期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL SCIENCES
卷 8, 期 5, 页码 630-639出版社
IVYSPRING INT PUBL
DOI: 10.7150/ijbs.3684
关键词
Voltage-gated sodium channel beta 4 subunit; Glycosylation; Filopodia-like protrusion; Neurite outgrowth; Parkinson's disease
资金
- Shanghai Natural Science Foundation [09ZR1439600]
Aberrant protein glycosylation plays major roles in neurodegenerative diseases, including Parkinson's disease (PD). Glycoproteomics showed that the glycosylation of sodium channel beta 4 was significantly increased in human brain tissue. beta 4-specific antibodies reacted in immunoblot assays with the 35- and 38-kDa bands from the membrane fractions isolated from neonatal PD transgenic mice but only with the 35-kDa band of the neonatal wild-type mice. The size of the 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. However, the neonatal wild-type mice membrane fractions only contained the 35-kDa immunoreactive protein, and the additional 38-kDa band was not shown until postnatal day 7. Enzymatic deglycosylation of the membrane preparations only converted the 38-kDa band into a faster migrating protein, which was consistent with heavy glycosylation of this protein. The glycosylated state of beta 4 was developmentally regulated and was altered in disease state. Neurite outgrowth assay demonstrated that overexpression of deglycosylated mutant beta 4-MUT accelerated neurite extension and increased the number of filopodia-like protrusions, when compared with beta 4-WT and the vector. These results suggest that extensive glycosylation of beta 4 subunit play roles in morphological changes, and the altered glycosylation may be involved in the pathogenesis of PD.
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