McLaughlin M, Hunter D J B, Thomson C E, Yool D, Kirkham D, Freer A A, Griffiths I R
Applied Neurobiology Group, Institute of Comparative Medicine, University of Glasgow Veterinary School, Glasgow, Scotland.
Glia. 2002 Jul;39(1):31-6. doi: 10.1002/glia.10091.
PLP and its smaller DM20 isoform constitute the major proteins of CNS myelin. Previous studies indicated a role for the proteins in maintaining the intraperiod line of the myelin sheath and the integrity of axons and suggested that both isoforms were necessary to provide these functions. The present study shows that each isoform is capable individually of inserting into compact myelin. Employing chromatographic extraction procedures designed to maintain the natural conformation of the proteins we found that most PLP and DM20 remained associated. Using an antibody specific to the PLP isoform, we were able to co-immunoprecipitate DM20 from the major fraction of the extracted equine myelin and from mouse native whole myelin. We suggest that PLP and DM20 may form a hetero-oligomeric complex within the myelin sheath, probably in association with specific lipids and that this arrangement is essential for the normal structure of myelin and axons.
蛋白脂蛋白(PLP)及其较小的DM20异构体构成中枢神经系统髓鞘的主要蛋白质。先前的研究表明这些蛋白质在维持髓鞘内节线以及轴突完整性方面发挥作用,并提示两种异构体对于发挥这些功能都是必需的。本研究表明,每种异构体都能够单独插入紧密髓鞘中。采用旨在维持蛋白质天然构象的色谱提取方法,我们发现大多数PLP和DM20仍然相互关联。使用针对PLP异构体的特异性抗体,我们能够从提取的马髓鞘主要部分以及小鼠天然全髓鞘中共免疫沉淀DM20。我们认为,PLP和DM20可能在髓鞘内形成异源寡聚体复合物,可能与特定脂质相关联,并且这种排列对于髓鞘和轴突的正常结构至关重要。