Healthy eating methods for socioeconomically deprived numbers: a new meta-ethnography.

Tissues hypoxia caused by hemorrhage is a common complication in many clinical diseases. However, its pathological mechanism remains largely unknown. To partly address this issue, an ischemic-hypoxic rat model was established and the plasma proteomic and metabolic profiles were quantified and analyzed using TMT-based quantitative proteomics and metabolomics. The analysis revealed a total of 177 differentially expressed proteins and 32 metabolites that were uniquely altered in the hypoxic rat plasma, compared to the control. Bioinformatics analysis showed that these altered proteins and metabolites were involved in a wide range of biological processes. Twelve of the 177 differentially expressed proteins were involved in PI3K-Akt signaling, a pathway that has been reported to be strongly associated with tissue hypoxia. Other signaling pathways such as complement and coagulation cascades, GnRH signaling, relaxin signaling, protein processing in endoplasmic reticulum, as well as AGE-RAGE signaling were markedly a in endoplasmic reticulum, and AGE-RAGE signaling. Moreover, a panel of 12 candidate proteins involved in PI3K-Akt signaling (i.e., Vtn, Hsp90b1, Ywhae, Tnc, Ywhaz, Thbs4, Lamc1, Col1a1, Il2rg, Egfr, Newgene 621,351, and Tfrc) may serve as the potential biomarkers to predict tissue hypoxia.Long-chain acyl-CoA synthetase 4 (ACSL4) is an ACSL family member that exhibits unique substrate preference for arachidonic acid. ACSL4 has a functional role in hepatic lipid metabolism, and is dysregulated in non-alcoholic fatty liver disease. Our previous studies demonstrated AA-induced ACSL4 degradation via the ubiquitin-proteasomal pathway (UPP). To characterize this unique mechanism, we applied proteomic approaches coupled with LC-MS/MS and identified the intracellular general vesicular trafficking protein p115 as the prominent ACSL4 interacting protein in HepG2 cells. Importantly, we found that AA greatly enhanced p115-ACSL4 association. Combined AA treatment with p115 knockdown suggested an additive role for p115 in AA-driven ACSL4 degradation. Furthermore, in vivo studies revealed a significant upregulation of p115 protein in the liver of mice fed a high fat diet that has been previously reported to induce downregulation of ACSL4 protein expression. selleck chemical This new finding has revealed a novel inverse correlcretion and protein degradation and opens up a new avenue to explore this partnership in controlling hepatic lipid metabolism. Overall, the complete elucidation of the AA-mediated ACSL4 regulation will help identify key targets in participating pathways that can be further studied for the development of therapeutics against diseases such as NAFLD, NASH and hepatocarcinoma, which are associated with dysregulated ACSL4 function.Acute myocardial infarction (AMI) remains a leading cause of morbidity and mortality worldwide. Novel biomarkers are needed to identify NSTEMI in AMI patients. The study objective was to use proteomics to identify novel plasma biomarkers for STEMI and NSTEMI patients. iTRAQ analysis was performed on pooled samples from 8 healthy controls and 12 STEMI and 12 NSTEMI patients. Bioinformatics analysis identified 95 differentially expressed proteins that were differentially expressed in the plasma of AMI patients and healthy controls; 28 of these proteins were found in STEMI/Con (22 upregulated and 6 downregulated), 48 in NSTEMI/Con (12 upregulated and 36 downregulated), and 44 in NSTEMI/STEMI (11 upregulated and 33 downregulated). Protein network analysis was then performed using STRING software. Functional analysis revealed that the identified plasma proteins were mainly involved with carbon metabolism, toll-like receptor signaling pathway, and hypertrophic cardiomyopathy. Nine of the proteins (SSA1, MDH1, FCN2,trophic cardiomyopathy may be the major driving forces for cardiac damage during myocardial infarction. However, further investigations are needed to verify the mechanisms involved in the development of AMI especially NSTEMI. Taken together, our findings lay the foundation for understanding the molecular mechanisms underlying the pathogenic processes of AMI, and suggest potential applications for specific biomarkers in early diagnosis and determination of prognosis.Hibernation is an energy-saving and adaptive strategy adopted by leech, an important medicinal resource in Asia, to survive low temperature. Reversible protein phosphorylation (RPP) plays a key role in the regulation of mammalian hibernation processes but has never been documented in freshwater invertebrate such as leech. In this study, we detected the effects of hibernation on the proteome and phosphoproteome of the leech Whitmania pigra. A total of 2184 proteins and 2598 sites were quantified. Deep-hibernation resulted in 85 up-regulated and 107 down-regulated proteins and 318 up-regulated and 204 down-regulated phosphosites using a 1.5-fold threshold (P less then 0.05). Proteins involved in protein digestion and absorption, amino acid metabolism and N-glycan biosynthesis were significantly down-regulated during deep-hibernation. However, proteins involved in maintaining cell structure stability in hibernating animals were up-regulated. Differentially phosphorylated proteins provided the first global pictur proteins that could be important for functionally adapt in freshwater animals.Passage of malaria parasites through mosquitoes involves multiple developmental transitions, from gametocytes that are ingested with the blood meal, through to sporozoites that are transmitted by insect bite to the host. selleck chemical During the transformation from gametocyte to oocyst, the parasite forms a unique transient organelle named the crystalloid, which is involved in sporozoite formation. In Plasmodium berghei, a complex of six LCCL domain-containing proteins (LAPs) reside in the crystalloid and are required for its biogenesis. However, little else is known about the molecular mechanisms that underlie the crystalloid’s role in sporogony. In this study, we have used transgenic parasites stably expressing LAP3 fused to GFP, combined with GFP affinity pulldown and high accuracy mass spectrometry, to identify an extended LAP interactome of some fifty proteins. We show that many of these are targeted to the crystalloid, including members of two protein families with CPW-WPC and pleckstrin homology-like domains, respectively.