Medical Journals

Functions of Amp-activated Protein Kinase in Adipose Tissue.

Authors:
  • Daval Marie
  • Foufelle Fabienne
  • Ferré Pascal

From: INSERM Unit 671, Paris 75006, France.

The Journal of physiology

  • Publish Date: Jul 2006
  • ISSN: 0022-3751
  • Volume: 574
  • Issue: Pt 1
  • Pages: 55-62
  • Medium: Print
  • Language: English
  • Citation (JAMA): Daval Marie, Foufelle Fabienne, Ferré Pascal, et al. Functions of Amp-activated Protein Kinase in Adipose Tissue.. J. Physiol. (Lond.) Jul 2006;574:55-62

Abstract

AMP-activated protein kinase (AMPK) is involved in cellular energy homeostasis. Its functions have been extensively studied in muscles and liver. AMPK stimulates pathways which increase energy production (glucose transport, fatty acid oxidation) and switches off pathways which consume energy (lipogenesis, protein synthesis, gluconeogenesis). This has led to the concept that AMPK has an interesting pharmaceutical potential in situations of insulin resistance and it is indeed the target of existing drugs and hormones which improve insulin sensitivity. Adipose tissue is a key player in energy metabolism through the release of substrates and hormones involved in metabolism and insulin sensitivity. Activation of AMPK in adipose tissue can be achieved through situations such as fasting and exercise. Leptin and adiponectin as well as hypoglycaemic drugs are activators of adipose tissue AMPK. This activation probably involves changes in the AMP/ATP ratio and the upstream kinase LKB1. When activated, AMPK limits fatty acid efflux from adipocytes and favours local fatty acid oxidation. Since fatty acids have a key role in insulin resistance, especially in muscles, activating AMPK in adipose tissue might be found to be beneficial in insulin-resistant states, particularly as AMPK activation also reduces cytokine secretion in adipocytes.

Mesh Headings (Keywords): Adipose Tissue, Animals, Fatty Acids, Glucose, Humans, Lipid Metabolism, Multienzyme Complexes, Muscle, Skeletal, Protein-Serine-Threonine Kinases


Check for Full Text / PubMed Unique Identifier (PMID): 16709632


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.

The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


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