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A new method for quantifying glucose transport in human red blood cells is described. In this method, glucose transport is determined by fluorescence quenching of NBD-glucose with red cell glucose-6-phosphate dehydrogenase. NBD-glucose transport was consistent with a simple diffusion model, and no cooperative interactions between the hexose carriers were detected. At 25 degrees C, the apparent equilibrium dissociation constant of the NBD-glucose-glucose-6-phosphate dehydrogenase reaction was 4.7 microM, and the maximum rate of transport was 4.67 pmol.mg protein-1.min-1. The maximum transport velocity was 0.11 nmol/min per 2.5 million cells. An analysis of the substrate interaction between hexose transport and glycolysis is described.Peroxisome proliferator-activated receptor gamma (PPARgamma) is the founding member of a new family of nuclear hormone receptors. These receptors bind to peroxisome proliferator response elements (PPRE) in the promotors of target genes. PPARgamma is expressed in many cell types and is activated by fatty acids and the prostaglandins. PPARgamma belongs to the group of peroxisome proliferator activated receptors (PPARs) that are known to be involved in a variety of physiological processes. PPARgamma agonists have been shown to be beneficial in the treatment of type II diabetes.
In humans, PPARgamma consists of three isoforms (PPARgamma1, PPARgamma2, and PPARgamma3), encoded by three different genes. The distinct biological functions and tissue-specific expression patterns of the three isoforms are the result of alternative splicing of their primary transcript, and subsequent differential