Roussel G, Neskovic N M, Trifilieff E, Artault J C, Nussbaum J L
J Neurocytol. 1987 Apr;16(2):195-204. doi: 10.1007/BF01795303.
Immunocytochemical investigations were performed on Jimpy and control mouse brains using three specific anti-myelin proteolipids antisera: immunoaffinity purified multivalent anti-(PLP + DM-20) proteolipid antibodies, anti-C-terminal hexapeptide 271-276 and anti-tridecapeptide 117-129 antisera. The results show that oligodendrocytes and myelin sheaths in normal mouse brain are labelled to the same extent by the three specific antisera; in contrast, in Jimpy brain these cellular structures are only stained by the multivalent antibodies and the site-specific, anti-tridecapeptide antiserum. The absence of labelling with C-terminal hexapeptide antiserum in mutant brain is interpreted as the result of either a large deletion or a point mutation producing a frameshift in the C-terminal part of the sequences of the proteolipids PLP and DM-20. Furthermore, we show that this mutation prevents the normal transport of proteolipid molecules through the Golgi apparatus. The existence of a minor, extra-Golgi apparatus metabolic route for proteolipids to myelin structures is also discussed.
使用三种特异性抗髓磷脂蛋白脂质抗血清对Jimpy小鼠和对照小鼠的大脑进行了免疫细胞化学研究：免疫亲和纯化的多价抗（PLP + DM - 20）蛋白脂质抗体、抗C末端六肽271 - 276和抗十三肽117 - 129抗血清。结果表明，正常小鼠大脑中的少突胶质细胞和髓鞘被这三种特异性抗血清标记的程度相同；相比之下，在Jimpy小鼠大脑中，这些细胞结构仅被多价抗体和位点特异性抗十三肽抗血清染色。突变体大脑中C末端六肽抗血清未出现标记，这被解释为蛋白脂质PLP和DM - 20序列C末端部分发生大的缺失或点突变导致移码的结果。此外，我们表明这种突变阻止了蛋白脂质分子通过高尔基体的正常转运。还讨论了存在一条从高尔基体以外的次要代谢途径将蛋白脂质转运到髓鞘结构的情况。
