Decrease in skin collagen glycation with improved glycemic control in patients with insulin-dependent diabetes mellitus.

Lyons, Timothy J.; Bailie, K.; Dyer, Daniel G.; Dunn, John A.; Baynes, John W.

doi:10.1172/jci115216

Cited by 126 publications

(85 citation statements)

References 31 publications

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“…The data support the assumption that the formation of collagen FL is in equilibrium with ambient glucose concentrations [5]. Glycation alone may have a pathogenic role in the development of diabetic complications, and collagen FL is a predictor of complications in DCCT subjects [21,22].…”

Section: Collagen Glycation Glycaemic Control and Complicationssupporting

confidence: 77%

“…It has been suggested that collagen glycation may directly reflect cumulative glycaemia for at least 1 year before measurement [21]. However, our earlier study of type 1 diabetic patients showed that 4 months of intensive therapy decreased skin collagen FL by 25%, while having no effect on levels of collagen AGEs [5].…”

Section: Collagen Glycation Glycaemic Control and Complicationsmentioning

confidence: 69%

“…In diabetes, levels of glycation and AGE products are increased in long-lived proteins such as collagen [5,6]. Since AGE formation involves free radical oxidation as well as glycation, AGE levels may be used to assess cumulative oxidative stress if corrected for long-term glycaemia.…”

Section: Discussionmentioning

confidence: 99%

“…Particularly in long-lived structural proteins such as collagen, it may be difficult to estimate the contribution of these variables to the accumulation of AGEs. Levels of FL in collagen are in equilibrium with ambient glucose [5], but AGEs accumulate steadily with age, and at an accelerated rate in diabetes [6]. Previous studies found that agecorrected skin collagen concentrations of pentosidine and CML, and Maillard-type fluorescence correlated with the severity of microvascular complications in type 1 diabetes [6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

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Advanced glycation end-products and methionine sulphoxide in skin collagen of patients with type 1 diabetes

Thorpe

Jenkins

et al. 2006

Diabetologia

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Aims/hypothesis We determined whether oxidative damage in collagen is increased in (1) patients with diabetes; (2) patients with diabetic complications; and (3) subjects from the Diabetes Control and Complications Trial (DCCT)/Epidemiology of Diabetes Interventions and Complications (EDIC) study, with comparison of subjects from the former standard vs intensive treatment groups 4 years after DCCT completion. Subjects, materials and methods We quantified the early glycation product fructose-lysine, the two AGEs N ɛ -(carboxymethyl)lysine (CML) and pentosidine, and the oxidised amino acid methionine sulphoxide (MetSO) in skin collagen from 96 patients with type 1 diabetes (taken from three groups: DCCT/EDIC patients and clinic patients from South Carolina and Scotland) and from 78 healthy subjects. Results Fructose-lysine was increased in diabetic patients (p<0.0001), both with or without complications (p<0.0001).Controlling for HbA 1c , rates of accumulation of AGEs were higher in diabetic patients than control subjects, regardless of whether the former had complications (CML and pentosidine given as log e [pentosidine]) or not (CML only) (all p<0.0001). MetSO (log e [MetSO]) also accumulated more rapidly in diabetic patients with complications than in controls (p<0.0001), but rates were similar in patients without complications and controls. For all three products, rates of accumulation with age were significantly higher in diabetic patients with complications than in those without (all p<0.0001). At 4 years after the end of the DCCT, no differences were found between the previous DCCT management groups for fructose-lysine, AGEs or MetSO. Conclusions/interpretation The findings suggest that in type 1 diabetic patients enhanced oxidative damage to collagen is associated with the presence of vascular complications.

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Section: Collagen Glycation Glycaemic Control and Complicationssupporting

confidence: 77%

Section: Collagen Glycation Glycaemic Control and Complicationsmentioning

confidence: 69%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Advanced glycation end-products and methionine sulphoxide in skin collagen of patients with type 1 diabetes

Thorpe

Jenkins

et al. 2006

Diabetologia

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“…This may, in part, explain the W. G. JOHN AND E. J. LAMB failure to observe a decrease in skin collagen pentosidine following institution of improved glycaemic control in diabetics. 40 Alternatively, Baynes41 has suggested that pentosidine is the result of an oxidative reaction between lysine and arginine. In addition to these AGE products, two further pyrrole-related compounds have been described and structures proposed.…”

Section: Biochemistry Of the Late Maillard Reactionmentioning

confidence: 99%

The maillard or browning reaction in diabetes

John¹,

Lamb²

1993

Eye

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A major pathophysiological consequence of hyperglycae mia is the extensive chemical interaction of glucose with proteins, leading to its attachment to these proteins with out the aid of enzymes. Even though the Maillard reac tions have been of considerable interest to food chemists since the tum of the century,' it has only been relatively recently that attention has focused on non-enzymic glyca tion of proteins in vivo. Although non-enzymic glycation leading to formation of reversible Amadori products acts on many proteins throughout the body, it is less obvious how these products are related to the pathophysiology of diabetic complications. Recent efforts have focused on biologically important further products of the glycation reaction, which are derived slowly from the Amadori product following a sequence of further reactions and rearrangements? These compounds, in contrast to the Amadori product, are formed irreversibly resulting in accumulation on long-lived proteins; these have been called advanced glycation end (AGE) products. BIOCHEMISTRY OF THE EARLY MAILLARD REACTIONThe initial Maillard reaction is the condensation of the free aldehyde group of carbohydrate with either the f-amino group of lysine or hydroxylysine residues or the a-amino group of the N-terminal amino acid of proteins.2 Only open forms of sugars react with proteins, the carbonyl group of an acyclic monosaccharide attaching to a protein amino group via nucleophilic attack to form a labile aldi mine (Schiff base).2 This product may hydrolyse back to glucose and protein or undergo an Amadori rearrange ment to form a l-amino-I-deoxyfructose (fructosamine) derivative by a stable, though slightly reversible, keto amine linkage (Fig. 1). This product can cyclise to a ring structure (N-substituted-I-amino-deoxyketopyranose ).2The rate of the Amadori rearrangement is approximately one-sixtieth that of the dissociation to glucose and protein3 and also varies between proteins: for example, the Ama- dori rearrangement occurs about five times more rapidly in albumin than in haemoglobin.4 The labile Schiff base form can also exist as a cyclic glucose adduct (N-substituted aldosylamine) and in vivo proteins will exist predom inantly in the cyclic form of both the Schiff base and the Amadori product, although the labile form is probably lost in most purification procedures.4Glycation of haemoglobin is somewhat atypical, as this reaction occurs predominantly between glucose and the N-terminal valine of the �-chain of haemoglobin to form HbA,/ on other proteins glucose adducts are found on lysine and hydroxylysine residues.2 A variety of other aldose and ketose sugars, including glucose-6-phosphate, galactose, mannose, ribose, fructose and xylulose, can participate in the glycation reaction.6 The relative reactiv ity varies up to 300-fold between monosaccharides and depends largely on the equilibrium between the reactive open (carbonyl) and closed (hemiacetal) configurations of the sugar. Aldose sugars react more rapidly than ketose sugars since the aldeh...

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Biochemical Abnormalities in Vitreous of Humans With Proliferative Diabetic Retinopathy

Sebag

Buckingham²,

Charles³

et al. 1992

Arch Ophthalmol

152

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Decrease in skin collagen glycation with improved glycemic control in patients with insulin-dependent diabetes mellitus.

Cited by 126 publications

References 31 publications

Advanced glycation end-products and methionine sulphoxide in skin collagen of patients with type 1 diabetes

Advanced glycation end-products and methionine sulphoxide in skin collagen of patients with type 1 diabetes

The maillard or browning reaction in diabetes

Biochemical Abnormalities in Vitreous of Humans With Proliferative Diabetic Retinopathy

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