Glycosylation accelerates albumin degradation in normal and diabetic dogs

Biochem Med Metab Biol. 1986 Jun;35(3):267-70. doi: 10.1016/0885-4505(86)90082-4.

Abstract

Nonenzymatic glycosylation of albumin was associated with an increased catabolic rate and decreased protein half-life in both normal and diabetic animals. The fractional catabolic rate of glycosylated albumin was increased significantly over albumin, from 0.100 +/- 0.004/day to 0.131 +/- 0.007/day in normal animals and from 0.104 +/- 0.004/day to 0.138 +/- 0.007/day when these animals were made diabetic with alloxan. The half-lives of Alb and GlyAlb in normal dogs were 6.81 +/- 0.12 days and 4.97 +/- 0.21 days, respectively. In diabetic animals, the half-lives of Alb and GlyAlb were 7.48 +/- 0.21 and 5.21 +/- 0.24 days, respectively. The increased catabolism of GlyAlb may reflect chronic increased extravasation of glycosylated plasma proteins, which are known to be increased in diabetes, into the microvascular wall.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Diabetes Mellitus, Experimental / blood*
  • Dogs
  • Half-Life
  • Iodine Radioisotopes
  • Kinetics
  • Male
  • Radioisotope Dilution Technique
  • Serum Albumin / metabolism*

Substances

  • Iodine Radioisotopes
  • Serum Albumin
  • glycosylated serum albumin