Pareek S, Suter U, Snipes G J, Welcher A A, Shooter E M, Murphy R A
Montreal Neurological Institute, McGill University, Quebec, Canada.
J Biol Chem. 1993 May 15;268(14):10372-9.
Peripheral myelin protein, 22 kDa (PMP22), is a myelin molecule associated with Schwann cells in peripheral nerves (Snipes, G. J., Suter, U., Welcher, A. A., and Shooter, E. M. (1992) J. Cell Biol. 117, 225-238). Mutations affecting the PMP22 gene have been implicated in the trembler mutation in mice (Suter, U., Welcher, A. A., Ozcelik, T., Snipes, G. J., Kosaras, B., Francke, U., Billings-Gagliardi, S., Sidman, R. L., and Shooter, E. M. (1992) Nature 356, 241-244; Suter, U., Moskow, J. J., Welcher, A. A., Snipes, G. J., Kosaras, B., Sidman, R. L., Buchberg, A. M., and Shooter, E. M. (1992) Proc. Natl. Acad. Sci. U. S. A. 89, 4382-4386) and Charcot-Marie-Tooth Disease in humans (Patel, P. I., Roa, B. B., Welcher, A. A., Schoener-Scott, R., Trask, B. J., Pentao, L., Snipes, G. J., Garcia, C. A., Francke, U., Shooter, E. M., Lupski, J. R., and Suter, U. (1992) Nature genet. 1, 159-165). In this report, we have studied PMP22 production in cultured rat Schwann cells. Schwann cells contain a 1.8-kilobase mRNA transcript coding for PMP22, and its production is up-regulated in vitro by forskolin. Metabolic labeling combined with immunoprecipitation methods using antibodies raised against synthetic peptides of PMP22 reveal that Schwann cells generate the protein from an 18-kDa precursor form which is post-translationally modified by N-linked glycosylation. A second molecule (molecular mass, 48 kDa) that reacted with PMP22 antibodies was also detected in Schwann cells but is not related chemically to PMP22 as determined by pulse-chase labeling. Metabolic labeling of rat sciatic nerve and Western blot analyses of purified rat sciatic nerve myelin reveal that deglycosylation of PMP22 gives rise to an 18-kDa protein similar in size to that in Schwann cells. These results indicate that cultured Schwann cells may provide a good model in which to investigate the production and function of PMP22 and to establish the cellular basis for the protein's involvement in inherited peripheral neuropathies.
外周髓鞘蛋白,22千道尔顿(PMP22),是一种与外周神经中的施万细胞相关的髓鞘分子(斯奈普斯,G. J.,苏特,U.,韦尔彻,A. A.,和舒特,E. M.(1992年)《细胞生物学杂志》117卷,225 - 238页)。影响PMP22基因的突变与小鼠的震颤突变(苏特,U.,韦尔彻,A. A.,奥泽利克,T.,斯奈普斯,G. J.,科萨拉斯,B.,弗兰克,U.,比林斯 - 加利亚迪,S.,西德曼,R. L.,和舒特,E. M.(1992年)《自然》356卷,241 - 244页;苏特,U.,莫斯科,J. J.,韦尔彻,A. A.,斯奈普斯,G. J.,科萨拉斯,B.,西德曼,R. L.,布赫伯格,A. M.,和舒特,E. M.(1992年)《美国国家科学院院刊》89卷,4382 - 4386页)以及人类的夏科 - 马里 - 图斯病(帕特尔,P. I.,罗阿,B. B.,韦尔彻,A. A.,舍纳 - 斯科特,R.,特拉斯克,B. J.,彭涛,L.,斯奈普斯,G. J.,加西亚,C. A.,弗兰克,U.,舒特,E. M.,卢普斯基,J. R.,和苏特,U.(1992年)《自然遗传学》1卷,159 - 165页)有关。在本报告中,我们研究了培养大鼠施万细胞中PMP22的产生。施万细胞含有一个编码PMP22的1.8千碱基mRNA转录本,其产生在体外被福斯可林上调。代谢标记结合用针对PMP22合成肽产生的抗体进行免疫沉淀方法表明,施万细胞从一种18千道尔顿的前体形式产生该蛋白质,该前体形式通过N - 连接糖基化进行翻译后修饰。在施万细胞中还检测到了第二个与PMP22抗体反应的分子(分子量48千道尔顿),但通过脉冲追踪标记确定其在化学上与PMP22无关。大鼠坐骨神经的代谢标记以及纯化大鼠坐骨神经髓鞘的蛋白质印迹分析表明,PMP22的去糖基化产生了一种大小与施万细胞中相似的18千道尔顿蛋白质。这些结果表明,培养的施万细胞可能提供一个良好的模型,用于研究PMP22的产生和功能,并为该蛋白质参与遗传性周围神经病建立细胞基础。