A novel secreted cyclophilin-like protein (SCYLP).

Article Details

Citation

Spik G, Haendler B, Delmas O, Mariller C, Chamoux M, Maes P, Tartar A, Montreuil J, Stedman K, Kocher HP, et al.

A novel secreted cyclophilin-like protein (SCYLP).

J Biol Chem. 1991 Jun 15;266(17):10735-8.

PubMed ID
2040592 [ View in PubMed
]
Abstract

A novel cyclosporin A binding glycoprotein of 21 kDa was isolated from human milk by several steps of cation exchange chromatography. The corresponding gene was cloned from human T cells, expressed in Escherichia coli and the recombinant protein purified. The protein shares 58% amino acid identity with the cytosolic cyclophilin and is initially synthesized with a hydrophobic leader sequence. The cyclophilin-like protein has also peptidyl-prolyl cis/trans-isomerase activity, although less efficient, that is inhibited by cyclosporin A. The existence of a secreted form of cyclophilin-like protein in addition to the previously known cytosolic cyclophilin implies that these proteins act on different in vivo targets.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Peptidyl-prolyl cis-trans isomerase BP23284Details