Vasseur C, Leclerc L, Hilly M, Bursaux E
INSERM U.299, Hôpital du Kremlin-Bicêtre, France.
Nouv Rev Fr Hematol (1978). 1992;34(2):155-61.
Several membrane abnormalities have been described in red cells from patients with sickle cell disease, responsible for chronic hemolytic anemia. We describe here a 35-50% inhibition of the binding of glyceraldehyde-3-phosphate dehydrogenase (G3PDH) to the membrane of sickle red cells. Varying the phosphorylation state of the membrane proteins did not change their affinity for the enzyme. Protein band 3 and the cytoplasmic domain of this protein isolated from sickle red cells showed normal interaction with the enzyme. The inhibition observed with intact membranes is not due to short term oxidation of membrane proteins, as various procedures inducing acute oxidative stress in normal membranes did not reproduce the inhibition of G3PDH binding. We conclude that the alteration of the binding of G3PDH to the membrane of sickle erythrocytes is probably related to long term processes involving cycles of HbS polymer formation.
镰状细胞病患者的红细胞中已发现几种膜异常，这些异常是慢性溶血性贫血的病因。我们在此描述了甘油醛-3-磷酸脱氢酶（G3PDH）与镰状红细胞膜结合受到35%-50%的抑制。改变膜蛋白的磷酸化状态并不会改变其对该酶的亲和力。从镰状红细胞中分离出的带3蛋白及其胞质结构域与该酶表现出正常的相互作用。完整膜所观察到的抑制作用并非由于膜蛋白的短期氧化，因为在正常膜中诱导急性氧化应激的各种方法并未重现对G3PDH结合的抑制。我们得出结论，G3PDH与镰状红细胞膜结合的改变可能与涉及血红蛋白S（HbS）聚合物形成循环的长期过程有关。
