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Acute regulation of 5'-AMP-activated protein kinase by long-chain fatty acid, glucose and insulin in rat primary adipocytes.

ABSTRACT: Palmitate increased AMPK (5'-AMP-activated protein kinase) activity, glucose utilization and 2-DOG (2-deoxyglucose) transport in rat adipocytes. All three effects were blocked by the AMPK inhibitor Compound C, leading to the conclusion that in response to an increase in long-chain NEFA (non-esterified fatty acid) concentration AMPK mediated an enhancement of adipocyte glucose transport, thereby providing increased glycerol 3-phosphate for FA (fatty acid) esterification to TAG (triacylglycerol). Activation of AMPK in response to palmitate was not due to an increase in the adipocyte AMP:ATP ratio. Glucose decreased AMPK activity and effects of palmitate and glucose on AMPK activity were antagonistic. While insulin had no effect on basal AMPK activity insulin did decrease AMPK activity in the presence of palmitate and also decreased the percentage effectiveness of palmitate to increase the transport of 2-DOG. 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.

SUBMITTER: Hebbachi A

PROVIDER: S-EPMC3522478 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Acute regulation of 5'-AMP-activated protein kinase by long-chain fatty acid, glucose and insulin in rat primary adipocytes.

Hebbachi Abdel A Saggerson David D

Bioscience reports 20121213 1

Palmitate increased AMPK (5'-AMP-activated protein kinase) activity, glucose utilization and 2-DOG (2-deoxyglucose) transport in rat adipocytes. All three effects were blocked by the AMPK inhibitor Compound C, leading to the conclusion that in response to an increase in long-chain NEFA (non-esterified fatty acid) concentration AMPK mediated an enhancement of adipocyte glucose transport, thereby providing increased glycerol 3-phosphate for FA (fatty acid) esterification to TAG (triacylglycerol). ...[more]

PMID: 23095119

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Project description:ObjectiveIntestinal barrier function is vital for homeostasis. Conditions where the mucosal barrier is compromised lead to increased plasma content of lipopolysaccharide (LPS). LPS acts on Toll-like receptor 4 (TLR4) and initiates cellular inflammatory responses. TLR4 receptors have been identified on enteric neurons and LPS exposure causes neuronal loss, counteracted by vasoactive intestinal peptide (VIP), by unknown mechanisms. In addition AMP activated protein kinase (AMPK) stimulation causes loss of enteric neurons. This study investigated a possible role of AMPK activation in LPS-induced neuronal loss.DesignPrimary cultures of myenteric neurons isolated from rat small intestine were used. Cultures were treated with LPS (0.2-20 µg/mL) with and without TAK1-inhibitor (5Z)-7-Oxozeaenol (10-6 M) or AMPK inhibitor compound C (10-5 M). AMPK-induced neuronal loss was verified treating cultures with three different AMPK activators, AICAR (10-4-3×10-3 M), metformin (0.2-20 µg/mL) and A-769662 (10-5-3×10-4 M) with or without the presence of compound C (10-5 M). Upstream activation of AMPK-induced neuronal loss was tested by treating cultures with AICAR (10-3 M) in the presence of TAK1 inhibitor (5Z)-7-Oxozeaenol (10-6 M). Neuronal survival and relative numbers of neurons immunoreactive (IR) for VIP were evaluated using immunocytochemistry.ResultsLPS caused a concentration dependent loss of neurons. All AMPK activators induced loss of myenteric neurons in a concentration dependent manner. LPS-, AICAR- and metformin-,but not A-769662-, induced neuronal losses were inhibited by presence of compound C. LPS, AICAR or metformin exposure increased the relative number of VIP-IR neurons; co-treatment with (5Z)-7-Oxozeaenol or compound C reversed the relative increase in VIP-IR neurons induced by LPS. (5Z)-7-Oxozeaenol, compound C or A-769662 did not per se change neuronal survival or relative numbers of VIP-IR neurons.ConclusionAMPK activation mimics LPS-induced loss of cultured myenteric neurons and LPS-induced neuronal loss is counteracted by TAK1 and AMPK inhibition. This suggests enteric neuroimmune interactions involving AMPK regulation.

Dataset Information

Acute regulation of 5'-AMP-activated protein kinase by long-chain fatty acid, glucose and insulin in rat primary adipocytes.

Publications

Acute regulation of 5'-AMP-activated protein kinase by long-chain fatty acid, glucose and insulin in rat primary adipocytes.

Similar Datasets

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