Department of Chemistry & Biochemistry, Florida Atlantic University, Jupiter, FL 33458, USA.
Department of Chemistry & Biochemistry, Florida Atlantic University, Jupiter, FL 33458, USA; Department of Chemistry, The Scripps Research Institute/Scripps Florida, Jupiter, FL 33458, USA.
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.
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.
胶原的蛋白水解加工(胶原降解)在发育和动态平衡中至关重要,但也会导致许多病理情况。哺乳动物间质胶原降解酶包括基质金属蛋白酶(MMP)家族和组织蛋白酶 K 的成员。尽管 MMP 早已因其能够催化胶原水解的能力而被人们所认识,但在生理和病理胶原降解中单个 MMP 的作用却不太明确。利用反映人类疾病的基因敲除和突变动物模型揭示了 MT1-MMP 和 MMP-13 的独特胶原降解作用。更好地理解时空胶原加工以及涉及的特定 MMP 的知识,最终将为癌症、关节炎、心血管疾病和传染病的更有效治疗方法提供帮助。本文是由 Rafael Fridman 编辑的题为“基质金属蛋白酶”的特刊的一部分。