Structure and Function of Human Matrix Metalloproteinases

The extracellular matrix (ECM) is a macromolecules network, in which the most abundant molecule is collagen. This protein in triple helical conformation is highly resistant to proteinases degradation, the only enzymes capable of degrading the collagen are matrix metalloproteinases (MMPs). This resis...

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Detalles Bibliográficos
Autores principales: Laronha, Helena, Caldeira, Jorge
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7290392/
https://www.ncbi.nlm.nih.gov/pubmed/32357580
http://dx.doi.org/10.3390/cells9051076
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author Laronha, Helena
Caldeira, Jorge
author_facet Laronha, Helena
Caldeira, Jorge
author_sort Laronha, Helena
collection PubMed
description The extracellular matrix (ECM) is a macromolecules network, in which the most abundant molecule is collagen. This protein in triple helical conformation is highly resistant to proteinases degradation, the only enzymes capable of degrading the collagen are matrix metalloproteinases (MMPs). This resistance and maintenance of collagen, and consequently of ECM, is involved in several biological processes and it must be strictly regulated by endogenous inhibitors (TIMPs). The deregulation of MMPs activity leads to development of numerous diseases. This review shows MMPs complexity.
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spelling pubmed-72903922020-06-15 Structure and Function of Human Matrix Metalloproteinases Laronha, Helena Caldeira, Jorge Cells Review The extracellular matrix (ECM) is a macromolecules network, in which the most abundant molecule is collagen. This protein in triple helical conformation is highly resistant to proteinases degradation, the only enzymes capable of degrading the collagen are matrix metalloproteinases (MMPs). This resistance and maintenance of collagen, and consequently of ECM, is involved in several biological processes and it must be strictly regulated by endogenous inhibitors (TIMPs). The deregulation of MMPs activity leads to development of numerous diseases. This review shows MMPs complexity. MDPI 2020-04-26 /pmc/articles/PMC7290392/ /pubmed/32357580 http://dx.doi.org/10.3390/cells9051076 Text en © 2020 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
Laronha, Helena
Caldeira, Jorge
Structure and Function of Human Matrix Metalloproteinases
title Structure and Function of Human Matrix Metalloproteinases
title_full Structure and Function of Human Matrix Metalloproteinases
title_fullStr Structure and Function of Human Matrix Metalloproteinases
title_full_unstemmed Structure and Function of Human Matrix Metalloproteinases
title_short Structure and Function of Human Matrix Metalloproteinases
title_sort structure and function of human matrix metalloproteinases
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7290392/
https://www.ncbi.nlm.nih.gov/pubmed/32357580
http://dx.doi.org/10.3390/cells9051076
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