Sato S, Quarles R H, Brady R O, Tourtellotte W W
Ann Neurol. 1984 Mar;15(3):264-7. doi: 10.1002/ana.410150310.
Incubation of human myelin at neutral pH resulted in the proteolytic conversion of the myelin-associated glycoprotein to a lower molecular weight derivative (dMAG) and the degradation of basic protein. The formation of dMAG occurred much more rapidly than the degradation of basic protein. The formation of dMAG and the degradation of basic protein both occurred significantly more rapidly in myelin preparations purified from brains of patients with multiple sclerosis than in preparations from control brain. The results suggest that this neutral protease associated with myelin may function in the pathogenesis of demyelinating diseases such as multiple sclerosis.
在中性pH条件下孵育人髓磷脂,导致髓磷脂相关糖蛋白发生蛋白水解转化为较低分子量的衍生物(dMAG),同时碱性蛋白降解。dMAG的形成比碱性蛋白的降解快得多。与从对照脑制备的髓磷脂相比,从多发性硬化症患者脑纯化的髓磷脂制剂中,dMAG的形成和碱性蛋白的降解都明显更快。结果表明,这种与髓磷脂相关的中性蛋白酶可能在多发性硬化症等脱髓鞘疾病的发病机制中起作用。