TY - JOUR
T1 - S-cyclophilin
T2 - New member of the cyclophilin family associated with the secretory pathway
AU - Caroni, Pico
AU - Rothenfluh, Adrian
AU - McGlynn, Elaine
AU - Schneider, Corinna
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1991
Y1 - 1991
N2 - Cyclophilin is an abundant and ubiquitous cytosolic protein that is conserved throughout evolution from man to bacteria. It is the target of the immunosuppressive drug cyclosporin A. Cyclophilin has peptidyl-prolyl cis/trans- isomerase activity, and it accelerates protein folding in vitro, suggesting that it might be involved in the folding of cytosolic proteins. We describe a novel cyclophilin-like protein, S-cyclophilin, in the chick. Analysis of S-cyclophilin cDNA revealed the presence of a signal sequence followed by an open reading frame coding for a protein very similar to cytosolic Cyclophilin, except for the presence of unique additional short amino acid segments at the N and C termini of the protein. S-Cyclophilin mRNA was abundant and present in all embryonic chick tissues tested. Cyclophilin and S-cyclophilin are coded by separate genes in the chick genome. Recombinant S-cyclophilin was expressed in insect cells by means of the baculovirus system. Pulse-chase experiments revealed that a significant fraction of newly synthesized recombinant S-cyclophilin was rapidly secreted into the culture medium. Our findings indicate that cyclophilins are associated with most if not all intra- and extracellular compartments and suggest that enzyme-assisted conformational conversions in proteins might also take place in post-endoplasmic reticulum compartments, possibly including the extracellular space.
AB - Cyclophilin is an abundant and ubiquitous cytosolic protein that is conserved throughout evolution from man to bacteria. It is the target of the immunosuppressive drug cyclosporin A. Cyclophilin has peptidyl-prolyl cis/trans- isomerase activity, and it accelerates protein folding in vitro, suggesting that it might be involved in the folding of cytosolic proteins. We describe a novel cyclophilin-like protein, S-cyclophilin, in the chick. Analysis of S-cyclophilin cDNA revealed the presence of a signal sequence followed by an open reading frame coding for a protein very similar to cytosolic Cyclophilin, except for the presence of unique additional short amino acid segments at the N and C termini of the protein. S-Cyclophilin mRNA was abundant and present in all embryonic chick tissues tested. Cyclophilin and S-cyclophilin are coded by separate genes in the chick genome. Recombinant S-cyclophilin was expressed in insect cells by means of the baculovirus system. Pulse-chase experiments revealed that a significant fraction of newly synthesized recombinant S-cyclophilin was rapidly secreted into the culture medium. Our findings indicate that cyclophilins are associated with most if not all intra- and extracellular compartments and suggest that enzyme-assisted conformational conversions in proteins might also take place in post-endoplasmic reticulum compartments, possibly including the extracellular space.
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M3 - Article
C2 - 2040593
AN - SCOPUS:0025735861
SN - 0021-9258
VL - 266
SP - 10739
EP - 10742
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 17
ER -