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MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms
Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a type I transmembrane proteinase that belongs to the matrix metalloproteinase (MMP) family. It is a potent modifier of cellular microenvironment and promotes cell migration and invasion of a wide variety of cell types both in physiological and p...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6599156/ https://www.ncbi.nlm.nih.gov/pubmed/31064864 http://dx.doi.org/10.1042/BST20180363 |
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author | Gifford, Valentina Itoh, Yoshifumi |
author_facet | Gifford, Valentina Itoh, Yoshifumi |
author_sort | Gifford, Valentina |
collection | PubMed |
description | Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a type I transmembrane proteinase that belongs to the matrix metalloproteinase (MMP) family. It is a potent modifier of cellular microenvironment and promotes cell migration and invasion of a wide variety of cell types both in physiological and pathological conditions. It promotes cell migration by degrading extracellular matrix on the cell surface and creates a migration path, by modifying cell adhesion property by shedding cell adhesion molecules to increase cell motility, and by altering cellular metabolism. Thus, MT1-MMP is a multifunctional cell motility enhancer. In this review, we will discuss the current understanding of the proteolytic and non-proteolytic mechanism of MT1-MMP-dependent cell migration. |
format | Online Article Text |
id | pubmed-6599156 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-65991562019-07-08 MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms Gifford, Valentina Itoh, Yoshifumi Biochem Soc Trans Review Articles Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a type I transmembrane proteinase that belongs to the matrix metalloproteinase (MMP) family. It is a potent modifier of cellular microenvironment and promotes cell migration and invasion of a wide variety of cell types both in physiological and pathological conditions. It promotes cell migration by degrading extracellular matrix on the cell surface and creates a migration path, by modifying cell adhesion property by shedding cell adhesion molecules to increase cell motility, and by altering cellular metabolism. Thus, MT1-MMP is a multifunctional cell motility enhancer. In this review, we will discuss the current understanding of the proteolytic and non-proteolytic mechanism of MT1-MMP-dependent cell migration. Portland Press Ltd. 2019-06-28 2019-05-07 /pmc/articles/PMC6599156/ /pubmed/31064864 http://dx.doi.org/10.1042/BST20180363 Text en © 2019 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Review Articles Gifford, Valentina Itoh, Yoshifumi MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms |
title | MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms |
title_full | MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms |
title_fullStr | MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms |
title_full_unstemmed | MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms |
title_short | MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms |
title_sort | mt1-mmp-dependent cell migration: proteolytic and non-proteolytic mechanisms |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6599156/ https://www.ncbi.nlm.nih.gov/pubmed/31064864 http://dx.doi.org/10.1042/BST20180363 |
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