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Extracellular cyclophilin A possesses chemotaxic activity in cattle
Cyclophilin A (CyPA) was originally discovered in bovine thymocytes as a cytosolic binding protein of the immunosuppressive drug cyclosporine A. Recent studies have revealed that in mice and humans, CyPA is secreted from cells in injured or infected tissues and plays a role in recruiting inflammator...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4498507/ https://www.ncbi.nlm.nih.gov/pubmed/26163364 http://dx.doi.org/10.1186/s13567-015-0212-1 |
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author | Takanashi, Satoru Nochi, Tomonori Abe, Miku Itaya, Nanami Urakawa, Megumi Sato, Katsuyoshi Zhuang, Tao Umemura, Saori Hayashi, Tomohito Kiku, Yoshio Kitazawa, Haruki Rose, Michael T. Watanabe, Kouichi Aso, Hisashi |
author_facet | Takanashi, Satoru Nochi, Tomonori Abe, Miku Itaya, Nanami Urakawa, Megumi Sato, Katsuyoshi Zhuang, Tao Umemura, Saori Hayashi, Tomohito Kiku, Yoshio Kitazawa, Haruki Rose, Michael T. Watanabe, Kouichi Aso, Hisashi |
author_sort | Takanashi, Satoru |
collection | PubMed |
description | Cyclophilin A (CyPA) was originally discovered in bovine thymocytes as a cytosolic binding protein of the immunosuppressive drug cyclosporine A. Recent studies have revealed that in mice and humans, CyPA is secreted from cells in injured or infected tissues and plays a role in recruiting inflammatory cells in those tissues. Here we found that in cattle abundant level of extracellular CyPA was observed in tissues with inflammation. To aid in investigating the role of extracellular CyPA in cattle, we generated recombinant bovine CyPA (rbCyPA) and tested its biological activity as an inflammatory mediator. When bovine peripheral blood cells were treated with rbCyPA in vitro, we observed that rbCyPA reacts with the membranous surface of granulocytes, monocytes and lymphocytes. Chemotaxis analysis showed that the granulocytes migrate toward rbCyPA and the migration is inhibited by pre-treatment with an anti-bovine CyPA antibody. These results indicate that, as for mice and humans, extracellular CyPA possesses chemotactic activity to recruit inflammatory cells (e.g., granulocytes) in cattle, and could thus be a potential therapeutic target for the treatment of inflammation. |
format | Online Article Text |
id | pubmed-4498507 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-44985072015-07-11 Extracellular cyclophilin A possesses chemotaxic activity in cattle Takanashi, Satoru Nochi, Tomonori Abe, Miku Itaya, Nanami Urakawa, Megumi Sato, Katsuyoshi Zhuang, Tao Umemura, Saori Hayashi, Tomohito Kiku, Yoshio Kitazawa, Haruki Rose, Michael T. Watanabe, Kouichi Aso, Hisashi Vet Res Research Article Cyclophilin A (CyPA) was originally discovered in bovine thymocytes as a cytosolic binding protein of the immunosuppressive drug cyclosporine A. Recent studies have revealed that in mice and humans, CyPA is secreted from cells in injured or infected tissues and plays a role in recruiting inflammatory cells in those tissues. Here we found that in cattle abundant level of extracellular CyPA was observed in tissues with inflammation. To aid in investigating the role of extracellular CyPA in cattle, we generated recombinant bovine CyPA (rbCyPA) and tested its biological activity as an inflammatory mediator. When bovine peripheral blood cells were treated with rbCyPA in vitro, we observed that rbCyPA reacts with the membranous surface of granulocytes, monocytes and lymphocytes. Chemotaxis analysis showed that the granulocytes migrate toward rbCyPA and the migration is inhibited by pre-treatment with an anti-bovine CyPA antibody. These results indicate that, as for mice and humans, extracellular CyPA possesses chemotactic activity to recruit inflammatory cells (e.g., granulocytes) in cattle, and could thus be a potential therapeutic target for the treatment of inflammation. BioMed Central 2015-07-11 2015 /pmc/articles/PMC4498507/ /pubmed/26163364 http://dx.doi.org/10.1186/s13567-015-0212-1 Text en © Takanashi et al. 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Takanashi, Satoru Nochi, Tomonori Abe, Miku Itaya, Nanami Urakawa, Megumi Sato, Katsuyoshi Zhuang, Tao Umemura, Saori Hayashi, Tomohito Kiku, Yoshio Kitazawa, Haruki Rose, Michael T. Watanabe, Kouichi Aso, Hisashi Extracellular cyclophilin A possesses chemotaxic activity in cattle |
title | Extracellular cyclophilin A possesses chemotaxic activity in cattle |
title_full | Extracellular cyclophilin A possesses chemotaxic activity in cattle |
title_fullStr | Extracellular cyclophilin A possesses chemotaxic activity in cattle |
title_full_unstemmed | Extracellular cyclophilin A possesses chemotaxic activity in cattle |
title_short | Extracellular cyclophilin A possesses chemotaxic activity in cattle |
title_sort | extracellular cyclophilin a possesses chemotaxic activity in cattle |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4498507/ https://www.ncbi.nlm.nih.gov/pubmed/26163364 http://dx.doi.org/10.1186/s13567-015-0212-1 |
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