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[iTRAQ] 糖尿病-iTRAQ-label free-SRM

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发表于 2016-1-4 13:51:54 | 显示全部楼层 |阅读模式

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Mol Cell Proteomics. 2011 Sep;10(9):M110.006650. doi: 10.1074/mcp.M110.006650. Epub 2011 Jun 22.
Characterization of human myotubes from type 2 diabetic and nondiabetic subjects usingcomplementary quantitative mass spectrometric methods.
IF=
14年6.564
13年7.254
12年7.251
11年7.398

研究关键词 2型糖尿病,iTRAQ,label free

研究概要  

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AbstractSkeletal muscle is a key tissue site of insulin resistance in type 2 diabetes. Human myotubes are primary skeletal muscle cells displaying both morphological and biochemical characteristics of mature skeletal muscle and the diabeticphenotype is conserved in myotubes derived from subjects with type 2 diabetes. Several abnormalities have been identified in skeletal muscle from type 2 diabetic subjects, however, the exact molecular mechanisms leading to thediabetic phenotype has still not been found. Here we present a large-scale study in which we combine a quantitativeproteomic discovery strategy using isobaric peptide tags for relative and absolute quantification (iTRAQ) and a label-free study with a targeted quantitative proteomic approach using selected reaction monitoring to identify, quantify, and validate changes in protein abundance among human myotubes obtained from nondiabetic lean, nondiabeticobese, and type 2 diabetic subjects, respectively. Using an optimized protein precipitation protocol, a total of 2832 unique proteins were identified and quantified using the iTRAQ strategy. Despite a clear diabetic phenotype indiabetic myotubes, the majority of the proteins identified in this study did not exhibit significant abundance changes across the patient groups. Proteins from all major pathways known to be important in type 2 diabetic subjects were well-characterized in this study. This included pathways like the trichloroacetic acid (TCA) cycle, lipid oxidation, oxidative phosphorylation, the glycolytic pathway, and glycogen metabolism from which all but two enzymes were found in the present study. None of these enzymes were found to be regulated at the level of protein expression or degradation supporting the hypothesis that these pathways are regulated at the level of post-translational modification. Twelve proteins were, however, differentially expressed among the three different groups. Thirty-six proteins were chosen for further analysis and validation using selected reaction monitoring based on the regulation identified in the iTRAQ discovery study. The abundance of adenosine deaminase was considerably down-regulated indiabetic myotubes and as the protein binds propyl dipeptidase (DPP-IV), we speculate whether the reduced binding of adenosine deaminase to DPP-IV may contribute to the diabetic phenotype in vivo by leading to a higher level of free DPP-IV to bind and inactivate the anti-diabetic hormones, glucagon-like peptide-1 and glucose-dependent insulintropic polypeptide.  
  
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3186194/

Mol Cell Proteomics-2011-Thingholm-IF7.251.pdf

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