FKBP的白细胞趋化活性及FK506对其的抑制作用。

Leukocyte chemotactic activity of FKBP and inhibition by FK506.

作者信息

Leiva M C, Lyttle C R

机构信息

Department of Obstetrics and Gynecology, University of Pennsylvania, Philadelphia 19104.

出版信息

Biochem Biophys Res Commun. 1992 Jul 31;186(2):1178-83. doi: 10.1016/0006-291x(92)90871-h.

DOI:10.1016/0006-291x(92)90871-h

PMID:1379802

Abstract

Cyclophilin, the cyclosporin A binding protein and member of the immunophilin family of proteins, demonstrates leukocyte chemotactic activity. In this study we demonstrate that FKBP, the FK506 and rapamycin binding protein, also displays leukocyte chemotactic activity. The chemotactic activity of FKBP is inhibited by FK506, however, FK506 was unable to inhibit cyclophilin-stimulated chemotactic activity. Rapamycin was unable to prevent the chemotactic activity of FKBP, similarly, the CsA analogue Me6Ala-CsA while displaying cyclophilin binding was unable to block cyclophilin-stimulated chemotactic activity. These results suggest that in addition to their intracellular role the immunophilins may also function as chemotactic agents, furthermore this activity is modulated by immunosuppressants.

摘要

亲环蛋白是环孢素A结合蛋白，属于亲免素蛋白家族成员，具有白细胞趋化活性。在本研究中，我们证明FKBP（FK506和雷帕霉素结合蛋白）也表现出白细胞趋化活性。FKBP的趋化活性被FK506抑制，然而，FK506无法抑制亲环蛋白刺激的趋化活性。雷帕霉素无法阻止FKBP的趋化活性，同样，环孢素A类似物Me6Ala-CsA虽然能结合亲环蛋白，但无法阻断亲环蛋白刺激的趋化活性。这些结果表明，亲免素除了在细胞内发挥作用外，还可能作为趋化因子发挥功能，此外，这种活性受免疫抑制剂调节。