Effect of Vitamin C on Glycosylation of Proteins

Effect of Vitamin C on Glycosylation of Proteins
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DOI：
10.2337/diab.41.2.167
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发表时间：
1992-02
期刊：
Diabetes
影响因子：
7.7
通讯作者：
S. Davie;B. Gould;J. Yudkin
S. Davie;B. Gould;J. Yudkin
中科院分区：
医学1区
文献类型：
--
作者：
S. Davie;B. Gould;J. Yudkin

文献摘要

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12名非糖尿病受试者每天摄入1g维生素C，连续3个月。在研究开始时和每个月结束时采集空腹血样，用于测量血浆和红细胞内血糖、维生素C、糖化血红蛋白(亲和层析和电泳法)和糖化白蛋白(亲和层析法)。虽然空腹血糖无明显变化，但糖化血红蛋白(亲和层析)下降了18%，从开始时的6.18±0.48%(平均值±SD)下降到3个月后的5.05±0.50%(P&lt；0.0001)，而电泳法测得的HbA1在此期间增加了16%，从6.17±0.61%增加到7.16±0.59%(P&lt；0.0001)。糖化白蛋白下降33%，从1.56±0.24降至1.04±1.01%(P&lt；0.0001)。用电泳法和亲和层析法测定糖化血红蛋白之间的差异是由于两种技术的方法不同，亲和层析法测定的是“真正的”糖化血红蛋白。糖化白蛋白下降较大可能是由于维生素C在血浆和红细胞内的分布不同，补充1mo后维生素C水平分别为109±19和59±9μM(P&lt；0.001)。这表明口服维生素C可能通过竞争性机制抑制体内蛋白质的糖基化。
Twelve nondiabetic subjects consumed 1 g/day vitamin C for 3 mo. A fasting blood sample was taken at the start of the study and at the end of each month for the measurement of plasma and intraerythrocyte glucose, vitamin C, glycosylated hemoglobin (affinity chromatography and electrophoresis), and glycosylated albumin (affinity chromatography). Although there were no significant changes in fasting glycemia, glycosylated hemoglobin (affinity chromatography) decreased 18%, from 6.18 ± 0.48% (mean ± SD) at the start to 5.05 ± 0.50% (P < 0.0001) after 3 mo, whereas, HbA1 measured by electrophoresis increased 16%, from 6.17 ± 0.61 to 7.16 ± 0.59% (P < 0.0001) in this period. Glycosylated albumin decreased 33%, from 1.56 ± 0.24 to 1.04 ± 1.01% (P < 0.0001) after 3 mo. This discrepancy between glycosylated hemoglobin measured by electrophoresis and affinity chromatography was due to methodological differences between the two techniques, with affinity chromatography measuring “true” glycosylated hemoglobin. The greater decrease found with glycosylated albumin was probably due to the different distribution of vitamin C between plasma and within the erythrocyte, levels after 1 mo of supplementation being 109 ± 19 and 59 ± 9 μM, respectively (P < 0.001). This indicates that administration of oral vitamin C may inhibit the glycosylation of proteins in vivo by a competitive mechanism.