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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2003-9-10
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pubmed:abstractText |
Activation of the enzyme indoleamine-(2,3)-dioxygenase (IDO) by interferon (IFN)-g leads to enhanced tryptophan conversion to kynurenine. In consequence of chronic immune activation, tryptophan availability is reduced, leading to inhibition of cell proliferation as protein synthesis is affected. Tryptophan deprivation due to IDO activation could therefore be effective in abrogating processes with high metabolic turnover, thus modulating cellular immune response.
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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 |
Sep
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pubmed:issn |
0315-162X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1935-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12966593-Arthritis, Rheumatoid,
pubmed-meshheading:12966593-Biological Markers,
pubmed-meshheading:12966593-Chromatography, High Pressure Liquid,
pubmed-meshheading:12966593-Cohort Studies,
pubmed-meshheading:12966593-Female,
pubmed-meshheading:12966593-Humans,
pubmed-meshheading:12966593-Kynurenine,
pubmed-meshheading:12966593-Male,
pubmed-meshheading:12966593-Neopterin,
pubmed-meshheading:12966593-Probability,
pubmed-meshheading:12966593-Prognosis,
pubmed-meshheading:12966593-Sensitivity and Specificity,
pubmed-meshheading:12966593-Severity of Illness Index,
pubmed-meshheading:12966593-Tryptophan
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pubmed:year |
2003
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|
pubmed:articleTitle |
Increased degradation of tryptophan in blood of patients with rheumatoid arthritis.
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pubmed:affiliation |
Institute of Medical Chemistry and Biochemistry, Leopold Franzens University of Innsbruck, Fritz Pregl Strasse 3, A-6020 Innsbruck, Austria.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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