c-Jun N-terminal kinase 1/2 activation by tumor necrosis factor-alpha induces insulin resistance in human visceral but not subcutaneous adipocytes: reversal by liver X receptor agonists

J Clin Endocrinol Metab. 2009 Sep;94(9):3583-93. doi: 10.1210/jc.2009-0558. Epub 2009 Jun 30.

Abstract

Aims: Obesity is associated with a chronic systemic low-grade inflammatory state. Markers of inflammation such as TNF-alpha are linked with increased risk for insulin resistance and type 2 diabetes. The objective of the present study was to dissect the molecular mechanisms that may regulate TNF-alpha-induced insulin resistance in human adipose tissue.

Methods: We analyzed the impact of TNF-alpha on glucose uptake and insulin action in human visceral and sc adipocytes. The contribution of different intracellular signaling pathways on metabolic effects of TNF-alpha and the reversal of some of these effects with nuclear receptor agonists were also studied.

Results: TNF-alpha per se increased glucose transporter-4 translocation to the plasma membrane and glucose uptake by activating the AMP-activated protein kinase/AS160 pathway in both visceral and sc adipocytes. Nevertheless, this cytokine induced an insulin-resistant state in visceral adipocytes by impairing insulin-stimulated glucose uptake and insulin signaling at the insulin receptor substrate (IRS)-1/AKT level. Activation of c-Jun N-terminal kinase (JNK) 1/2 seems to be involved in TNF-alpha-induced insulin resistance, causing phosphorylation of IRS1 at the Ser312 residue. Accordingly, silencing JNK1/2 with either small interfering RNA or chemical inhibitors impaired serine phosphorylation of IRS1, restored downstream insulin signaling, and normalized insulin-induced glucose uptake in the presence of TNF-alpha. Furthermore, TNF-alpha increased the secretion of other proinflammatory cytokines such as IL-6. Pharmacological treatment of adipocytes with liver X receptor agonists reestablished insulin sensitivity by impairing TNF-alpha induction of JNK1/2, phosphorylation of IRS1 (Ser312), and stabilizing IL-6 secretion.

Conclusions: TNF-alpha induces insulin resistance on glucose uptake in human visceral but not sc adipocytes, suggesting depot-specific effects of TNF-alpha on glucose uptake. Activation of JNK1/2 appears to be involved in serine phosphorylation of IRS1 and subsequently insulin resistance on glucose uptake, a state that can be reversed by liver X receptor agonists.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases / physiology
  • Adipocytes / metabolism*
  • Cell Line, Tumor
  • DNA-Binding Proteins / agonists*
  • Glucose / metabolism
  • Glucose Transporter Type 1 / analysis
  • Glucose Transporter Type 4 / analysis
  • Humans
  • Insulin Receptor Substrate Proteins / physiology
  • Insulin Resistance*
  • Intra-Abdominal Fat / metabolism*
  • Liver X Receptors
  • Mitogen-Activated Protein Kinase 8 / metabolism*
  • Mitogen-Activated Protein Kinase 9 / metabolism*
  • Orphan Nuclear Receptors
  • Proto-Oncogene Proteins c-akt / physiology
  • Receptors, Cytoplasmic and Nuclear / agonists*
  • Signal Transduction
  • Subcutaneous Fat / metabolism*
  • Tumor Necrosis Factor-alpha / pharmacology*

Substances

  • DNA-Binding Proteins
  • Glucose Transporter Type 1
  • Glucose Transporter Type 4
  • IRS1 protein, human
  • Insulin Receptor Substrate Proteins
  • Liver X Receptors
  • Orphan Nuclear Receptors
  • Receptors, Cytoplasmic and Nuclear
  • SLC2A1 protein, human
  • SLC2A4 protein, human
  • Tumor Necrosis Factor-alpha
  • Mitogen-Activated Protein Kinase 9
  • Proto-Oncogene Proteins c-akt
  • Mitogen-Activated Protein Kinase 8
  • AMP-Activated Protein Kinases
  • Glucose