Increased glycosylation of glomerular basement membrane collagen in diabetes

Cohen, Morrel H.; Urdanivia, Enrique; Surma, Maria Linda; Wu, Van-Yu

doi:10.1016/0006-291x(80)90852-9

Cited by 146 publications

(53 citation statements)

References 22 publications

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“…Small amounts of the SchifTs base intermediates formed between glucose and hydroxylysine or lysine, which are re duced to glucitol-hydroxylysine and glucitol-lysine with borohydride and thus labeled with NaB'H4, are also apparently present. Previous studies have demonstrated that glucose can condense in vivo with GBM col lagen in a nonenzymatic reaction analogous to that described for other proteins [24,27], and that glucitol-lysine and glucitol-hydrox ylysine are products of this nonenzymatic glucosylation [24], The demonstration that [IJC]-lysine is incorporated into di-OHLNL and glucosylamines corroborates the iden tity of these compounds and their derivation from lysine. The presence of additional [M C]-lysine-labeled compounds suggests that GBM contains other lysine-derived cross-links, including OHLNL and LNL.…”

Section: Discussionsupporting

confidence: 48%

Intermolecular Reducible Cross-Links in Rat Glomerular Basement Membrane

Wu¹,

Cohen²

1983

Kidney Blood Press Res

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Glomerular basement membrane (GBM) was purified from adult rats and treated with tritiated borohyride for analysis of the reducible cross-links. After acid hydrolysis, samples were subjected, with and without prior gel filtration on Biogel P-2, to a chromatographic system standardized with known cross-links. The major peak of radioactivity co-eluted with authentic di-hydroxylysinonorleucine (di-OHLNL) standard. Derivation of this cross-link from lysine was corroborated by demonstrating its presence in GBM purified after incubation of isolated glomeruli with [¹⁴C]-lysine and after in vivo injection of [¹⁴C]-lysine. GBM labeled in vitro with radioactive lysine also contained peaks co-eluting with hydroxylysinonorleucine and lysinonorleucine standards, as well as at unidentified positions in the chromatogram. The findings indicate that rat GBM contains lysine-derived cross-links, of which di-OHLNL is the major reduced form.

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Section: Discussionsupporting

confidence: 48%

Intermolecular Reducible Cross-Links in Rat Glomerular Basement Membrane

Wu¹,

Cohen²

1983

Kidney Blood Press Res

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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 is an increased glucosylation of insoluble collagen from tendon (13) and skin of human diabetics. 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).…”

Section: Discussionmentioning

confidence: 95%

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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Increased glycosylation of glomerular basement membrane collagen in diabetes

Cited by 146 publications

References 22 publications

Intermolecular Reducible Cross-Links in Rat Glomerular Basement Membrane

Intermolecular Reducible Cross-Links in Rat Glomerular Basement Membrane

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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