Resveratrol enhances brown adipocyte formation and function by activating AMP-activated protein kinase (AMPK) α1 in mice fed high-fat diet

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Abstract

<div class="section"> <a class="named-anchor" id="S1">  </a> <h5 class="section-title" id="d12804368e189">Scope</h5> <p id="P1">Enhancing the formation and function of brown adipose tissue (BAT) increases thermogenesis and hence reduces obesity. Thus, we investigate the effects of resveratrol (Resv) on brown adipocyte formation and function in mouse interscapular BAT (iBAT). </p> </div><div class="section"> <a class="named-anchor" id="S2">  </a> <h5 class="section-title" id="d12804368e194">Methods and results</h5> <p id="P2">CD1 mice and stromal vascular cells (SVCs) isolated from iBAT were treated with Resv. Expression of brown adipogenic and thermogenic markers, and involvement of AMP-activated protein kinase (AMPK)α1 were assessed. <i>In vivo</i>, Resv enhanced expression of brown adipogenic markers, PR domain-containing 16 (PRDM16) and thermogenic genes, uncoupling protein 1 (UCP1) and cytochrome C in iBAT, along with smaller lipid droplets, elevated AMPKα activity and increased oxygen consumption. Meanwhile, Resv promoted expression of PRDM16, UCP1, PGC1α, cytochrome C and pyruvate dehydrogenase (PDH) in differentiated iBAT SVCs, suggesting that Resv enhanced brown adipocyte formation and function <i>in vitro</i>. In addition, Resv stimulated AMPKα and oxygen consumption in differentiated iBAT SVCs. However, the promotional effects of Resv were diminished by AMPK inhibition or AMPKα1 knockout, implying the involvement of AMPKα1 in this process. </p> </div><div class="section"> <a class="named-anchor" id="S3">  </a> <h5 class="section-title" id="d12804368e205">Conclusion</h5> <p id="P3">Resv enhanced brown adipocyte formation and thermogenic function in mouse iBAT by promoting the expression of brown adipogenic markers via activating AMPKα1, which contributed to the anti-obesity effects of Resv. </p> </div>

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Transcriptional control of brown fat determination by PRDM16.

Patrick Seale, Shingo Kajimura, Wenli Yang … (2007)

Brown fat cells are specialized to dissipate energy and can counteract obesity; however, the transcriptional basis of their determination is largely unknown. We show here that the zinc-finger protein PRDM16 is highly enriched in brown fat cells compared to white fat cells. When expressed in white fat cell progenitors, PRDM16 activates a robust brown fat phenotype including induction of PGC-1alpha, UCP1, and type 2 deiodinase (Dio2) expression and a remarkable increase in uncoupled respiration. Transgenic expression of PRDM16 at physiological levels in white fat depots stimulates the formation of brown fat cells. Depletion of PRDM16 through shRNA expression in brown fat cells causes a near total loss of the brown characteristics. PRDM16 activates brown fat cell identity at least in part by simultaneously activating PGC-1alpha and PGC-1beta through direct protein binding. These data indicate that PRDM16 can control the determination of brown fat fate.

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The Global Burden of Obesity and the Challenges of Prevention

Jacob Seidell, Jutka Halberstadt (2015)

The prevalence of obesity is increasing at an alarming rate in many parts of the world. About 2 billion people are overweight and one third of them obese. The plight of the most affected populations, like those in high-income countries in North America, Australasia and Europe, has been well publicized. However, the more recent increases in population obesity in low- and middle-income countries that are now increasingly being observed have been less recognized. Based on the existing prevalence and trend data and the epidemiological evidence linking obesity with a range of physical and psychosocial health conditions, it is reasonable to describe obesity as a public health crisis that severely impairs the health and quality of life of people and adds considerably to national health-care budgets. Intersectoral action to manage and prevent obesity is urgently required to reverse current trends.

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AMPK: positive and negative regulation, and its role in whole-body energy homeostasis.

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The AMP-activated protein kinase (AMPK) is a sensor of energy status that, when activated by metabolic stress, maintains cellular energy homeostasis by switching on catabolic pathways and switching off ATP-consuming processes. Recent results suggest that activation of AMPK by the upstream kinase LKB1 in response to nutrient lack occurs at the surface of the lysosome. AMPK is also crucial in regulation of whole body energy balance, particularly by mediating effects of hormones acting on the hypothalamus. Recent crystal structures of complete AMPK heterotrimers have illuminated its complex mechanisms of activation, involving both allosteric activation and increased net phosphorylation mediated by effects on phosphorylation and dephosphorylation. Finally, AMPK is negatively regulated by phosphorylation of the 'ST loop' within the catalytic subunit. Copyright © 2014. Published by Elsevier Ltd.