Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases

International Journal of Molecular Sciences

Ulrich auf dem Keller¹  Fabio Sabino¹  Elizabeta Madzharova¹  Philipp Kastl¹ 

[1] Department of Biotechnology and Biomedicine, Technical University of Denmark, DK-2800 Kongens Lyngby, Denmark;

关键词: MMPs;    PTMs;    glycosylation;    phosphorylation;    glycosaminoglycans;   

DOI  :  10.3390/ijms20123077

来源: DOAJ

【 摘 要 】

Due to their capacity to process different proteins of the extracellular matrix (ECM), matrix metalloproteinases (MMPs) were initially described as a family of secreted proteases, functioning as main ECM regulators. However, through proteolytic processing of various biomolecules, MMPs also modulate intra- and extracellular pathways and networks. Thereby, they are functionally implicated in the regulation of multiple physiological and pathological processes. Consequently, MMP activity is tightly regulated through a combination of epigenetic, transcriptional, and post-transcriptional control of gene expression, proteolytic activation, post-translational modifications (PTMs), and extracellular inhibition. In addition, MMPs, their substrates and ECM binding partners are frequently modified by PTMs, which suggests an important role of PTMs in modulating the pleiotropic activities of these proteases. This review summarizes the recent progress towards understanding the role of PTMs (glycosylation, phosphorylation, glycosaminoglycans) on the activity of several members of the MMP family.

【 授权许可】

Unknown