A novel secreted cyclophilin-like protein (SCYLP).
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.
Spik
G
G
Laboratoire de Chimie Biologique, Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq, France.
Haendler
B
B
Delmas
O
O
Mariller
C
C
Chamoux
M
M
Maes
P
P
Tartar
A
A
Montreuil
J
J
Stedman
K
K
Kocher
H P
HP
D000591:Amino Acid Isomerases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D002850:Chromatography, Gel; D003524:Cyclosporins / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D005260:Female; D006801:Humans; D007700:Kinetics; D008895:Milk, Human / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D015345:Oligonucleotide Probes; D019696:Peptidylprolyl Isomerase; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid
D002352:Carrier Proteins; D003524:Cyclosporins; D015345:Oligonucleotide Probes; D011994:Recombinant Proteins; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase