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Papers In Press, published online ahead of print August 9, 2002
Department of Medicine, University of California, Los Angeles, Los Angeles, CA 90024
Corresponding Author: ikurland{at}mednet.ucla.edu
The hypoglycemia seen in the fasting PPAR
J. Biol. Chem, 10.1074/jbc.M201208200
Submitted on February 6, 2002
Revised on August 6, 2002
Accepted on August 9, 2002
PPAR
influences substrate utilization for hepatic glucose production
null mouse is thought to reflect a depletion of liver glycogen, and a decrease in gluconeogenesis secondary to impaired liver fatty acid beta-oxidation. The etiology of hypoglycemia in the PPAR null mouse was determined via stable isotope studies. Glucose, lactate and glycerol flux was assessed in the fasted and fed states in 4-month old PPAR null mice, and C57BL/6 controls (WT), using a new protocol for flux assessment in the fasted and fed states. Hepatic glucose production (HGP), and glucose carbon recycling , were estimated using [U-13C6] glucose; and HGP, lactate, and glycerol turnover was estimated utilizing either [U-13C3] lactate or [2-13C] glycerol, infused subcutaneously via Alza mini-osmostic pumps. . At the end of a 17-hour fast, HGP was higher in the PPAR null mice than in WT by 37% (p<0.01). However, recycling of glucose carbon from lactate, back to glucose, was lower in the PPAR null than WT (39% vs. 51%, p<0.02). In the fasted state, HGP from lactate, and lactate production, measured using an [U-13C3] lactate infusion, were decreased by 65% and 55%, respectively (p<0.05) in PPAR null mice. In contrast, when [2-13C] glycerol was infused, glycerol production and HGP from glycerol increased by 80% and 250%, respectively, (p<0.01), in the fasted state of PPAR null mice. The increased HGP from glycerol was not suppressed in the fed state. The fasted and fed insulin levels were comparable, but blood glucose levels were lower in the PPAR null mice than controls. In conclusion, PPAR receptor function creates a setpoint for a metabolic network that regulates the rate and route of HGP in the fasted and fed states, in part, by controlling the flux of glycerol and lactate between the triose-phosphate and pyruvate/lactate pools.
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