Harauz George, Musse Abdiwahab A
Department of Molecular and Cellular Biology, and Biophysics Interdepartmental Group, University of Guelph, 50 Stone Road East, Guelph, ON, Canada, N1G 2W1.
Neurochem Res. 2007 Feb;32(2):137-58. doi: 10.1007/s11064-006-9108-9. Epub 2006 Aug 9.
Myelin basic protein (MBP) binds to negatively charged lipids on the cytosolic surface of oligodendrocyte membranes and is responsible for adhesion of these surfaces in the multilayered myelin sheath. The pattern of extensive post-translational modifications of MBP is dynamic during normal central nervous system (CNS) development and during myelin degeneration in multiple sclerosis (MS), affecting its interactions with the myelin membranes and with other molecules. In particular, the degree of deimination (or citrullination) of MBP is correlated with the severity of MS, and may represent a primary defect that precedes neurodegeneration due to autoimmune attack. That the degree of MBP deimination is also high in early CNS development indicates that this modification plays major physiological roles in myelin assembly. In this review, we describe the structural and functional consequences of MBP deimination in healthy and diseased myelin.
髓鞘碱性蛋白（MBP）与少突胶质细胞膜胞质表面带负电荷的脂质结合，负责多层髓鞘中这些表面的黏附。MBP广泛的翻译后修饰模式在正常中枢神经系统（CNS）发育过程以及多发性硬化症（MS）的髓鞘变性过程中是动态变化的，影响其与髓鞘膜及其他分子的相互作用。特别是，MBP的脱氨（或瓜氨酸化）程度与MS的严重程度相关，可能代表自身免疫攻击导致神经退行性变之前的原发性缺陷。MBP脱氨程度在中枢神经系统早期发育中也很高，这表明这种修饰在髓鞘组装中起主要生理作用。在本综述中，我们描述了健康和患病髓鞘中MBP脱氨的结构和功能后果。
