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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1988-4-25
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pubmed:abstractText |
Previous studies on the distribution of circulating ciclosporin have shown that the majority of the drug is associated with erythrocytes. In order to investigate the nature of ciclosporin-erythrocyte binding, binding studies were performed on isolated erythrocytes. At therapeutic concentrations (approx. 0.5 microgram/ml in whole blood) greater than 90% of the erythrocyte associated ciclosporin was found in the cytosol. The cytosolic binding capacity was approximately (2-2.5).10(5) molecules of ciclosporin per cell. A lower affinity binding of the drug to the plasma membrane occurred only at higher ciclosporin concentrations. The ciclosporin-binding species was purified from erythrocyte cytosol using ciclosporin-Affigel affinity chromatography. This revealed a 16 kDa protein, similar in size to the ciclosporin-binding protein, cyclophilin, previously identified in lymphocyte cytosol. Immunochemical analysis using rabbit anti-bovine spleen cyclophilin antisera revealed that the erythrocyte ciclosporin-binding protein was either cyclophilin or a closely related protein. It is concluded that intracellular ciclosporin-binding within erythrocytes is mostly attributable to the presence of a single protein or protein family represented by cyclophilin. The presence of (2-2.5).10(5) copies of this binding protein within each erythrocyte is responsible for the ciclosporin found associated with erythrocytes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclosporins,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidylprolyl Isomerase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
938
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
447-55
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:3280030-Binding, Competitive,
pubmed-meshheading:3280030-Blood Proteins,
pubmed-meshheading:3280030-Carrier Proteins,
pubmed-meshheading:3280030-Chromatography, Affinity,
pubmed-meshheading:3280030-Cyclosporins,
pubmed-meshheading:3280030-Cytosol,
pubmed-meshheading:3280030-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3280030-Erythrocyte Membrane,
pubmed-meshheading:3280030-Erythrocytes,
pubmed-meshheading:3280030-Hemoglobins,
pubmed-meshheading:3280030-Humans,
pubmed-meshheading:3280030-Immunoassay,
pubmed-meshheading:3280030-Peptidylprolyl Isomerase
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pubmed:year |
1988
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pubmed:articleTitle |
Identification of cyclophilin as the erythrocyte ciclosporin-binding protein.
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pubmed:affiliation |
Sandoz Ltd., Basle, Switzerland.
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pubmed:publicationType |
Journal Article
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