Glycosylation accelerates albumin degradation in normal and diabetic dogs.
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.
D000818:Animals; D003921:Diabetes Mellitus, Experimental / Q000097:blood*; D004285:Dogs; D017127:Glycation End Products, Advanced; D006207:Half-Life; D007457:Iodine Radioisotopes; D007700:Kinetics; D008297:Male; D011865:Radioisotope Dilution Technique; D012709:Serum Albumin / Q000378:metabolism*; D000093423:Glycated Serum Albumin
D017127:Glycation End Products, Advanced; D007457:Iodine Radioisotopes; D012709:Serum Albumin; D000093423:Glycated Serum Albumin