Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.14 (ATP synthase)
 7,042 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Efficiency of nutrient utilization is high in neonates with normal birth weights but is reduced in those with intrauterine growth restriction (IUGR). However, the underlying mechanisms are largely unknown. This study was conducted with the piglet model and proteomics technology to test the hypothesis that IUGR affects expression of key proteins that regulate growth and development of the small intestine, liver, and muscle, the major organs involved in the digestion, absorption, and metabolism of dietary nutrients. Jejunum, liver, and gastrocnemius muscle were obtained from IUGR and normal birth-weight piglets at birth for analysis of proteomes using the 2-dimensional-PAGE MS technology. The results indicate that IUGR decreased the levels of proteins that regulate immune function (immunoglobulins and annexin A1), oxidative defense (peroxiredoxin 1, transferrin, and zeta-crystallin), intermediary metabolism (creatine kinase, alcohol dehydrogenase, L-lactate dehydrogenase, prostaglandin F synthase, apolipoprotein AI, catecho O-methyltransferase, and phosphoglycerate kinase 1), protein synthesis (eukaryotic translation initiation factor-3), and tissue growth (beta-actin, desmin, and keratin 10) in a tissue-specific manner. In addition, IUGR increased the levels of proteins that are involved in proteolysis (proteasome alpha-5 and alpha-1 subunits), response to oxidative stress (scavenger-receptor protein and alpha-1 acid glycoprotein), and ATP hydrolysis (F1-ATPase). These novel findings suggest that cellular signaling defects, redox imbalance, reduced protein synthesis, and enhanced proteolysis may be the major mechanisms responsible for abnormal absorption and metabolism of nutrients, as well as reduced growth and impaired development of the small intestine, liver, and muscle in IUGR neonates.
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PMID:Intrauterine growth restriction affects the proteomes of the small intestine, liver, and skeletal muscle in newborn pigs. 1815 5

Quercetin is a flavonoid natural product, that is, found in many foods and has been found to have a wide range of medicinal effects. Though a number of quercetin binding proteins have been identified, there has been no systematic approach to identifying all potential targets of quercetin. We describe an O7-biotinylated derivative of quercetin (BioQ) that can act as a photoaffinity proteomics reagent for capturing quercetin binding proteins, which can then be identified by LC-MS/MS. BioQ was shown to inhibit heat induction of HSP70 with almost the same efficiency as quercetin, and to both inhibit and photocrosslink to CK2 kinase, a known target of quercetin involved in activation of the heat shock transcription factor. BioQ was also able to pull down a number of proteins from unheated and heated Jurkat cells following UV irradiation that could be detected by both silver staining and Western blot analysis with an anti-biotin antibody. Analysis of the protein bands by trypsinization and LC-MS/MS led to the identification of heat shock proteins HSP70 and HSP90 as possible quercetin target proteins, along with ubiquitin-activating enzyme, a spliceosomal protein, RuvB-like 2 ATPases, and eukaryotic translation initiation factor 3. In addition, a mitochondrial ATPase was identified that has been previously shown to be a target of quercetin. Most of the proteins identified have also been previously suggested to be potential anticancer targets, suggesting that quercetin's antitumor activity may be due to its ability to inhibit multiple target proteins.
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PMID:Biotinylated quercetin as an intrinsic photoaffinity proteomics probe for the identification of quercetin target proteins. 2179 48

Four hundred male chickens were selected to study the effects of pyruvate (Pyr), creatine pyruvate (CrPyr) and creatine (Cr) on the expression of hepatic mitochondrial and cytoplasm proteins associated with lipid and protein metabolism. Mitochondrial purification was accomplished using the two-step differential centrifugation and density gradient method, and the activities of organelle-specific marker enzymes were determined to assess the purity of the mitochondria. Proteins were extracted and fractionated by two-dimensional electrophoresis and the differential protein spots were assessed by matrix-assisted laser desorption/ionization-time of flight mass spectrometry. CrPyr reduced fatty acid accumulation by down-regulating adipose differentiation-related protein, inhibited ATP synthase expression, and reduced cholesteryl ester transfer protein (CETP) expression, thus reducing the levels of high density lipoprotein and triglycerol (TG) levels (thereby lowering fat and cholesterol deposition). CrPyr increased the expression of eukaryotic translation initiation factor (eIF) 2B, calreticulin (CRT) and eIF3a, thus promoting protein synthesis. CrPyr up-regulated the expression of fatty acid-binding proteins, CETP and apolipoprotein A-IV in cytoplasmic extracts, and these proteins accelerated the decomposition of fatty acids and TG, thus reducing fat deposition. In conclusion, CrPyr plays an important role in lipolysis and protein synthesis, and this effect was more pronounced than was the effect of Pyr and Cr.
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PMID:Use of comparative proteomics to identify the effects of creatine pyruvate on lipid and protein metabolism in broiler chickens. 2239 30