Ideguchi H, Nishimura J, Nawata H, Hamasaki N
Third Department of Internal Medicine, Faculty of Medicine, Kyushu University, Japan.
Br J Haematol. 1990 Mar;74(3):347-53. doi: 10.1111/j.1365-2141.1990.tb02594.x.
We report two patients with hereditary spherocytosis associated with band 4.2 protein deficiency from a Japanese family. The defect of band 4.2 protein was confirmed by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) not only in freshly prepared white ghosts but also in washed whole erythrocytes. The finding was quite reproducible and was also recognized postsplenectomy. The interaction of ankyrin with band 3 in the patients' ghosts was stable both at low ionic strength and at acidic pH. Our results suggested that band 4.2 protein might not be essential for the structural stability of band 3-ankyrin interaction. On the other hand, membrane protein phosphorylation studies revealed an increased phosphorylation of spectrin/ankyrin, band 3 and band 4.1 in the patients' erythrocytes as compared with normal cells. The finding might be related to a dysregulation of protein phosphorylation which could result in membrane instability in affected cells. Band 4.2 deficiency is an inherited disorder in association with hereditary haemolytic anaemias and seems to be relatively prevalent in the Japanese population.
我们报告了来自一个日本家庭的两名遗传性球形红细胞增多症患者，他们伴有4.2带蛋白缺乏。通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）证实，不仅在新鲜制备的白色血影中，而且在洗涤后的全红细胞中均存在4.2带蛋白缺陷。这一发现具有很高的可重复性，并且在脾切除术后也能观察到。在低离子强度和酸性pH条件下，患者血影中锚蛋白与3带蛋白的相互作用均很稳定。我们的结果表明，4.2带蛋白对于3带蛋白-锚蛋白相互作用的结构稳定性可能并非必不可少。另一方面，膜蛋白磷酸化研究显示，与正常细胞相比，患者红细胞中的血影蛋白/锚蛋白、3带蛋白和4.1带蛋白的磷酸化增加。这一发现可能与蛋白磷酸化失调有关，而蛋白磷酸化失调可能导致受影响细胞的膜不稳定。4.2带蛋白缺乏是一种与遗传性溶血性贫血相关的遗传性疾病，在日本人群中似乎相对普遍。
