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The role of thrombomodulin lectin-like domain in inflammation

Thrombomodulin (TM) is a cell surface glycoprotein which is widely expressed in a variety of cell types. It is a cofactor for thrombin binding that mediates protein C activation and inhibits thrombin activity. In addition to its anticoagulant activity, recent evidence has revealed that TM, especiall...

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Detalles Bibliográficos
Autores principales: Li, Yi-Heng, Kuo, Cheng-Hsiang, Shi, Guey-Yueh, Wu, Hua-Lin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3342133/
https://www.ncbi.nlm.nih.gov/pubmed/22449172
http://dx.doi.org/10.1186/1423-0127-19-34
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author Li, Yi-Heng
Kuo, Cheng-Hsiang
Shi, Guey-Yueh
Wu, Hua-Lin
author_facet Li, Yi-Heng
Kuo, Cheng-Hsiang
Shi, Guey-Yueh
Wu, Hua-Lin
author_sort Li, Yi-Heng
collection PubMed
description Thrombomodulin (TM) is a cell surface glycoprotein which is widely expressed in a variety of cell types. It is a cofactor for thrombin binding that mediates protein C activation and inhibits thrombin activity. In addition to its anticoagulant activity, recent evidence has revealed that TM, especially its lectin-like domain, has potent anti-inflammatory function through a variety of molecular mechanisms. The lectin-like domain of TM plays an important role in suppressing inflammation independent of the TM anticoagulant activity. This article makes an extensive review of the role of TM in inflammation. The molecular targets of TM lectin-like domain have also been elucidated. Recombinant TM protein, especially the TM lectin-like domain may play a promising role in the management of sepsis, glomerulonephritis and arthritis. These data demonstrated the potential therapeutic role of TM in the treatment of inflammatory diseases.
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spelling pubmed-33421332012-05-03 The role of thrombomodulin lectin-like domain in inflammation Li, Yi-Heng Kuo, Cheng-Hsiang Shi, Guey-Yueh Wu, Hua-Lin J Biomed Sci Review Thrombomodulin (TM) is a cell surface glycoprotein which is widely expressed in a variety of cell types. It is a cofactor for thrombin binding that mediates protein C activation and inhibits thrombin activity. In addition to its anticoagulant activity, recent evidence has revealed that TM, especially its lectin-like domain, has potent anti-inflammatory function through a variety of molecular mechanisms. The lectin-like domain of TM plays an important role in suppressing inflammation independent of the TM anticoagulant activity. This article makes an extensive review of the role of TM in inflammation. The molecular targets of TM lectin-like domain have also been elucidated. Recombinant TM protein, especially the TM lectin-like domain may play a promising role in the management of sepsis, glomerulonephritis and arthritis. These data demonstrated the potential therapeutic role of TM in the treatment of inflammatory diseases. BioMed Central 2012-03-27 /pmc/articles/PMC3342133/ /pubmed/22449172 http://dx.doi.org/10.1186/1423-0127-19-34 Text en Copyright ©2012 Li 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
Li, Yi-Heng
Kuo, Cheng-Hsiang
Shi, Guey-Yueh
Wu, Hua-Lin
The role of thrombomodulin lectin-like domain in inflammation
title The role of thrombomodulin lectin-like domain in inflammation
title_full The role of thrombomodulin lectin-like domain in inflammation
title_fullStr The role of thrombomodulin lectin-like domain in inflammation
title_full_unstemmed The role of thrombomodulin lectin-like domain in inflammation
title_short The role of thrombomodulin lectin-like domain in inflammation
title_sort role of thrombomodulin lectin-like domain in inflammation
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3342133/
https://www.ncbi.nlm.nih.gov/pubmed/22449172
http://dx.doi.org/10.1186/1423-0127-19-34
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