Glyburide protein binding and the effect of albumin glycation in children, young adults, and older adults with diabetes.

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Olsen KM, Kearns GL, Kemp SF

Glyburide protein binding and the effect of albumin glycation in children, young adults, and older adults with diabetes.

J Clin Pharmacol. 1995 Jul;35(7):739-45.

PubMed ID
7560255 [ View in PubMed
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Abstract

Because glyburide is a weak acid that is more than 98% bound to albumin, the authors evaluated the binding in vitro and the influence of albumin glycation in children, young adults, and older adults with diabetes mellitus. Glyburide binding to non-glycated albumin was greater than 98%, and remained constant over a total concentration range of 50 to 1000 ng/mL. Increasing the albumin concentration from 0.5 to 5.0 g/dL was logarithmically related to the free fraction of glyburide. After the in vitro glycation of albumin (range, 5.7-15.6%), mean (+/- SD) glyburide binding was 99.05 +/- 0.082%, a value in agreement with that obtained from control serum. Serum samples from 57 subjects with type I and 16 patients with type II diabetes were incubated with 300 ng/mL of unlabeled glyburide and 200 ng/mL of 14C-glyburide. The extent of albumin glycation varied from 5 to 22% for the type I subjects and 5 to 14% for the type II subjects. The free fraction from these groups ranged from 1.07 to 1.75% and 0.66 to 0.88% for the type I and type II subjects, respectively. Although these values did not differ significantly from those of the control samples, the glyburide free fraction in patients with type I diabetes (1.39 +/- 0.85%) was significantly greater than that found for the 16 elderly patients with type II diabetes (0.78 +/- 0.05%). A significant linear relationship was not found between glyburide free fraction and the degree of albumin glycation for either group. Glyburide protein binding did not appear to be influenced by the extent of albumin glycation.

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