Structure and Function of Human Matrix Metalloproteinases.


Journal

Cells
ISSN: 2073-4409
Titre abrégé: Cells
Pays: Switzerland
ID NLM: 101600052

Informations de publication

Date de publication:
26 04 2020
Historique:
received: 12 03 2020
revised: 15 04 2020
accepted: 21 04 2020
entrez: 3 5 2020
pubmed: 3 5 2020
medline: 17 3 2021
Statut: epublish

Résumé

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.

Identifiants

pubmed: 32357580
pii: cells9051076
doi: 10.3390/cells9051076
pmc: PMC7290392
pii:
doi:

Substances chimiques

Matrix Metalloproteinase Inhibitors 0
Collagen 9007-34-5
Matrix Metalloproteinases EC 3.4.24.-

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

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Auteurs

Helena Laronha (H)

Centro de investigação interdisciplinar Egas Moniz, Instituto Universitário Egas Moniz, 2829 Caparica, Portugal.
UCIBIO and LAQV Requimte Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.

Jorge Caldeira (J)

Centro de investigação interdisciplinar Egas Moniz, Instituto Universitário Egas Moniz, 2829 Caparica, Portugal.
UCIBIO and LAQV Requimte Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.

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Classifications MeSH