Unknown

Dataset Information

0

Matrix metalloproteinase collagenolysis in health and disease.


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.

SUBMITTER: Amar S 

PROVIDER: S-EPMC5605394 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Matrix metalloproteinase collagenolysis in health and disease.

Amar Sabrina S   Smith Lyndsay L   Fields Gregg B GB  

Biochimica et biophysica acta. Molecular cell research 20170426 11 Pt A


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 m  ...[more]

Similar Datasets

| S-EPMC3298817 | biostudies-literature
| S-EPMC3798536 | biostudies-literature
| S-EPMC4824997 | biostudies-literature
| S-EPMC9018075 | biostudies-literature
| S-EPMC4302670 | biostudies-literature
2016-03-21 | GSE78174 | GEO
2023-02-24 | GSE202662 | GEO
| S-EPMC4960106 | biostudies-literature
| S-EPMC5617391 | biostudies-literature
| S-EPMC3463216 | biostudies-literature