rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2000-7-18
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pubmed:abstractText |
The influence of the gene expression of critical components of the cytoplasmic and lysosomal proteolytic pathways on the rate of protein degradation was evaluated in the leg skeletal muscle of 8 severely traumatized patients. Muscle proteolysis was determined as the intramuscular phenylalanine rate of appearance by L-[ring-2H5]phenylalanine infusion and the leg arteriovenous catheterization technique combined with muscle biopsy. Muscle mRNA levels of UbB polyubiquitin and cathepsin B were determined by reverse transcriptase-competitive polymerase chain reaction and expressed as a percent of the mRNA level of the housekeeping gene glyceraldehyde-3-phosphate dehydrogenase (GAPDH). In the patients, individual values for UbB polyubiquitin mRNA levels directly correlated with the rate of muscle proteolysis (r = .76, P < .05), whereas no correlation (r = .10) was found between cathepsin B mRNA levels and proteolysis. Thus, after trauma, the rate of muscle proteolysis appears to be largely regulated by the ubiquitin-proteasome system at the level of gene transcription.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin B,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylalanine,
http://linkedlifedata.com/resource/pubmed/chemical/Polyubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0026-0495
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
689-91
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10877190-Adult,
pubmed-meshheading:10877190-Biopolymers,
pubmed-meshheading:10877190-Cathepsin B,
pubmed-meshheading:10877190-Cysteine Endopeptidases,
pubmed-meshheading:10877190-Gene Expression Regulation,
pubmed-meshheading:10877190-Humans,
pubmed-meshheading:10877190-Male,
pubmed-meshheading:10877190-Multienzyme Complexes,
pubmed-meshheading:10877190-Muscle, Skeletal,
pubmed-meshheading:10877190-Muscle Proteins,
pubmed-meshheading:10877190-Phenylalanine,
pubmed-meshheading:10877190-Polyubiquitin,
pubmed-meshheading:10877190-Proteasome Endopeptidase Complex,
pubmed-meshheading:10877190-RNA, Messenger,
pubmed-meshheading:10877190-Transcription, Genetic,
pubmed-meshheading:10877190-Ubiquitins,
pubmed-meshheading:10877190-Wounds and Injuries
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pubmed:year |
2000
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pubmed:articleTitle |
Contribution of the ubiquitin-proteasome pathway to overall muscle proteolysis in hypercatabolic patients.
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pubmed:affiliation |
Istituto di Clinica Medica, University of Trieste, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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