Bosman G J, Engbersen A, Vollaard C H, Bartholomeus I G, Pistorius A M, Renkawek K, De Grip W J
Department of Biochemistry, Faculty of Medicine, University of Nijmegen, The Netherlands.
Cell Mol Biol (Noisy-le-grand). 1996 Nov;42(7):905-18.
Fourier-transform infrared spectroscopy was applied to examine the nature and extent of changes in membrane composition and structure during the aging process of the human erythrocyte. Analysis of the Amide I region (1700-1600 cm-1) indicates an aging-related decrease in alpha-helical structure with a concomitant increase in beta-structure. These changes can be explained by structural changes in the erythrocyte anion exchanger (band 3 or AE1) molecules, that may be caused by fragmentation, but not by aggregation. Immunohistochemical analysis of human brain tissue shows an increase in neuronal AE protein expression with age and suggests an additional increase in Alzheimer's disease. Biochemical analyses indicate that the latter may be caused by conformational changes in the AE membrane domain that are similar to those observed in AE1 during erythrocyte aging. AE proteins provide a binding site for the cytoskeleton in neurons, and AE-catalyzed chloride/bicarbonate exchange plays a major role in maintenance of neuronal pH. Thus, changes in AE structure are likely to contribute to loss of neuron homeostasis during aging and in neurodegenerative diseases.
傅里叶变换红外光谱法被用于检测人类红细胞衰老过程中膜组成和结构变化的性质及程度。对酰胺I区域（1700 - 1600厘米-1）的分析表明，随着衰老，α-螺旋结构减少，同时β-结构增加。这些变化可以用红细胞阴离子交换蛋白（带3或AE1）分子的结构变化来解释，这种变化可能是由片段化而非聚集引起的。对人类脑组织的免疫组织化学分析显示，随着年龄增长，神经元AE蛋白表达增加，且在阿尔茨海默病中表达进一步增加。生化分析表明，后者可能是由AE膜结构域的构象变化引起的，这种变化与红细胞衰老过程中AE1所观察到的变化相似。AE蛋白为神经元中的细胞骨架提供了一个结合位点，并且AE催化的氯离子/碳酸氢根离子交换在维持神经元pH值中起主要作用。因此，AE结构的变化可能导致衰老过程和神经退行性疾病中神经元内环境稳态的丧失。
