Beniac D R, Wood D D, Palaniyar N, Ottensmeyer F P, Moscarello M A, Harauz G
Department of Molecular Biology and Genetics, University of Guelph, Ontario, Canada.
Mol Cell Biol Res Commun. 1999 Apr;1(1):48-51. doi: 10.1006/mcbr.1999.0111.
Multiple sclerosis (MS) is an autoimmune disease in which the myelin sheath of the central nervous system is degraded, and the 18.5 kDa isoform of myelin basic protein (MBP) is reduced in cationicity. In a unique case of acute, fulminating MS (Marburg's variant), MBP is considerably less cationic than MBP from both normal, and chronic MS-afflicted individuals. This electron microscopical study has identified that, in vitro, the less cationic Marburg MBP isomer forms a more extended protein-lipid complex than MBP from healthy or chronic MS-afflicted individuals. This correlation implies that chemical modifications to MBP in vivo contribute directly to the structural instability of myelin, and subsequent autoantigenic presentation of this protein, observed in vivo in MS.
多发性硬化症（MS）是一种自身免疫性疾病，其中中枢神经系统的髓鞘会退化，并且髓鞘碱性蛋白（MBP）的18.5 kDa亚型的阳离子性降低。在一例独特的急性暴发性MS（马尔堡变异型）中，MBP的阳离子性明显低于正常人和慢性MS患者的MBP。这项电子显微镜研究已经确定，在体外，阳离子性较低的马尔堡MBP异构体比来自健康人或慢性MS患者的MBP形成更伸展的蛋白质-脂质复合物。这种相关性意味着，体内MBP的化学修饰直接导致髓鞘结构不稳定，以及在MS体内观察到的该蛋白质随后的自身抗原呈递。
