Cargando…
Role of ADAM and ADAMTS metalloproteinases in airway diseases
Lungs are exposed to the outside environment and therefore to toxic and infectious agents or allergens. This may lead to permanent activation of innate immune response elements. A Disintegrin And Metalloproteinases (ADAMs) and ADAMs with Thrombospondin motifs (ADAMTS) are proteinases closely related...
Autores principales: | , , , , , , , , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2805617/ https://www.ncbi.nlm.nih.gov/pubmed/20034386 http://dx.doi.org/10.1186/1465-9921-10-127 |
_version_ | 1782176203625463808 |
---|---|
author | Paulissen, Genevieve Rocks, Natacha Gueders, Maud M Crahay, Celine Quesada-Calvo, Florence Bekaert, Sandrine Hacha, Jonathan El Hour, Mehdi Foidart, Jean-Michel Noel, Agnes Cataldo, Didier D |
author_facet | Paulissen, Genevieve Rocks, Natacha Gueders, Maud M Crahay, Celine Quesada-Calvo, Florence Bekaert, Sandrine Hacha, Jonathan El Hour, Mehdi Foidart, Jean-Michel Noel, Agnes Cataldo, Didier D |
author_sort | Paulissen, Genevieve |
collection | PubMed |
description | Lungs are exposed to the outside environment and therefore to toxic and infectious agents or allergens. This may lead to permanent activation of innate immune response elements. A Disintegrin And Metalloproteinases (ADAMs) and ADAMs with Thrombospondin motifs (ADAMTS) are proteinases closely related to Matrix Metalloproteinases (MMPs). These multifaceted molecules bear metalloproteinase and disintegrin domains endowing them with features of both proteinases and adhesion molecules. Proteinases of the ADAM family are associated to various physiological and pathological processes and display a wide spectrum of biological effects encompassing cell fusion, cell adhesion, "shedding process", cleavage of various substrates from the extracellular matrix, growth factors or cytokines... This review will focus on the putative roles of ADAM/ADAMTS proteinases in airway diseases such as asthma and COPD. |
format | Text |
id | pubmed-2805617 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-28056172010-01-13 Role of ADAM and ADAMTS metalloproteinases in airway diseases Paulissen, Genevieve Rocks, Natacha Gueders, Maud M Crahay, Celine Quesada-Calvo, Florence Bekaert, Sandrine Hacha, Jonathan El Hour, Mehdi Foidart, Jean-Michel Noel, Agnes Cataldo, Didier D Respir Res Review Lungs are exposed to the outside environment and therefore to toxic and infectious agents or allergens. This may lead to permanent activation of innate immune response elements. A Disintegrin And Metalloproteinases (ADAMs) and ADAMs with Thrombospondin motifs (ADAMTS) are proteinases closely related to Matrix Metalloproteinases (MMPs). These multifaceted molecules bear metalloproteinase and disintegrin domains endowing them with features of both proteinases and adhesion molecules. Proteinases of the ADAM family are associated to various physiological and pathological processes and display a wide spectrum of biological effects encompassing cell fusion, cell adhesion, "shedding process", cleavage of various substrates from the extracellular matrix, growth factors or cytokines... This review will focus on the putative roles of ADAM/ADAMTS proteinases in airway diseases such as asthma and COPD. BioMed Central 2009 2009-12-24 /pmc/articles/PMC2805617/ /pubmed/20034386 http://dx.doi.org/10.1186/1465-9921-10-127 Text en Copyright ©2009 Paulissen et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Paulissen, Genevieve Rocks, Natacha Gueders, Maud M Crahay, Celine Quesada-Calvo, Florence Bekaert, Sandrine Hacha, Jonathan El Hour, Mehdi Foidart, Jean-Michel Noel, Agnes Cataldo, Didier D Role of ADAM and ADAMTS metalloproteinases in airway diseases |
title | Role of ADAM and ADAMTS metalloproteinases in airway diseases |
title_full | Role of ADAM and ADAMTS metalloproteinases in airway diseases |
title_fullStr | Role of ADAM and ADAMTS metalloproteinases in airway diseases |
title_full_unstemmed | Role of ADAM and ADAMTS metalloproteinases in airway diseases |
title_short | Role of ADAM and ADAMTS metalloproteinases in airway diseases |
title_sort | role of adam and adamts metalloproteinases in airway diseases |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2805617/ https://www.ncbi.nlm.nih.gov/pubmed/20034386 http://dx.doi.org/10.1186/1465-9921-10-127 |
work_keys_str_mv | AT paulissengenevieve roleofadamandadamtsmetalloproteinasesinairwaydiseases AT rocksnatacha roleofadamandadamtsmetalloproteinasesinairwaydiseases AT guedersmaudm roleofadamandadamtsmetalloproteinasesinairwaydiseases AT crahayceline roleofadamandadamtsmetalloproteinasesinairwaydiseases AT quesadacalvoflorence roleofadamandadamtsmetalloproteinasesinairwaydiseases AT bekaertsandrine roleofadamandadamtsmetalloproteinasesinairwaydiseases AT hachajonathan roleofadamandadamtsmetalloproteinasesinairwaydiseases AT elhourmehdi roleofadamandadamtsmetalloproteinasesinairwaydiseases AT foidartjeanmichel roleofadamandadamtsmetalloproteinasesinairwaydiseases AT noelagnes roleofadamandadamtsmetalloproteinasesinairwaydiseases AT cataldodidierd roleofadamandadamtsmetalloproteinasesinairwaydiseases |