Objective We aimed to estimate the up-to-date prevalence of metabolic syndrome (MS) and its influencing factors among the Chinese adults. Methods Data were obtained from the China Health and Nutrition Survey conducted in 2009, which was a cross-sectional and partially nationally representative study including a total of 7488 Chinese adults (age ≥ 18 years). Results The overall age-standardized prevalence estimates of the MS were 21.3% (95%confidence interval (CI): 20.4%–22.2%), 18.2% (95%CI: 17.3%–19.1%) and 10.5% (95%CI: 9.8%–11.2%) based on definitions of revised NCEP ATPIII, IDF and CDS criteria, respectively. Individuals who were women (compared to men: odds ratio [OR] = 1.37, 95% CI=1.16–1.61), 40 years or older (compared to less than 40 years old: OR=2.82, 95%CI=2.37–3.34 for 40–59 years; OR = 4.41, 95%CI = 3.68–5.29 for 60 years or older), overweight/obese (compared to normal weight: OR=4.32, 95%CI=3.77–4.95 for overweight; OR=11.24, 95%CI=9.53–13.26 for obese), and living in urban area (compared to living in rural area: OR=1.27, 95%CI=1.12–1.43) were more likely to have a higher prevalence estimate of MS. In addition, frequency of alcohol consumption and cigarette intake were also found to be significantly associated with probability of MS. Conclusions Our results suggest an urgent need to develop national strategies for the prevention, detection, treatment and control of obesity and MS in China.

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Site-selective bioconjugation to native protein residues is a powerful tool for protein functionalization, with cysteine and lysine side chains being the most common points for attachment owing to their high nucleophilicity. We now report a strategy for histidine modification using thiophosphorodichloridate reagents that mimic post-translational histidine phosphorylation, enabling fast and selective labeling of protein histidines under mild conditions where various payloads can be introduced via copper-assisted alkyne-azide cycloaddition (CuAAC) chemistry. We establish that these reagents are particularly effective at covalent modification of His-tags, which are common motifs to facilitate protein purification, as illustrated by selective attachment of polyarginine cargoes to enhance the uptake of proteins into living cells. This work provides a starting point for probing and enhancing protein function using histidine-directed chemistry.

Hypoxia-inducible factor 1 (HIF-1) transcriptionally promotes production of adenosine triphosphate (ATP) whereas AMPK senses and regulates cellular energy homeostasis. A histone deacetylase (HDAC) activity has been proven to be critical for HIF-1 activation but the underlying mechanism and its role in energy homesostasis remain unclear. Here, we demonstrate that HIF-1 activation depends on a cytosolic, enzymatically active HDAC5. HDAC5 knockdown impairs hypoxia-induced HIF-1a accumulation and HIF-1 transactivation, whereas HDAC5 overexpression enhances HIF-1a stabilization and nuclear translocation. Mechanistically, we show that Hsp70 is a cytosolic substrate of HDAC5; and hyperacetylation renders Hsp70 higher affinity for HIF-1a binding, which correlates with accelerated degradation and attenuated nuclear accumulation of HIF-1a. Physiologically, AMPK-triggered cytosolic shuttling of HDAC5 is critical; inhibition of either AMPK or HDAC5 impairs HIF-1a nuclear accumulation under hypoxia or low glucose conditions. Finally, we show specifically suppressing HDAC5 is sufficient to inhibit tumor cell proliferation under hypoxic conditions. Our data delineate a novel link between AMPK, the energy sensor, and HIF-1, the major driver of ATP production, indicating that specifically inhibiting HDAC5 may selectively suppress the survival and proliferation of hypoxic tumor cells.