Matrix Metalloproteinases: How Much Can They Do?

Zinc-dependent matrix metalloproteinases (MMPs) belong to metzincins that comprise not only 23 human MMPs but also other metalloproteinases, such as 21 human ADAMs (a disintegrin and metalloproteinase domain) and 19 secreted ADAMTSs (a disintegrin and metalloproteinase thrombospondin domain). The ma...

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Detalles Bibliográficos
Autores principales: Ågren, Magnus S., auf dem Keller, Ulrich
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Editorial
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7215854/
https://www.ncbi.nlm.nih.gov/pubmed/32290531
http://dx.doi.org/10.3390/ijms21082678
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author Ågren, Magnus S.
auf dem Keller, Ulrich
author_facet Ågren, Magnus S.
auf dem Keller, Ulrich
author_sort Ågren, Magnus S.
collection PubMed
description Zinc-dependent matrix metalloproteinases (MMPs) belong to metzincins that comprise not only 23 human MMPs but also other metalloproteinases, such as 21 human ADAMs (a disintegrin and metalloproteinase domain) and 19 secreted ADAMTSs (a disintegrin and metalloproteinase thrombospondin domain). The many setbacks from the clinical trials of broad-spectrum MMP inhibitors for cancer indications in the late 1990s emphasized the extreme complexity of the participation of these proteolytic enzymes in biology. This editorial mini-review summarizes the Special Issue, which includes four review articles and 10 original articles that highlight the versatile roles of MMPs, ADAMs, and ADAMTSs, in normal physiology as well as in neoplastic and destructive processes in tissue. In addition, we briefly discuss the unambiguous involvement of MMPs in wound healing.
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spelling pubmed-72158542020-05-22 Matrix Metalloproteinases: How Much Can They Do? Ågren, Magnus S. auf dem Keller, Ulrich Int J Mol Sci Editorial Zinc-dependent matrix metalloproteinases (MMPs) belong to metzincins that comprise not only 23 human MMPs but also other metalloproteinases, such as 21 human ADAMs (a disintegrin and metalloproteinase domain) and 19 secreted ADAMTSs (a disintegrin and metalloproteinase thrombospondin domain). The many setbacks from the clinical trials of broad-spectrum MMP inhibitors for cancer indications in the late 1990s emphasized the extreme complexity of the participation of these proteolytic enzymes in biology. This editorial mini-review summarizes the Special Issue, which includes four review articles and 10 original articles that highlight the versatile roles of MMPs, ADAMs, and ADAMTSs, in normal physiology as well as in neoplastic and destructive processes in tissue. In addition, we briefly discuss the unambiguous involvement of MMPs in wound healing. MDPI 2020-04-12 /pmc/articles/PMC7215854/ /pubmed/32290531 http://dx.doi.org/10.3390/ijms21082678 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 Editorial
Ågren, Magnus S.
auf dem Keller, Ulrich
Matrix Metalloproteinases: How Much Can They Do?
title Matrix Metalloproteinases: How Much Can They Do?
title_full Matrix Metalloproteinases: How Much Can They Do?
title_fullStr Matrix Metalloproteinases: How Much Can They Do?
title_full_unstemmed Matrix Metalloproteinases: How Much Can They Do?
title_short Matrix Metalloproteinases: How Much Can They Do?
title_sort matrix metalloproteinases: how much can they do?
topic Editorial
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7215854/
https://www.ncbi.nlm.nih.gov/pubmed/32290531
http://dx.doi.org/10.3390/ijms21082678
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