Effects of a Water-Soluble Cinnamon Extract on Body Composition and Features of the Metabolic Syndrome in Pre-Diabetic Men and Women

Purpose: The purpose of this study was to determine the effects of supplementation with a water-soluble cinnamon extract (Cinnulin PF®) on body composition and features of the metabolic syndrome. Methods: Twenty-two subjects with prediabetes and the metabolic syndrome (mean ± SD: age, BMI, systolic blood pressure [SBP], fasting blood glucose [FBG]: 46.0 ± 9.7 y; 33.2 ± 9.3 kg/m 2; 133 ± 17 mm Hg; 114.3 ± 11.6 mg/dL) were randomly assigned to supplement their diet with either Cinnulin PF ® (500 mg/d) or a placebo for 12-weeks. Main outcome measures were changes in FBG, SBP, and body composition measured after 12-weeks of supplementation. The primary statistical analyses consisted of two factor (group x time), repeated-measures ANOVA for between group differences over time. In all analyses, an intent-to-treat approach was used and significance was accepted at P<0.05. Results: Subjects in the Cinnulin PF ® group had significant decreases in FBG (-8.4%: 116.3 ± 12.8 mg/dL [pre] to 106.5 ± 20.1 mg/dL [post], p<0.01), SBP (-3.8%: 133 ± 14 mm Hg [pre] to 128 ± 18 mm Hg [post], p<0.001), and increases in lean mass (+1.1%: 53.7 ± 11.8 kg [pre] to 54.3 ± 11.8 kg [post], p<0.002) compared with the placebo group. Additionally, within-group analyses uncovered small, but statistically significant decreases in body fat (-0.7%: 37.9 ± 9.2 % [pre] to 37.2 ± 8.9 % [post], p<0.02) in the Cinnulin PF ® group. No significant changes in clinical blood chemistries were observed betwee

POWERDRESS and HDA9 interact and promote histone H3 deacetylation at specific genomic sites in Arabidopsis

Histone acetylation is a major epigenetic control mechanism that is tightly linked to the promotion of gene expression. Histone acetylation levels are balanced through the opposing activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). Arabidopsis HDAC genes (AtHDACs) compose a large gene family, and distinct phenotypes among AtHDAC mutants reflect the functional specificity of individual AtHDACs. However, the mechanisms underlying this functional diversity are largely unknown. Here, we show that POWERDRESS (PWR), a SANT (SWI3/DAD2/N-CoR/TFIII-B) domain protein, interacts with HDA9 and promotes histone H3 deacetylation, possibly by facilitating HDA9 function at target regions. The developmental phenotypes of pwr and hda9 mutants were highly similar. Three lysine residues (K9, K14, and K27) of H3 retained hyperacetylation status in both pwr and hda9 mutants. Genome-wide H3K9 and H3K14 acetylation profiling revealed elevated acetylation at largely overlapping sets of target genes in the two mutants. Highly similar gene-expression profiles in the two mutants correlated with the histone H3 acetylation status in the pwr and hda9 mutants. In addition, PWR and HDA9 modulated flowering time by repressing AGAMOUS-LIKE 19 expression through histone H3 deacetylation in the same genetic pathway. Finally, PWR was shown to physically interact with HDA9, and its SANT2 domain, which is homologous to that of subunits in animal HDAC complexes, showed specific binding affinity to acetylated histone H3. We therefore propose that PWR acts as a subunit in a complex with HDA9 to result in lysine deacetylation of histone H3 at specific genomic targets. © 2016, National Academy of Sciences. All rights reserved.