in at 120006g at 4uC. The supernatant was Acetic Acid Activates the AMPK Signaling Pathway ferred onto PVDF membranes. The membranes were blocked in bovine serum albumin/TBST buffer for 4 h and hybridized with antibodies specific for SIRT1, LKB1, AMPKa, phosphorylated AMPKa, ACC1, phosphorylated ACC1, PPARa, SREBP-1c, and ChREBP overnight at 4uC. The membranes were then incubated with the appropriate BCTC biological activity peroxidase-conjugated secondary antibodies. Immunoreactive bands were detected with an enhanced chemiluminescence solution. The blots were exposed to X-ray film, and the band intensity was measured using BandScan software version 5.0. extract protein for 20 min at room temperature. DNA-protein complexes were separated by electrophoresis on non-denaturing 6.5% polyacrylamide TBE gels and were electrotransferred onto a nylon membrane, which was UV crosslinked. The biotin-labeled probe was detected with a chemiluminescence solution. The blots were exposed to X-ray film, and the band intensity was measured using BandScan software version 5.0. Statistical analysis Results are expressed as the mean 6 standard deviation. SPSS 16.0 software was used to analyze the data. The group differences were compared using Duncan’s multiple range test. A p value of less than 0.05 was considered statistically significant, and values less than 0.01 were considered markedly significant. Electrophoretic Mobility Shift Assay An electrophoretic mobility shift assay was used to detect the transcriptional activity of PPARa, SREBP-1c, and ChREBP. Nuclear proteins were extracted using a nuclear protein extraction kit according to the manufacturer’s instructions. Protein concentrations were measured with the Bio-Rad protein assay reagent. The special probe recognition sequences for PPARa, SREBP-1c, and ChREBP are shown in Myeloperoxidase is the most abundant proinflammatory enzyme stored in the azurophilic granules of neutrophilic granulocytes, accounting for approximately 5% of 21836025 their dry mass. It catalyzes the formation of hypochlorous acid from hydrogen peroxide, generates other highly reactive molecules such as tyrosyl radicals, and cross-links proteins. Recently, MPO has been found 21415165 to be implicated in a multitude of diseases, including 
atherosclerosis, myocardial infarction, atrial fibrillation, multiple sclerosis, Alzheimer’s disease, lung cancer, and transplant rejection. Scientific research on MPO has steadily increased over the last 2 decades, with approximately 1000 manuscripts published in 2012 alone. While MPO expression or protein level measurements can provide some information regarding the abundance of the MPO molecule, the enzymatic activity of MPO can vary considerably between individuals even if the amount of MPO present is similar. Besides effects such as age and gender, multiple polymorphisms have been identified both with decreased and increased MPO activity. Furthermore, as MPO can be inhibited by endogenous inhibitors, MPO activity does not always correspond to MPO protein or expression levels. Evaluating MPO activity is crucial to understanding its effects in inflammation, and it is not surprising that MPO activity assays are widely used in the literature for this purpose. However, no consensus has been reached on which of the many available assays to use. This is further complicated by the fact that most available probes are general peroxidase substrates, lacking specificity towards MPO. Moreover, tissue inhibitors of MPO can interfere with assa