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A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions
Since the discovery of the first disintegrin protein from snake venom and the following identification of a mammalian membrane-anchored metalloprotease-disintegrin implicated in fertilization, almost three decades of studies have identified additional members of these families and several biochemica...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4848645/ https://www.ncbi.nlm.nih.gov/pubmed/27120619 http://dx.doi.org/10.3390/toxins8040122 |
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author | Giebeler, Nives Zigrino, Paola |
author_facet | Giebeler, Nives Zigrino, Paola |
author_sort | Giebeler, Nives |
collection | PubMed |
description | Since the discovery of the first disintegrin protein from snake venom and the following identification of a mammalian membrane-anchored metalloprotease-disintegrin implicated in fertilization, almost three decades of studies have identified additional members of these families and several biochemical mechanisms regulating their expression and activity in the cell. Most importantly, new in vivo functions have been recognized for these proteins including cell partitioning during development, modulation of inflammatory reactions, and development of cancers. In this review, we will overview the a disintegrin and metalloprotease (ADAM) family of proteases highlighting some of the major research achievements in the analysis of ADAMs’ function that have underscored the importance of these proteins in physiological and pathological processes over the years. |
format | Online Article Text |
id | pubmed-4848645 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-48486452016-05-04 A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions Giebeler, Nives Zigrino, Paola Toxins (Basel) Review Since the discovery of the first disintegrin protein from snake venom and the following identification of a mammalian membrane-anchored metalloprotease-disintegrin implicated in fertilization, almost three decades of studies have identified additional members of these families and several biochemical mechanisms regulating their expression and activity in the cell. Most importantly, new in vivo functions have been recognized for these proteins including cell partitioning during development, modulation of inflammatory reactions, and development of cancers. In this review, we will overview the a disintegrin and metalloprotease (ADAM) family of proteases highlighting some of the major research achievements in the analysis of ADAMs’ function that have underscored the importance of these proteins in physiological and pathological processes over the years. MDPI 2016-04-23 /pmc/articles/PMC4848645/ /pubmed/27120619 http://dx.doi.org/10.3390/toxins8040122 Text en © 2016 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 Giebeler, Nives Zigrino, Paola A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions |
title | A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions |
title_full | A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions |
title_fullStr | A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions |
title_full_unstemmed | A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions |
title_short | A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions |
title_sort | disintegrin and metalloprotease (adam): historical overview of their functions |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4848645/ https://www.ncbi.nlm.nih.gov/pubmed/27120619 http://dx.doi.org/10.3390/toxins8040122 |
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