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Biochim Biophys Acta Mol Cell Res. 2017 Nov;1864(11 Pt A):1940-1951. doi: 10.1016/j.bbamcr.2017.04.015. Epub 2017 Apr 26.

Matrix metalloproteinase collagenolysis in health and disease.

Author information

1
Department of Chemistry & Biochemistry, Florida Atlantic University, Jupiter, FL 33458, USA. Electronic address: samar@fau.edu.
2
Department of Chemistry & Biochemistry, Florida Atlantic University, Jupiter, FL 33458, USA. Electronic address: lyndsaysmith2015@fau.edu.
3
Department of Chemistry & Biochemistry, Florida Atlantic University, Jupiter, FL 33458, USA; Department of Chemistry, The Scripps Research Institute/Scripps Florida, Jupiter, FL 33458, USA. Electronic address: fieldsg@fau.edu.

Abstract

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.

KEYWORDS:

Arthritis; Collagen; Matrix metalloproteinase; Metastasis; Skeletal defects; Wound healing

PMID:
28456643
PMCID:
PMC5605394
DOI:
10.1016/j.bbamcr.2017.04.015
[Indexed for MEDLINE]
Free PMC Article

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