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Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases
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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6627178/ https://www.ncbi.nlm.nih.gov/pubmed/31238509 http://dx.doi.org/10.3390/ijms20123077 |
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author | Madzharova, Elizabeta Kastl, Philipp Sabino, Fabio auf dem Keller, Ulrich |
author_facet | Madzharova, Elizabeta Kastl, Philipp Sabino, Fabio auf dem Keller, Ulrich |
author_sort | Madzharova, Elizabeta |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6627178 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-66271782019-07-19 Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases Madzharova, Elizabeta Kastl, Philipp Sabino, Fabio auf dem Keller, Ulrich Int J Mol Sci Review 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. MDPI 2019-06-24 /pmc/articles/PMC6627178/ /pubmed/31238509 http://dx.doi.org/10.3390/ijms20123077 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Madzharova, Elizabeta Kastl, Philipp Sabino, Fabio auf dem Keller, Ulrich Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases |
title | Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases |
title_full | Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases |
title_fullStr | Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases |
title_full_unstemmed | Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases |
title_short | Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases |
title_sort | post-translational modification-dependent activity of matrix metalloproteinases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6627178/ https://www.ncbi.nlm.nih.gov/pubmed/31238509 http://dx.doi.org/10.3390/ijms20123077 |
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