domingo, 5 de agosto de 2012

Resveratrol Stimulates the Expression of Beneficial Fat Hormone / Up-regulation of Adiponectin by Resveratrol


Fuente: http://www.ahealthblog.com/resveratrol-stimulates-the-expression-of-beneficial-fat-hormone.html


Resveratrol Stimulates the Expression of Beneficial Fat Hormone

Resveratrol-Molecule
Resveratrol Stimulates the Expression of Beneficial Fat Hormone
Resveratrol, a compound in grapes, displays antioxidant and other positive properties. Researchers describe a novel way in which resveratrol exerts these beneficial health effects.
Resveratrol stimulates the expression of adiponectin, a hormone derived from cells that manufacture and store fat, the team found. Adiponectin has a wide range of beneficial effects on obesity-related medical complications, said senior author Feng Liu.
Both adiponectin and resveratrol display anti-obesity, anti-insulin resistance and anti-aging properties.
“Results from these studies should be of interest to those who are obese, diabetic and growing older,” Dr. Liu said. “The findings should also provide important information on the development of novel therapeutic drugs for the treatment of these diseases.”
Previous studies
In July 2009 in the journal Nature, the Barshop Institute and collaborators reported that the compound rapamycin extended life in mice. Rapamycin, like resveratrol, is under scrutiny for its beneficial health effects.
In 2010, Dr. Liu and colleagues announced that resveratrol inhibits activity of the mammalian target of rapamycin (mTOR). This discovery was included in the prestigious Faculty of 1000 (F1000), a service that identifies and evaluates the most important articles in biology and medical research publications. The selection process involves a peer-nominated global “faculty” of the world’s leading scientists and clinicians who rate the best of the articles they read and explain their importance.
A reviewer said the study, which appeared in the Journal of Biological Chemistry, would open up work in a new area: explaining how resveratrol and rapamycin synergistically achieve their results.

Fuente:   http://www.jbc.org/content/286/1/60

Up-regulation of Adiponectin by Resveratrol

THE ESSENTIAL ROLES OF THE Akt/FOXO1 AND AMP-ACTIVATED PROTEIN KINASE SIGNALING PATHWAYS AND DsbA-L*

  1. Feng Liu§,2
+Author Affiliations
  1. From the Metabolic Syndrome Research Center, Second Xiangya Hospital, Central South University, Hunan 410011, China and
  2. the Departments of §Pharmacology,
  3. Cellular and Structural Biology, and
  4. Ophthalmology, University of Texas Health Science Center, San Antonio, Texas 78229
  1. 1 To whom correspondence may be addressed. E-mail: lium2@uthscsa.edu.
  2. 2 To whom correspondence may be addressed. E-mail: liuf@uthscsa.edu.

Abstract

The natural polyphenol resveratrol (RSV) displays a wide spectrum of health beneficial activities, yet the precise mechanisms remain to be fully elucidated. Here we show that RSV promotes the multimerization and cellular levels of adiponectin in 3T3-L1 adipocytes. The stimulatory effect of RSV was not affected by knocking out Sirt1, but was diminished by suppressing the expression levels of DsbA-L, a recently identified adiponectin-interactive protein that promotes adiponectin multimerization. Suppression of the Akt signaling pathway resulted in an increase in the expression levels of DsbA-L and adiponectin. On the other hand, knocking out FOXO1 or suppressing the activity or expression levels of the AMP-activated protein kinase (AMPK) down-regulated DsbA-L and adiponectin. The stimulatory effect of RSV on adiponectin and DsbA-L expression was completely diminished in FOXO1-suppressed and AMPK-inactivated 3T3-L1 adipocytes. Taken together, our results demonstrate that RSV promotes adiponectin multimerization in 3T3-L1 adipocytes via a Sirt1-independent mechanism. In addition, we show that the stimulatory effect of RSV is regulated by both the Akt/FOXO1 and the AMPK signaling pathways. Last, we show that DsbA-L plays a critical role in the promoting effect of RSV on adiponectin multimerization and cellular levels.

Footnotes

  • * This work was supported, in whole or in part, by National Institutes of Health Grants RO1 DK76902 (to F. L.) and DK69930 (to L. Q. D.) and a Research Award from the San Antonio Life Sciences Institute (SALSI) (to T. J. S., R. D. G., and F. L.).
  • Received September 23, 2010.
  • Revision received October 25, 2010.

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