Glucosylation of human collagen in aging and diabetes mellitus.

Abstract

A B S T R A C T Several of the characteristic complications of diabetes mellitus resemble age-like changes in collagen-rich tissues. It has been reported that increased glucosylation of hemoglobin and serum proteins occurs in diabetes. Glucosylation of insoluble human tendon collagen, a protein with little or no turnover, was determined by a thiobarbituric acid method in 23 subjects as a function of age and the presence or absence of diabetes. Amounts of glucose and collagen solubilized by collagenase digestion of the samples were also determined. Glucosylation of collagen was found to increase with age and was markedly increased in juvenile onset diabetes. There appeared to be a limit to the amount of glucosylation that could occur, and older individuals with maturity-onset diabetes demonstrated glucosylation within that limit. The glucose nonenzymatically bound to human collagen may indicate the level of long-term control of the diabetes, and may play a role in the alteration of collagenous tissue properties that occurs in both aging and diabetes.

Ultra-structural changes in collagen of penile tunica albuginea in aged and diabetic rats

“…At the same time, these animals have also showed the highest levels of blood glucose levels during this work and now it is well known that an accelerated rate of formation of AGP proceeds when plasma glucose is elevated. 22 So, we agree with those who showed the important link between chronic hyperglycemia and numerous pathophysiologic processes that affect collagen via these AGP. 19 However, we disagree with others who claimed that the severity of ultrastructural changes did not correlate with the longer duration of the disease.…”

Non-enzymatic glycosylation and the chronic complications of diabetes: an overview

“…Increased non-enzymatic glycosylation of diaphragmatic tendon and skin collagens is observed with both age and diabetes in man [59,60]; and, in rats similar effects were noted with aortic and glomerular basement membrane collagens [61,62]. The increased glycosylation of collagen in vivo has been correlated with its decreased solubility, elasticity and sensitivity to protease digestion [60], and increased thermal stability [63], all of which suggest increased crosslinking of collagen in diabetes.…”

Dietary Interventions to Extend Life Span and Health Span Based on Calorie Restriction

“…These compounds were found to attract other proteins and congregate in a web-like network that could stiffen joints, block arteries, and cloud clear tissues like the lens of the eye, leading to cataracts (45). Given the considerable overlap between the complications of diabetes and general ailments associated with aging, it was unsurprising that glycosylated proteins were found to accumulate in normal aging tissues (46). since then, considerable interest has been shown in the potential to identify or develop compounds that could inhibit or reverse the accumulation of these advanced glycation end products (AGEs) as a treatment for complications associated with both diabetes and aging.…”