Involvement of AMP-activated protein kinase in glucose uptake stimulated by the globular domain of adiponectin in primary rat adipocytes.

@article{Wu2003InvolvementOA,
  title={Involvement of AMP-activated protein kinase in glucose uptake stimulated by the globular domain of adiponectin in primary rat adipocytes.},
  author={Xiangdong Wu and H. Motoshima and K. Mahadev and T. Stalker and R. Scalia and B. Goldstein},
  journal={Diabetes},
  year={2003},
  volume={52 6},
  pages={
          1355-63
        }
}
Adiponectin is an abundant adipocyte-derived plasma protein with anti-atherosclerotic and insulin-sensitizing properties that suppresses hepatic glucose production and enhances glucose uptake into skeletal muscle. To characterize the potential effects of adiponectin on glucose uptake into adipose cells, we incubated isolated epididymal rat adipocytes with the globular domain of recombinant adiponectin purified from an E. coli expression system. Globular adiponectin increased glucose uptake in… Expand
Adiponectin-mediated stimulation of AMP-activated protein kinase (AMPK) in pancreatic beta cells.
TLDR
It is concluded that adiponectin induces an activation of AMPK in beta cells, which inhibits their cataplerosis of glucose-carbon to lipids. Expand
Acute regulation of 5′-AMP-activated protein kinase by long-chain fatty acid, glucose and insulin in rat primary adipocytes
TLDR
It is suggested that activation of adipocyte AMPK by NEFA, as well as decreasing the activity of hormone-sensitive lipase, could modulate adipose tissue dynamics by increasing FA esterification and, under certain circumstances, FA synthesis. Expand
Adiponectin Stimulates Angiogenesis by Promoting Cross-talk between AMP-activated Protein Kinase and Akt Signaling in Endothelial Cells*
TLDR
Data indicate that adiponectin can function to stimulate the new blood vessel growth by promoting cross-talk between AMP-activated protein kinase and Akt signaling within endothelial cells. Expand
Autocrine action of adiponectin on human fat cells prevents the release of insulin resistance-inducing factors.
TLDR
It is suggested that adiponectin operates as a key regulator of adipocyte secretory function and may prevent the induction of skeletal muscle insulin resistance and may partly explain the antidiabetes action of this hormone. Expand
Globular adiponectin increases GLUT4 translocation and glucose uptake but reduces glycogen synthesis in rat skeletal muscle cells
TLDR
The present study is the first to show that globular adiponectin increases glucose uptake in skeletal muscle cells via GLUT4 translocation and subsequently reduces the rate of glycogen synthesis and shifts glucose metabolism toward lactate production. Expand
Functions of AMP‐activated protein kinase in adipose tissue
TLDR
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. Expand
Globular adiponectin regulates energy homeostasis through AMP-activated protein kinase–acetyl-CoA carboxylase (AMPK/ACC) pathway in the hypothalamus
TLDR
It is suggested that adiponectin regulated energy homeostasis through the AMPK/ACC pathway but not the JAK/STAT3 pathway in the hypothalamus. Expand
Adiponectin deletion impairs insulin signaling in insulin-sensitive but not insulin-resistant 3T3-L1 adipocytes.
TLDR
Prolonged incubation with insulin significantly reduced insulin-stimulated glucose uptake, suggesting the development of insulin resistance and adiponectin mRNA expression in insulin-resistant 3T3-L1 adipocytes. Expand
Role of AMP-activated protein kinase in adipose tissue metabolism and inflammation.
TLDR
The role of AMPK in adipose tissue is discussed, focussing on the regulation of carbohydrate and lipid metabolism, adipogenesis and pro-inflammatory pathways in physiological and pathophysiological conditions. Expand
Regulation of adiponectin receptor gene expression in diabetic mice.
TLDR
The results indicate that regulation of AdipoR1, but not that of AdIPoR2, may be involved in glucose and lipid metabolism in diabetic states. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 65 REFERENCES
Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase
TLDR
It is shown that phosphorylation and activation of the 5′-AMP-activated protein kinase (AMPK) are stimulated with globular and full-length Ad in skeletal muscle and only with full- lengths Ad in the liver, indicating that stimulation of glucose utilization and fatty-acid oxidation by Ad occurs through activation of AMPK. Expand
Characterization of the role of the AMP-activated protein kinase in the stimulation of glucose transport in skeletal muscle cells.
TLDR
It is demonstrated that adenoviral-mediated expression of a constitutively active mutant of AMPK alpha leads to activation of glucose transport in a skeletal-muscle cell line, similar to that seen following treatment with 5-amino-imidazolecarboxamide riboside, hyperosmotic stress or insulin. Expand
Activation of AMPK is essential for AICAR-induced glucose uptake by skeletal muscle but not adipocytes.
TLDR
Overexpression of the wild-type AMPKalpha2 subunit significantly increased AMPK activity in muscle but did not enhance glucose uptake, suggesting that AMPK activation appears essential for AICAR-induced glucose uptake in muscle. Expand
Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
TLDR
It is shown that leptin selectively stimulates phosphorylation and activation of the α2 catalytic subunit of AMPK (α2 AMPK) in skeletal muscle, thus establishing a previously unknown signalling pathway for leptin, and identifying AMPK as a principal mediator of the effects of leptin on fatty-acid metabolism in muscle. Expand
Stimulation of AMP-activated protein kinase (AMPK) is associated with enhancement of Glut1-mediated glucose transport.
TLDR
It is concluded that stimulation of AMPK activity is associated with enhancement of Glut1-mediated glucose transport, and that the glucose transport response is mediated by activation of GlUT1 transporters preexisting in the plasma membrane. Expand
Role of AMP-activated protein kinase in mechanism of metformin action.
TLDR
It is reported that metformin activates AMPK in hepatocytes; as a result, acetyl-CoA carboxylase (ACC) activity is reduced, fatty acid oxidation is induced, and expression of lipogenic enzymes is suppressed. Expand
Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: Acetyl–CoA carboxylase inhibition and AMP-activated protein kinase activation
  • E. Tomás, T. Tsao, +5 authors N. Ruderman
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2002
TLDR
Both in vivo and in vitro, activation of AMPK was the first effect of gACRP30 and was transient, whereas alterations in malonyl CoA and ACC occurred later and were more sustained, indicating that gAC RP30 most likely exerts its actions on muscle fatty acid oxidation by inactivating ACC via activation ofAMPK and perhaps other signal transduction proteins. Expand
Translocation of myocardial GLUT-4 and increased glucose uptake through activation of AMPK by AICAR.
TLDR
It is concluded that AMPK activation increases cardiac muscle glucose uptake through translocation of GLUT-4 via a pathway that is independent of PI3K. Expand
5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) inhibits insulin-stimulated glucose transport in 3T3-L1 adipocytes.
TLDR
It is proposed that in contrast to skeletal muscle, in which AM PK stimulation promotes glucose transport to provide ATP as a fuel, AMPK stimulation inhibits insulin-stimulated glucose transport in adipocytes, inhibiting triacylglycerol synthesis, to conserve ATP under conditions of cellular stress. Expand
Adiponectin, an Adipocyte-Derived Plasma Protein, Inhibits Endothelial NF-&kgr;B Signaling Through a cAMP-Dependent Pathway
TLDR
The possibility that adiponectin, which is naturally present in the blood stream, modulates the inflammatory response of endothelial cells through cross talk between cAMP-PKA and NF-&kgr;B signaling pathways is raised. Expand
...
1
2
3
4
5
...