Magnani M, Rossi L, Bianchi M, Serafini G, Stocchi V
Istituto di Chimica Biologica, Università degli Studi, Urbino, Italy.
Biochem Biophys Res Commun. 1988 Aug 30;155(1):423-8. doi: 10.1016/s0006-291x(88)81103-3.
Human erythrocytes overloaded with homogeneous human hexokinase (up to 15-times the activity of normal RBC) show almost unmodified rates of glucose metabolized in the HMP, however hexokinase-loaded RBC are able to metabolize 1.5 fold more glucose than controls through the HMP when an oxidizing agent like methylene blue (5 to 100 microM) is present. Similarly, RBC loaded with inactivating anti-hexokinase IgG (12 +/- 3% residual hexokinase activity) show HMP rates unchanged under resting conditions, but only 12% of the HMP rate found in normal controls under oxidative stress. These data provide clear evidence that the HMP rate under conditions of oxidative stress is controlled by hexokinase activity and suggest that RBC from patients with hexokinase deficiency are not able to increase the HMP rate under oxidative stress like erythrocytes from individuals with G6PD deficiency.
负载均一的人己糖激酶（活性高达正常红细胞的15倍）的人红细胞在磷酸戊糖途径（HMP）中葡萄糖代谢速率几乎未改变，然而，当存在像亚甲蓝（5至100微摩尔）这样的氧化剂时，负载己糖激酶的红细胞通过HMP代谢葡萄糖的能力比对照高1.5倍。同样，负载失活的抗己糖激酶IgG（残余己糖激酶活性为12±3%）的红细胞在静息条件下HMP速率未改变，但在氧化应激下仅为正常对照中HMP速率的12%。这些数据提供了明确的证据，表明氧化应激条件下的HMP速率受己糖激酶活性控制，并表明己糖激酶缺乏患者的红细胞在氧化应激下无法像葡萄糖-6-磷酸脱氢酶（G6PD）缺乏个体的红细胞那样增加HMP速率。
