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Diabetes Publish Ahead of Print published online ahead of print June 6, 2002
DOI: 10.2337/diabetes.51.7.2005
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Received for publication 6 March 2002
Accepted in revised form 6 May 2002

Lipid-Induced Insulin Resistance in Human Muscle Is Associated With Changes in Diacylglycerol, Protein Kinase C, and I{kappa}B-{alpha}

Samar I. Itani 1 , Neil B. Ruderman 1 , Frank Schmieder 2 , and Guenther Boden 3 *

From the 1 Diabetes Unit, Section of Endocrinology and Departments of Medicine and Physiology, Boston University Medical Center, Boston, Massachusetts, 2 Department of Surgery and the General Clinical Research Center, Temple University Hospital, Philadelphia, Pennsylvania, and 3 Division of Endocrinology, Diabetes, and Metabolism and the General Clinical Research Center, Temple University Hospital, Philadelphia, Pennsylvania

* Address correspondence and reprint requests to Guenther Boden. Email: bodengh{at}tuhs.temple.edu.

The possibility that lipid-induced insulin resistance in human muscle is related to alterations in diacylglycerol (DAG)/protein kinase C (PKC) signaling was investigated in normal volunteers during euglycemic-hyperinsulinemic clamping in which plasma free fatty acid (FFA) levels were increased by a lipid/heparin infusion. In keeping with previous reports, rates of insulin-stimulated glucose disappearance (GRd) were normal after 2 h but were reduced by 43% (from 52.7 ± 8.2 to 30.0 ± 5.3 µmol · kg--1 · min--1, P < 0.05) after 6 h of lipid infusion. No changes in PKC activity or DAG mass were seen in muscle biopsy samples after 2 h of lipid infusion; however, at ~6 h, PKC activity and DAG mass were increased approximately fourfold, as were the abundance of membrane-associated PKC-ßII and -{delta}. A threefold increase in membrane-associated PKC-ßII was also observed at ~2 h but was not statistically significant (P = 0.058). Ceramide mass was not changed at either time point. To evaluate whether the fatty acid--induced insulin activation of PKC was associated with a change in the IkB kinase (IKK)/nuclear factor (NF)-{kappa}B pathway, we determined the abundance in muscle of I{kappa}B-{alpha}, an inhibitor of NF-{kappa}B that is degraded after its phosphorylation by IKK. In parallel with the changes in DAG/PKC, no change in I{kappa}B-{alpha} mass was observed after 2 h of lipid infusion, but at ~6 h, I{kappa}B-{alpha} was diminished by 70%. In summary, the results indicated that the insulin resistance observed in human muscle when plasma FFA levels were elevated during euglycemic-hyperinsulinemic clamping was associated with increases in DAG mass and membrane-associated PKC-ßII and -{delta} and a decrease in I{kappa}B-{alpha}. Whether acute FFA-induced insulin resistance in human skeletal muscle is caused by the activation of these specific PKC isoforms and the IKK-ß/I{kappa}B/NF{kappa}B pathway remains to be established.


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