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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
1991-7-10
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pubmed:databankReference |
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10739-42
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:2040593-Amino Acid Isomerases,
pubmed-meshheading:2040593-Amino Acid Sequence,
pubmed-meshheading:2040593-Animals,
pubmed-meshheading:2040593-Base Sequence,
pubmed-meshheading:2040593-Carrier Proteins,
pubmed-meshheading:2040593-Cell Line,
pubmed-meshheading:2040593-Chick Embryo,
pubmed-meshheading:2040593-Cloning, Molecular,
pubmed-meshheading:2040593-Cyclosporins,
pubmed-meshheading:2040593-DNA,
pubmed-meshheading:2040593-Gene Library,
pubmed-meshheading:2040593-Insects,
pubmed-meshheading:2040593-Molecular Sequence Data,
pubmed-meshheading:2040593-Open Reading Frames,
pubmed-meshheading:2040593-Peptidylprolyl Isomerase,
pubmed-meshheading:2040593-Protein Sorting Signals,
pubmed-meshheading:2040593-Recombinant Proteins,
pubmed-meshheading:2040593-Spinal Cord,
pubmed-meshheading:2040593-Transfection
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pubmed:year |
1991
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pubmed:articleTitle |
S-cyclophilin. New member of the cyclophilin family associated with the secretory pathway.
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pubmed:affiliation |
Friedrich Miescher Institute, Basel, Switzerland.
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pubmed:publicationType |
Journal Article
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