ArticleInternational journal of biological sciences2012
Glycosylation of the sodium channel β4 subunit is developmentally regulated and involves in neuritic degeneration.
Article in International journal of biological sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- ERVW-1 Activates ATF6-Mediated Unfolded Protein Response by Decreasing GANAB in Recent-Onset Schizophrenia.Viruses · 2023Article
- Glycans and Carbohydrate-Binding/Transforming Proteins in Axon Physiology.Advances in neurobiology · 2023Article
- Post-translational Modifications in Parkinson's Disease.Advances in experimental medicine and biology · 2022Article
- Glycosylation of β1 subunit plays a pivotal role in the toxin sensitivity and activation of BK channels.The journal of venomous animals and toxins including tropical diseases · 2021Article
- Emerging roles for multifunctional ion channel auxiliary subunits in cancer.Cell calcium · 2019Review
- Voltage-gated sodium channel β subunits: The power outside the pore in brain development and disease.Neuropharmacology · 2018Review
- Voltage-Gated Sodium Channel β Subunits and Their Related Diseases.Handbook of experimental pharmacology · 2018Review
- The glycosylation of the extracellular loop of β2 subunits diversifies functional phenotypes of BK Channels.Channels (Austin, Tex.) · 2017Article
- Differential effects of N-linked glycosylation of Vstm5 at multiple sites on surface expression and filopodia formation.PloS one · 2017Article
- Glycosylation and other PTMs alterations in neurodegenerative diseases: Current status and future role in neurotrauma.Electrophoresis · 2016Review
- Sodium channel β subunits: emerging targets in channelopathies.Annual review of physiology · 2015Review
- Assembly of AMPA receptors: mechanisms and regulation.The Journal of physiology · 2015Review
- Crystallographic insights into sodium-channel modulation by the β4 subunit.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aberrant protein glycosylation plays major roles in neurodegenerative diseases, including Parkinson's disease (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 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 β4 was developmentally regulated and was altered in disease state. Neurite outgrowth assay demonstrated that overexpression of deglycosylated mutant β4-MUT accelerated neurite extension and increased the number of filopodia-like protrusions, when compared with β4-WT and the vector. These results suggest that extensive glycosylation of β4 subunit play roles in morphological changes, and the altered glycosylation may be involved in the pathogenesis of PD.
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