Receptor (immunophilin-binding) assay for immunosuppressive drugs.
The major immunophilins that bind cyclosporine (cyclophilin) and FK-506/rapamycin (FK-BP12) have been well characterized. They possess rotamase activity, which is inhibited by the immunosuppressant that binds to them. The immunosuppressive action does not appear to be coupled to rotamase activity. The literature on some possible mechanisms of immunosuppression is reviewed. Minor immunophilins of 14, 37, and 52 kDa have also been isolated and partially characterized. The 14-kDa immunophilin binds FK-506 and rapamycin whereas the 52-kDa immunophilin binds all three drugs. Neither of these proteins have rotamase activity. Receptor assays employing immunophilins have been developed. Preliminary results are encouraging indicating that they may possess some advantages over current immunoassay procedures.
Soldin
S J
SJ
Department of Laboratory Medicine, Children's National Medical Center, Washington, D.C. 20010, USA.
D000591:Amino Acid Isomerases / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D006360:Heat-Shock Proteins / Q000737:chemistry*; D006801:Humans; D007118:Immunoassay; D007166:Immunosuppressive Agents / Q000737:chemistry*; D019696:Peptidylprolyl Isomerase; D011869:Radioligand Assay; D016559:Tacrolimus / Q000737:chemistry*; D022021:Tacrolimus Binding Proteins
D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D006360:Heat-Shock Proteins; D007166:Immunosuppressive Agents; D000591:Amino Acid Isomerases; D022021:Tacrolimus Binding Proteins; D019696:Peptidylprolyl Isomerase; D016559:Tacrolimus