Posttranslational degradation of the major myelin glycoprotein by Schwann cells in vivo and in vitro.
Posttranslational degradation of the major myelin glycoprotein by Schwann cells in vivo and in vitro.
复制标题
体内和体外雪旺细胞对主要髓磷脂糖蛋白的翻译后降解。
DOI:
10.1111/j.1749-6632.1990.tb42395.x
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发表时间:
1990
影响因子:
5.2
通讯作者:
Poduslo,JF
中科院分区:
文献类型:
--
作者:
Brunden,KR;Poduslo,JF
The expression of the major glycoprotein of peripheral nerve myelin, Po, has been investigated in two in viuo experimental paradigms: after crash injury of the sciatic nerve of the adult rat and after permanent transection injury.'-3 These models are initially characterized by Wallerian degeneration, followed by the presence or absence of subsequent axonal regeneration and remyelination, respectively. It has been demonstrated that the level of newly synthesized Pol4 and its mRNA5*" is reduced after transection injury and its posttranslational oligosaccharide processing is altered when compared to crush-injured nerve..'Using the in viw permanent transection paradigm,'we have shown that some of the apparent down-regulation of PO in the transected nerve is the result of lysosomal degradation of the glycoprotein shortly after its biosynthesis. This degradation is inhibited by lysosomal perturbation or by altering the degree of oligosaccharide processing. Protein catabolism, therefore, appears to be a posttranslational mechanism for regulating the level of Po expression in the absence of myelination. The following chapter further addresses this regulation in the permanently transected nerve in vivo and compares it with the regulation of expression that occurs in vitro after culturing Schwann cells from neonatal and young endoneurial explants.