Key result
Type I poorly controlled diabetes was associated with much greater nonenzymatic glycation of platelet membrane proteins compared to nondiabetics (1.58 vs 0.37 nmol/mg protein).
Case-Control (n=23)
Platelet membrane proteins undergo nonenzymatic glycation, which is significantly elevated in patients with poorly controlled type I diabetes and may contribute to altered platelet function.
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May link glycation to altered platelet function in type 1 diabetes; hypothesis-generating and requires prospective validation.
Human platelet membrane proteins (PMP), incubated in vitro in the presence of various concentrations of glucose, undergo nonenzymatic glycation, as evidenced by incorporation of [3-3H]glucose radioactivity into the acid-precipitable fraction. The time course of the reaction is linear for the first hours, and the rate of glycation depends on the glucose concentration in the medium: at a glucose concentration of 80 mmol/L, up to 60 nmol of glucose is bound per milligram of PMP. The ketoaminic nature of the glucose/protein linkages was demonstrated by the finding of 5-hydroxymethylfurfuraldehyde by liquid-chromatographic analysis of acid hydrolysates of PMP. We analyzed PMP from 13 subjects with type I poorly controlled diabetes and from 10 nondiabetics. Nonenzymatic glycation, evaluated as nanomoles of the aldehyde per milligram of protein, was much greater in diabetic patients than in nondiabetics: 1.58 +/- 0.70 vs 0.37 +/- 0.18 (mean +/- SD).
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Sampietro et al. (1986) conducted a case-control in Type I poorly controlled diabetes (n=23). Type I poorly controlled diabetes vs. Nondiabetics was evaluated on Nonenzymatic glycation (nanomoles of aldehyde per milligram of protein). Type I poorly controlled diabetes was associated with much greater nonenzymatic glycation of platelet membrane proteins compared to nondiabetics (1.58 vs 0.37 nmol/mg protein).
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