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Structural and functional diversity of collectins and ficolins and their relationship to disease
Pattern recognition molecules are sensors for the innate immune system and trigger a number of pathophysiological functions after interaction with the corresponding ligands on microorganisms or altered mammalian cells. Of those pattern recognition molecules used by the complement system, collagen-li...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5794833/ https://www.ncbi.nlm.nih.gov/pubmed/28894916 http://dx.doi.org/10.1007/s00281-017-0642-0 |
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author | Howard, Mark Farrar, Conrad A. Sacks, Steven H. |
author_facet | Howard, Mark Farrar, Conrad A. Sacks, Steven H. |
author_sort | Howard, Mark |
collection | PubMed |
description | Pattern recognition molecules are sensors for the innate immune system and trigger a number of pathophysiological functions after interaction with the corresponding ligands on microorganisms or altered mammalian cells. Of those pattern recognition molecules used by the complement system, collagen-like lectins (collectins) are an important subcomponent. Whereas the best known of these collectins, mannose-binding lectin, largely occurs as a circulating protein following production by hepatocytes, the most recently described collectins exhibit strong local biosynthesis. This local production and release of soluble collectin molecules appear to serve local tissue functions at extravascular sites, including a developmental function. In this article, we focus on the characteristics of collectin-11 (CL-11 or CL-K1), whose ubiquitous expression and multiple activities likely reflect a wide biological relevance. Collectin-11 appears to behave as an acute phase protein whose production associated with metabolic and physical stress results in locally targeted inflammation and tissue cell death. Early results indicate the importance of fucosylated ligand marking the injured cells targeted by collectin-11, and we suggest that further characterisation of this and related ligands will lead to better understanding of pathophysiological significance and exploitation for clinical benefit. |
format | Online Article Text |
id | pubmed-5794833 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
spelling | pubmed-57948332018-02-05 Structural and functional diversity of collectins and ficolins and their relationship to disease Howard, Mark Farrar, Conrad A. Sacks, Steven H. Semin Immunopathol Review Pattern recognition molecules are sensors for the innate immune system and trigger a number of pathophysiological functions after interaction with the corresponding ligands on microorganisms or altered mammalian cells. Of those pattern recognition molecules used by the complement system, collagen-like lectins (collectins) are an important subcomponent. Whereas the best known of these collectins, mannose-binding lectin, largely occurs as a circulating protein following production by hepatocytes, the most recently described collectins exhibit strong local biosynthesis. This local production and release of soluble collectin molecules appear to serve local tissue functions at extravascular sites, including a developmental function. In this article, we focus on the characteristics of collectin-11 (CL-11 or CL-K1), whose ubiquitous expression and multiple activities likely reflect a wide biological relevance. Collectin-11 appears to behave as an acute phase protein whose production associated with metabolic and physical stress results in locally targeted inflammation and tissue cell death. Early results indicate the importance of fucosylated ligand marking the injured cells targeted by collectin-11, and we suggest that further characterisation of this and related ligands will lead to better understanding of pathophysiological significance and exploitation for clinical benefit. Springer Berlin Heidelberg 2017-09-11 2018 /pmc/articles/PMC5794833/ /pubmed/28894916 http://dx.doi.org/10.1007/s00281-017-0642-0 Text en © The Author(s) 2017 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Review Howard, Mark Farrar, Conrad A. Sacks, Steven H. Structural and functional diversity of collectins and ficolins and their relationship to disease |
title | Structural and functional diversity of collectins and ficolins and their relationship to disease |
title_full | Structural and functional diversity of collectins and ficolins and their relationship to disease |
title_fullStr | Structural and functional diversity of collectins and ficolins and their relationship to disease |
title_full_unstemmed | Structural and functional diversity of collectins and ficolins and their relationship to disease |
title_short | Structural and functional diversity of collectins and ficolins and their relationship to disease |
title_sort | structural and functional diversity of collectins and ficolins and their relationship to disease |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5794833/ https://www.ncbi.nlm.nih.gov/pubmed/28894916 http://dx.doi.org/10.1007/s00281-017-0642-0 |
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