TY - JOUR
T1 - Extracellular cyclophilin A possesses chemotaxic activity in cattle
AU - Takanashi, Satoru
AU - Nochi, Tomonori
AU - Abe, Miku
AU - Itaya, Nanami
AU - Urakawa, Megumi
AU - Sato, Katsuyoshi
AU - Zhuang, Tao
AU - Umemura, Saori
AU - Hayashi, Tomohito
AU - Kiku, Yoshio
AU - Kitazawa, Haruki
AU - Rose, Michael T.
AU - Watanabe, Kouichi
AU - Aso, Hisashi
N1 - Funding Information:
We thank Dr T. Uchida, Graduate School of Agricultural Science, Tohoku University, for the use of flow cytometry. We also thank Calpis Co., Ltd., for contribution. This work was supported in part by KAKENHI from the Japan Society for the Promotion of Science (grant numbers: 26660217 to HA and 26660245 to TN) and by research program on innovative technologies for animal breeding, reproduction and vaccine development from the Ministry of Agriculture, Forestry and Fisheries of Japan (to TH, YK, HA and TN).
Publisher Copyright:
© 2015 Takanashi et al.
PY - 2015/7/11
Y1 - 2015/7/11
N2 - 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.
AB - 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.
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U2 - 10.1186/s13567-015-0212-1
DO - 10.1186/s13567-015-0212-1
M3 - Article
C2 - 26163364
AN - SCOPUS:84936851781
SN - 0928-4249
VL - 46
JO - Annales de Recherches Veterinaires
JF - Annales de Recherches Veterinaires
IS - 1
M1 - 80
ER -