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A novel secreted cyclophilin-like protein (SCYLP)

Open AccessPublished:June 15, 1991DOI:https://doi.org/10.1016/S0021-9258(18)99078-2
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      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.

      REFERENCES

        • Sawada S.
        • Suzuki G.
        • Kawase Y.
        • Takaku F.
        J. Immunol. 1987; 139: 1797-1803
        • Handschumacher R.E.
        • Harding M.W.
        • Rice J.
        • Drugge R.J
        • Speicher D2.W.
        Science. 1984; 226: 544-547
        • Siekierka J.J.
        • Hung S.H.Y.
        • Poe M.
        • Lin C.S
        • Sigal N.H.
        Nature. 1989; 341: 755-757
        • Harding M.
        • Galat A.
        • Uehling D.E.
        • Schreiber S.L.
        Nature. 1989; 341: 758-760
        • Fischer G.
        • Wittman-Liebold B.
        • Lang K.
        • Kiefhaber T.
        • Schmid F.X.
        Nature. 1989; 337: 476-478
        • Takahashi N.
        • Hayano T.
        • Suzuki M.
        Nature. 1989; 337: 473-475
        • Elliott J.F.
        • Lin '.
        • Mizel S.
        Science. 1984; 226: 1439-1441
        • Kronke M.
        • Leonard W.
        • Depper J.
        • Greene W.
        Proc. Natl. Acad. Sei. U. S. A. 1984; 81: 5214-5218
        • Tocci M.J.
        • Matkovich D.A.
        • Collier K.A.
        • Kwok P.
        • Dumont F.
        • Lin S.
        • Degudicibus S.
        • Siekierka J.J.
        • Chin J.
        • Hutchinson N.I.
        J. Immunol. 1989; 143: 718-726
        • Maniatis T.
        • Fritsch E.F.
        • Sambrook J.
        Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY1982
        • Amman E.
        • Brosius J.
        Gene (Amst.). 1985; 40: 183-190
        • Plouet J.
        • Olivie M.
        • Courtois Y.
        • Barritault D.
        J. Cell. Mol. Biol. 1984; 30: 105-110
        • Haselbeck A.
        • Hosel W.
        Glycoconjugate J. 1990; 7: 63-74
        • Harding M.W.
        • Handschumacher R.E.
        • Speicher D.W.
        J. Biol. Chem. 1989; 261: 8547-8555
        • Haendler B.
        • Hofer-Warbinek R.
        • Hofer E.
        EMBOJ. 1987; 6: 947-950
        • Koletsky A.J.
        • Harding M.W.
        • Handschumacher R.E.
        J. Immunol. 1986; 137: 1054-1059
        • VonHeijne G.
        Nucleic Acids Res. 1986; 14: 4683-4690
        • Kozak M.
        Cell. 1986; 44: 283-292
        • Haendler B.
        • Keller R.
        • Hiestand P.C.
        • Kocher H.P.
        • Wegmann G.
        • Movva N.R.
        Gene (Amst.). 1989; 83: 39-46
        • Freedman R.B.
        Cell. 1989; 57: 1069-1072
        • Munro S.
        • Pelham H.R.B.
        Cell. 1987; 48: 899-907
        • Munro S.
        • Pelham H.R.B.
        Cell. 1986; 46: 291-300
        • Tropschug M.
        • Nicholson D.
        • Hartl F.
        • Koeler H.
        • Pf'nner N.
        • W'chter E.
        • Neupeit W.
        J. Biol. Chem. 1988; 263: 14433-14440
        • Koser P.L.
        • Sylvester D.
        • Livi G.P.
        • Bergsma D.J.
        Nucleic Acids Res. 1990; 18: 1643
        • Schneuwly S.
        • Shortridge R.D.
        • Larrivee D.C.
        • Ono T.
        • Ozaki M.
        • Pak W.L.
        Proc. Natl. Acad. Sei. U. S. A. 1989; 86: 5390-5394
        • Liu J.
        • Walsh C.
        Proc. Natl. Acad. Sei. U. S. A. 1990; 87: 4028-4032
        • Haendler B.
        • Hofer E.
        Eur. J. Biochem. 1990; 190: 477-482
        • Caroni P.
        • Rothenfluh A.
        • McGlynn E.
        • Schneider C.
        J. Biol. Chem. 1991; 266: 10739-10742

      Linked Article

      • Cyclophilin B is really a major growth factor in breast milk
        Journal of Biological ChemistryVol. 298Issue 1
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          Cyclophilin B (CypB) was first described and its sequence was reported by Spik et al. in 1991 (1). These authors prepared and characterized recombinant CypB demonstrating that it had prolyl isomerase activity, which was inhibited by cyclosporin (1). At that time, no mitogenic activity was observed for CypB. This may be because of the absence of glycosylation, incorrect folding, denaturation, or to the cellular model used in these initial exploratory experiments (3T3). We wish to report that an earlier unpublished study (2) showed that CypB has growth factor activity on CCL-39 cells at around 30 ng/ml, similar to EGF, acidic FGF, and basic FGF.
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