Glycosylated collagen

Rosenberg, H.; Modrak, John B.; Hassing, Jeanne M.; Al‐Turk, Walid A.; Stohs, Sidney J.

doi:10.1016/0006-291x(79)91549-3

Cited by 95 publications

(21 citation statements)

References 12 publications

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“…A possible explanation for this is that in postmature insoluble tendon collagen there is a limited number of sites available for glucosylation and that these sites are occupied early during the course of hyperglycemia. In support of this hypothesis, the amount of ketoamine-linked glucose released per microgram digested collagen was the same in the 61.9-yr-old sub- (14) in which streptozotocin induced diabetes in rats was found to result in an increased glucosylation of aortic collagenous material. The purity of their collagen preparation, however, was not documented.…”

Section: Discussionsupporting

confidence: 55%

Glucosylation of human collagen in aging and diabetes mellitus.

Schnider¹,

Kohn²

1980

J. Clin. Invest.

200

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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.

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Section: Discussionsupporting

confidence: 55%

Glucosylation of human collagen in aging and diabetes mellitus.

Schnider¹,

Kohn²

1980

J. Clin. Invest.

200

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“…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.…”

Section: Extracellular Matrix Proteinsmentioning

confidence: 85%

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

Kennedy¹,

1984

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“…There are also reports of increased glucosylation of a collagenous fraction isolated from glomerular basement membrane of human diabetics (36) and from rats with streptozotocin-induced hyperglycemia (37). It has also been reported that nonenzymatic glucosylation of rat aortic collagenous material is increased in streptozotocin-induced hyperglycemia (38). It has not been demonstrated, however, that glucosylation of collagen results in the observed altered properties of collagen occurring with age and accelerated in diabetes (i.e., solubility and collagenase digestibility).…”

Section: Discussionmentioning

confidence: 96%

Effects of age and diabetes mellitus on the solubility and nonenzymatic glucosylation of human skin collagen.

Schnider¹,

Kohn²

1981

J. Clin. Invest.

312

112

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A B S T R A C T Collagen from human skin was fractionated into neutral salt-soluble, acid-soluble, pepsinreleased, and insoluble fractions. No age-related changes were observed in the proportion ofcollagen extracted by neutral salt. A significant age-related decrease in the proportion of acid-soluble collagen was found. A highly significant (P < 0.001) agerelated decrease in the amount of collagen released by pepsini digestion was observed, with a concomitant age-related increase in the fraction of insoluble collagen. The amount of ketoamine-linked glucose bound to this insoluble collagen also increased significantly with age.Skin collagen from three juvenile onset diabetics (JOD) and one young maturity onset diabetic (MOD) appeared to have undergone accelerated aging. JOD and the young MOD had significantly less collagen released by pepsin digestion and significantly more insoluble collagen than would be predicted by their ages. The collagen released by pepsin digestion of the diabetic samples had more high molecular weight components than similar fractions obtained from agematched nondiabetic controls. There was also more ketoamine-linked glucose bound to the insoluble collagen of JOD than to that fraction from comparably aged control subjects. The apparent acceleration of collagen aging in diabetes mellitus may play a role in complications of diabetes that occur in collagenrich tissues.

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Glycosylated collagen

Cited by 95 publications

References 12 publications

Glucosylation of human collagen in aging and diabetes mellitus.

Glucosylation of human collagen in aging and diabetes mellitus.

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

Effects of age and diabetes mellitus on the solubility and nonenzymatic glucosylation of human skin collagen.

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