Source:http://linkedlifedata.com/resource/pubmed/id/17184142
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rdf:type | |
lifeskim:mentions |
umls-concept:C0036986,
umls-concept:C0040300,
umls-concept:C0041538,
umls-concept:C0205373,
umls-concept:C0337051,
umls-concept:C0441655,
umls-concept:C0449432,
umls-concept:C0871261,
umls-concept:C1179435,
umls-concept:C1509144,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1704259,
umls-concept:C1704632,
umls-concept:C1705248,
umls-concept:C1705987,
umls-concept:C1706817,
umls-concept:C2911692
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pubmed:issue |
5
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pubmed:dateCreated |
2007-11-1
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pubmed:abstractText |
Based on the biological significance of the ubiquitin-proteasome pathway (UPP) and its potential role during sepsis, burns and ischemia-reperfusion injury, we hypothesized that the systemic response to traumatic shock (TS) is accompanied by tissue-specific UPP alterations. Therefore, we studied tissue ubiquitin pools, chymotryptic- and tryptic-like proteasome peptidase activities and ubiquitin-protein ligation (UbPL) rates in skeletal muscle, heart, lung, liver, spleen and kidney using a clinically relevant porcine model (bilateral femur fracture/hemorrhage followed by fluid resuscitation). TS induced a systemic reduction of tissue-specific high molecular mass ubiquitin-protein conjugates (>50 kDa). Free ubiquitin was unaffected. The dynamic organ patterns of ubiquitin pools paralleled the typical physiological response to TS and resuscitation. Reduction of ubiquitin-protein conjugates was most pronounced in heart and lung (p<0.05 vs. control) and accompanied by significant increases in proteasome peptidase and UbPL activities in these organs. Unlike all other tissues, spleen proteasome peptidase and UbPL activities were significantly reduced 10 h after TS. These findings support the concept that the UPP could play an important role in regulation of cell functions during the early whole-body response to TS. The UPP might be a therapeutic target to improve the metabolic care after TS, particularly in the heart, lung, and spleen.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0862-8408
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
547-57
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pubmed:dateRevised |
2008-4-2
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pubmed:meshHeading |
pubmed-meshheading:17184142-Animals,
pubmed-meshheading:17184142-Chymases,
pubmed-meshheading:17184142-Disease Models, Animal,
pubmed-meshheading:17184142-Femoral Fractures,
pubmed-meshheading:17184142-Fluid Therapy,
pubmed-meshheading:17184142-Hemorrhage,
pubmed-meshheading:17184142-Kidney,
pubmed-meshheading:17184142-Lung,
pubmed-meshheading:17184142-Muscle, Skeletal,
pubmed-meshheading:17184142-Myocardium,
pubmed-meshheading:17184142-Proteasome Endopeptidase Complex,
pubmed-meshheading:17184142-Serine Endopeptidases,
pubmed-meshheading:17184142-Shock, Traumatic,
pubmed-meshheading:17184142-Spleen,
pubmed-meshheading:17184142-Swine,
pubmed-meshheading:17184142-Time Factors,
pubmed-meshheading:17184142-Ubiquitins
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pubmed:year |
2007
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pubmed:articleTitle |
Dynamics of tissue ubiquitin pools and ubiquitin-proteasome pathway component activities during the systemic response to traumatic shock.
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pubmed:affiliation |
DeWitt Daughtry Family Department of Surgery, Division of Trauma and Surgical Critical Care, University of Miami Miller School of Medicine, Miami, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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