A. Jaschke et al., HUMAN T-CELL CYCLOPHILIN18 BINDS TO THIOL-SPECIFIC ANTIOXIDANT PROTEIN AOP1 AND STIMULATES ITS ACTIVITY, Journal of Molecular Biology, 277(4), 1998, pp. 763-769
Cyclophilins (CyPs) define a family of proteins binding to the immunos
uppressive drug cyclosporin A (CsA). They are evolutionary highly cons
erved proteins being present in both pro- and eukaryotes and in differ
ent subcellular locations. CyPs possess enzymatic activity, namely pep
tidyl-prolyl cis-trans isomerase (PPIase) activity and are involved in
cellular protein folding and protein interactions. Hero we describe a
novel interaction of human T cell cyclophilin18 (hCyP18). Abundant cy
tosolic hCyP18 binds to the thiol-specific antioxidant protein Aop1 an
d stimulates its enzymatic activity. Aop1 belongs to a family of prote
ins thought to be involved in defense of oxidative stress. The interac
tion of both proteins seem to be specific, since other PPIases do not
have any stimulatory effect on Aop1. (C) 1998 Academic Press Limited.