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| The Research of the Glycosylation of Sodium Channel β4 Subunit |
| ZHOU Ting-ting1,2, PAN Chuan-yong2, ZHANG Jian-peng2, JIN Hui-ying1 |
1. East-China Institute for Medical Biotechniques, Nanjing 210002, China;
2. Department of Biochemistry & Molecular Biology, Second Military Medical University, Shanghai 200433, China |
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Abstract Aberrant protein glycosylation plays major roles in neurodegenerative disease, including PD. Glycoproteomics showed that the glycosylation of sodium channel β4 was significantly increased in human brain tissue. β4-specific antibodies reacted in immunoblot assays with ~38 kDa band from the membrane fractions isolated from neonatal PD transgenic mice but not expressed in the neonatal wild-type mice. The molecular weight of ~38 kDa immunoreactive protein is in close agreement with previously reported, suggesting heavy glycosylation of this protein in adult wild-type and neonatal PD transgenic brain tissues. Enzymatic deglycosylation of the membrane preparations converted the 38 kDa band into a faster migrating protein, which was consistent with heavy glycosylation of this protein. The glycosylated state of β4 was developmentally regulated and was altered in disease state. We also expressed β4-wild type and deglycosylated mutant β4-MUT plasmids in HEK-293 and Neuro2A cells. These results lay a foundation of studying β4 subunit in the pathogenesis of PD. Further studies will focus on the effects of the oligosaccharides on the sodium channel activities and neuritic degeneration.
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Received: 26 June 2013
Published: 25 July 2014
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