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Structure, regulatory factors and cancer-related physiological effects of ADAM9
The ADAMs family belongs to the transmembrane protein superfamily of zinc-dependent metalloproteases, which consists of multiple domains. These domains have independent but complementary functions that enable them to participate in multiple biological processes. Among them, ADAM9 can not only partic...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Taylor & Francis
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7513870/ https://www.ncbi.nlm.nih.gov/pubmed/32875951 http://dx.doi.org/10.1080/19336918.2020.1817251 |
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author | Haoyuan, MA Yanshu, LI |
author_facet | Haoyuan, MA Yanshu, LI |
author_sort | Haoyuan, MA |
collection | PubMed |
description | The ADAMs family belongs to the transmembrane protein superfamily of zinc-dependent metalloproteases, which consists of multiple domains. These domains have independent but complementary functions that enable them to participate in multiple biological processes. Among them, ADAM9 can not only participate in the degradation of extracellular matrix as a metalloprotease, but also mediate tumor cell adhesion through its deintegrin domain, which is closely related to tumor invasion and metastasis. It is widely expressed in a variety of tumor cells and can affect the proliferation, invasion and metastasis of related cancer cells. We provide our views on current progress, its increasing importance as a strategic treatment goal, and our vision for the future of ADAM9. |
format | Online Article Text |
id | pubmed-7513870 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-75138702020-10-01 Structure, regulatory factors and cancer-related physiological effects of ADAM9 Haoyuan, MA Yanshu, LI Cell Adh Migr Review The ADAMs family belongs to the transmembrane protein superfamily of zinc-dependent metalloproteases, which consists of multiple domains. These domains have independent but complementary functions that enable them to participate in multiple biological processes. Among them, ADAM9 can not only participate in the degradation of extracellular matrix as a metalloprotease, but also mediate tumor cell adhesion through its deintegrin domain, which is closely related to tumor invasion and metastasis. It is widely expressed in a variety of tumor cells and can affect the proliferation, invasion and metastasis of related cancer cells. We provide our views on current progress, its increasing importance as a strategic treatment goal, and our vision for the future of ADAM9. Taylor & Francis 2020-09-12 /pmc/articles/PMC7513870/ /pubmed/32875951 http://dx.doi.org/10.1080/19336918.2020.1817251 Text en © 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Haoyuan, MA Yanshu, LI Structure, regulatory factors and cancer-related physiological effects of ADAM9 |
title | Structure, regulatory factors and cancer-related physiological effects of ADAM9 |
title_full | Structure, regulatory factors and cancer-related physiological effects of ADAM9 |
title_fullStr | Structure, regulatory factors and cancer-related physiological effects of ADAM9 |
title_full_unstemmed | Structure, regulatory factors and cancer-related physiological effects of ADAM9 |
title_short | Structure, regulatory factors and cancer-related physiological effects of ADAM9 |
title_sort | structure, regulatory factors and cancer-related physiological effects of adam9 |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7513870/ https://www.ncbi.nlm.nih.gov/pubmed/32875951 http://dx.doi.org/10.1080/19336918.2020.1817251 |
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