Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1864, Issue 11, Pages 1940-1951Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2017.04.015
Keywords
Arthritis; Collagen; Matrix metalloproteinase; Metastasis; Skeletal defects; Wound healing
Categories
Funding
- National Institutes of Health [CA98799, AR063795, MH078948]
- National Institutes of Health (NHLBI) [268201000036C]
- Multiple Sclerosis National Research Institute
- Robert A. Welch Foundation
- Lustgarten Foundation
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The proteolytic processing of collagen (collagenolysis) is critical in development and homeostasis, but also contributes to numerous pathologies. Mammalian interstitial collagenolytic enzymes include members of the matrix metalloproteinase (MMP) family and cathepsin K. While MMPs have long been recognized for their ability to catalyze the hydrolysis of collagen, the roles of individual MMPs in physiological and pathological collagenolysis are less defined. The use of knockout and mutant animal models, which reflect human diseases, has revealed distinct collagenolytic roles for MT1-MMP and MMP-13. A better understanding of temporal and spatial collagen processing, along with the knowledge of the specific MMP involved, will ultimately lead to more effective treatments for cancer, arthritis, cardiovascular conditions, and infectious diseases. This article is part of a Special Issue entitled: Matrix Metalloproteinases edited by Rafael Fridman.
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