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Snake Venom Disintegrins and Cell Migration
Cell migration is a key process for the defense of pluricellular organisms against pathogens, and it involves a set of surface receptors acting in an ordered fashion to contribute directionality to the movement. Among these receptors are the integrins, which connect the cell cytoskeleton to the extr...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153172/ https://www.ncbi.nlm.nih.gov/pubmed/22069567 http://dx.doi.org/10.3390/toxins2112606 |
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author | Selistre-de-Araujo, Heloisa S. Pontes, Carmen L. S. Montenegro, Cyntia F. Martin, Ana Carolina B. M. |
author_facet | Selistre-de-Araujo, Heloisa S. Pontes, Carmen L. S. Montenegro, Cyntia F. Martin, Ana Carolina B. M. |
author_sort | Selistre-de-Araujo, Heloisa S. |
collection | PubMed |
description | Cell migration is a key process for the defense of pluricellular organisms against pathogens, and it involves a set of surface receptors acting in an ordered fashion to contribute directionality to the movement. Among these receptors are the integrins, which connect the cell cytoskeleton to the extracellular matrix components, thus playing a central role in cell migration. Integrin clustering at focal adhesions drives actin polymerization along the cell leading edge, resulting in polarity of cell movement. Therefore, small integrin-binding proteins such as the snake venom disintegrins that inhibit integrin-mediated cell adhesion are expected to inhibit cell migration. Here we review the current knowledge on disintegrin and disintegrin-like protein effects on cell migration and their potential use as pharmacological tools in anti-inflammatory therapy as well as in inhibition of metastatic invasion. |
format | Online Article Text |
id | pubmed-3153172 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-31531722011-11-08 Snake Venom Disintegrins and Cell Migration Selistre-de-Araujo, Heloisa S. Pontes, Carmen L. S. Montenegro, Cyntia F. Martin, Ana Carolina B. M. Toxins (Basel) Review Cell migration is a key process for the defense of pluricellular organisms against pathogens, and it involves a set of surface receptors acting in an ordered fashion to contribute directionality to the movement. Among these receptors are the integrins, which connect the cell cytoskeleton to the extracellular matrix components, thus playing a central role in cell migration. Integrin clustering at focal adhesions drives actin polymerization along the cell leading edge, resulting in polarity of cell movement. Therefore, small integrin-binding proteins such as the snake venom disintegrins that inhibit integrin-mediated cell adhesion are expected to inhibit cell migration. Here we review the current knowledge on disintegrin and disintegrin-like protein effects on cell migration and their potential use as pharmacological tools in anti-inflammatory therapy as well as in inhibition of metastatic invasion. MDPI 2010-10-29 /pmc/articles/PMC3153172/ /pubmed/22069567 http://dx.doi.org/10.3390/toxins2112606 Text en © 2010 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Review Selistre-de-Araujo, Heloisa S. Pontes, Carmen L. S. Montenegro, Cyntia F. Martin, Ana Carolina B. M. Snake Venom Disintegrins and Cell Migration |
title | Snake Venom Disintegrins and Cell Migration |
title_full | Snake Venom Disintegrins and Cell Migration |
title_fullStr | Snake Venom Disintegrins and Cell Migration |
title_full_unstemmed | Snake Venom Disintegrins and Cell Migration |
title_short | Snake Venom Disintegrins and Cell Migration |
title_sort | snake venom disintegrins and cell migration |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3153172/ https://www.ncbi.nlm.nih.gov/pubmed/22069567 http://dx.doi.org/10.3390/toxins2112606 |
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