issue 3 / DOI: 10.2741/2036

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Article

Matrix Metalloproteinase Dependent and Independent Collagen Degradation

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1 Department of Oral Biology, Indiana University School of Dentistry, Indianapolis, Indiana 46202
Front. Biosci. (Landmark Ed) 2006, 11(3), 3100–3120; https://doi.org/10.2741/2036
Published: 1 September 2006
Abstract

Cleavage of the fibrillar collagens occurs during physiological conditions, as well as pathological conditions. The resistance of the fibrillar collagens to degradation is due to their rigid and compact structures. There are only a limited number of proteinases that have the capability to initiate the cleavage of the fibrillar collagens. These include some of the matrix metalloproteinases (MMPs) and cathepsins, as well as a few serine proteinases. The MMPs have long been implicated in the collagen degradation and remodeling that occurs at physiological pHs. The cathepsins, on the other hand, have been implicated in the collagen cleavage that occurs at acidic pHs, particularly the collagen degradation that is mediated by osteoclasts. In addition to the MMPs, a few serine proteinases have been implicated in the collagen degradation that occurs at neutral pH. The characteristics that contribute to the resistance of the fibrillar collagens to cleavage are discussed along with the MMPs, cathepsins, and serine proteinases that can cleave these collagens.

Keywords
Fibrillar Collagen
Matrix metalloproteinases
Cathepsins
Serine Proteinases
Review
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