Administration of an aldose reductase inhibitor induces a decrease of collagen fluorescence in diabetic rats.

As a consequence of an increased flux through the sorbitol pathway fructose levels rise in various tissues in diabetes. Also, in vitro nonenzymatic fructosylation of protein induces the generation of fluorescence at a rate 10 times greater than glucosylation. The administration of sorbinil, an aldose reductase inhibitor known to lower tissue fructose concentration, to experimental diabetic rats led to a decrease in the fluorescence related to advanced Maillard products in their skin collagen.

Insulin binding to isolated liver nuclei from obese and lean mice.

Nuclei isolated from the livers of mice are capable of binding [125I]insulin. A class of high-affinity binding sites having a Kd of 1--2 nM and a capacity of approximately 2000 insulin molecules/nucleus are present on these nuclei. Removal of nuclear membranes by Triton X-100 treatment of the nuclei reduces or eliminates the high-affinity binding sites.

Activation of the rat liver glucocorticoid--receptor complex.

The rat liver glucorcorticoid receptor has been activated using three procedures: heat, gel filtration, and dilution. With time after heat activation the steroid--receptor complex loses its capacity to bind to DNA--cellulose, while receptor activated by Sephadex G-25 and by dilution maintains DNA--cellulose binding capacity. The rates of steroid dissociation from nonactivated and activated receptor and essentially identical.