A novel secreted cyclophilin-like protein (SCYLP) - PubMed (original) (raw)

Comparative Study

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

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Comparative Study

A novel secreted cyclophilin-like protein (SCYLP)

G Spik et al. J Biol Chem. 1991.

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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.

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