Kawamura N, Ookawara T, Suzuki K, Konishi K, Mino M, Taniguchi N
Department of Biochemistry, Osaka University Medical School, Japan.
J Clin Endocrinol Metab. 1992 Jun;74(6):1352-4. doi: 10.1210/jcem.74.6.1592880.
Our previous study indicated that erythrocyte Cu,Zn-superoxide dismutase (Cu,Zn-SOD) undergoes glycation and inactivation in vivo (1) and in vitro (2). The aim of the present study was to assess glycated Cu,Zn-SOD in patients with insulin-dependent diabetes mellitus. Glycated Cu,Zn-SOD, which binds to a boronic acid affinity column, was measured by the enzyme-linked immunosorbent assay. The percentage of the glycated form in 25 insulin-dependent diabetic children was 40.2 +/- 8.2%; this was significantly higher than that in the normal controls (P less than 0.01). The specific activity of the glycated form in the diabetic children was 163,000 +/- 33,000 IU/mg Cu,Zn-SOD protein, significantly lower than that in controls (P less than 0.01). These data indicate that glycated and less active Cu,Zn-SOD is increased in erythrocytes of patients with insulin-dependent diabetes mellitus.
我们之前的研究表明，红细胞铜锌超氧化物歧化酶（Cu,Zn-SOD）在体内（1）和体外（2）均会发生糖基化并失活。本研究的目的是评估胰岛素依赖型糖尿病患者体内糖基化的Cu,Zn-SOD。通过酶联免疫吸附测定法测量结合到硼酸亲和柱上的糖基化Cu,Zn-SOD。25名胰岛素依赖型糖尿病儿童中糖基化形式的百分比为40.2±8.2%；这显著高于正常对照组（P<0.01）。糖尿病儿童中糖基化形式的比活性为163,000±33,000 IU/mg Cu,Zn-SOD蛋白，显著低于对照组（P<0.01）。这些数据表明，胰岛素依赖型糖尿病患者红细胞中糖基化且活性较低的Cu,Zn-SOD增加。
