Age and Ageing · 1996 · 29 citations · 22 references
Life SciencesBiochemistryNutritional SciencesAgingGlycobiologyHuman NutritionDiabetic NephropathyDiabetic RetinopathyGlycan AnalysisGlycan DegradationProtein GlycoengineeringAdvanced Glycation End ProductsAge-related Scleral ChangesCollagen BiologyCollagen Cross-linking ChangesDiabetic ComplicationsMolecular Architecture Of CollagenScleral Collagen OrganizationX-ray Diffraction Analysis
The ageing of connective tissues involves modifications of collagen, which are currently generating much interest amongst protein researchers. Protein glycation, a non-enzymic reaction involving sugar, appears to play a role in the evolution of age-related physical changes and diabetic complications-retinopathy, neuropathy, renal failure and atherosclerosis. Our studies show that the glycation of human corneal and scleral collagen produces increases in the collagen intermolecular spacing-these increases are similar to those we previously reported on the ageing of collagen in these tissues. The present investigation employs X-ray diffraction to look at the structural effects of various substances that are believed in inhibit protein glycation. Aspirin-like compounds and certain vitamins successfully prevented the sugar-induced molecular changes from occurring in corneal and scleral collagen, suggesting that such compounds could have a useful role in this aspect of ageing.
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Vitamin E Consumption and the Risk of Coronary Disease in Women
Meir J. Stampfer, Charles H. Hennekens, JoAnn E. Manson et al. · New England Journal of Medicine · 1993 · 2.1K citations · Full text
Aminoguanidine Prevents Diabetes-Induced Arterial Wall Protein Cross-Linking
M. Brownlee, Helen Vlassara, A. Kooney et al. · Science · 1986 · 1.1K citations