Mining the Virgin Land of Neurotoxicology: A Novel Paradigm of Neurotoxic Peptides Action on Glycosylated Voltage-Gated Sodium Channels
Voltage-gated sodium channels (VGSCs) are important membrane protein carrying on the molecular basis for action potentials (AP) in neuronal firings. Even though the structure-function studies were the most pursued spots, the posttranslation modification processes, such as glycosylation, phosphorylat...
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| Format: | Article |
| Language: | English |
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Wiley
2012-01-01
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| Series: | Journal of Toxicology |
| Online Access: | http://dx.doi.org/10.1155/2012/843787 |
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| author | Zhirui Liu Jie Tao Pin Ye Yonghua Ji |
| author_facet | Zhirui Liu Jie Tao Pin Ye Yonghua Ji |
| author_sort | Zhirui Liu |
| collection | DOAJ |
| description | Voltage-gated sodium channels (VGSCs) are important membrane protein carrying on the molecular basis for action potentials (AP) in neuronal firings. Even though the structure-function studies were the most pursued spots, the posttranslation modification processes, such as glycosylation, phosphorylation, and alternative splicing associating with channel functions captured less eyesights. The accumulative research suggested an interaction between the sialic acids chains and ion-permeable pores, giving rise to subtle but significant impacts on channel gating. Sodium channel-specific neurotoxic toxins, a family of long-chain polypeptides originated from venomous animals, are found to potentially share the binding sites adjacent to glycosylated region on VGSCs. Thus, an interaction between toxin and glycosylated VGSC might hopefully join the campaign to approach the role of glycosylation in modulating VGSCs-involved neuronal network activity. This paper will cover the state-of-the-art advances of researches on glycosylation-mediated VGSCs function and the possible underlying mechanisms of interactions between toxin and glycosylated VGSCs, which may therefore, fulfill the knowledge in identifying the pharmacological targets and therapeutic values of VGSCs. |
| format | Article |
| id | doaj-art-3b266245c000409bbba8e6e1f95f145c |
| institution | Kabale University |
| issn | 1687-8191 1687-8205 |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Toxicology |
| spelling | doaj-art-3b266245c000409bbba8e6e1f95f145c2025-02-03T01:12:13ZengWileyJournal of Toxicology1687-81911687-82052012-01-01201210.1155/2012/843787843787Mining the Virgin Land of Neurotoxicology: A Novel Paradigm of Neurotoxic Peptides Action on Glycosylated Voltage-Gated Sodium ChannelsZhirui Liu0Jie Tao1Pin Ye2Yonghua Ji3Laboratory of Neuropharmacology and Neurotoxicology, Shanghai University, Nanchen Road 333, Shanghai 200444, ChinaLaboratory of Neuropharmacology and Neurotoxicology, Shanghai University, Nanchen Road 333, Shanghai 200444, ChinaLaboratory of Neuropharmacology and Neurotoxicology, Shanghai University, Nanchen Road 333, Shanghai 200444, ChinaLaboratory of Neuropharmacology and Neurotoxicology, Shanghai University, Nanchen Road 333, Shanghai 200444, ChinaVoltage-gated sodium channels (VGSCs) are important membrane protein carrying on the molecular basis for action potentials (AP) in neuronal firings. Even though the structure-function studies were the most pursued spots, the posttranslation modification processes, such as glycosylation, phosphorylation, and alternative splicing associating with channel functions captured less eyesights. The accumulative research suggested an interaction between the sialic acids chains and ion-permeable pores, giving rise to subtle but significant impacts on channel gating. Sodium channel-specific neurotoxic toxins, a family of long-chain polypeptides originated from venomous animals, are found to potentially share the binding sites adjacent to glycosylated region on VGSCs. Thus, an interaction between toxin and glycosylated VGSC might hopefully join the campaign to approach the role of glycosylation in modulating VGSCs-involved neuronal network activity. This paper will cover the state-of-the-art advances of researches on glycosylation-mediated VGSCs function and the possible underlying mechanisms of interactions between toxin and glycosylated VGSCs, which may therefore, fulfill the knowledge in identifying the pharmacological targets and therapeutic values of VGSCs.http://dx.doi.org/10.1155/2012/843787 |
| spellingShingle | Zhirui Liu Jie Tao Pin Ye Yonghua Ji Mining the Virgin Land of Neurotoxicology: A Novel Paradigm of Neurotoxic Peptides Action on Glycosylated Voltage-Gated Sodium Channels Journal of Toxicology |
| title | Mining the Virgin Land of Neurotoxicology: A Novel Paradigm of Neurotoxic Peptides Action on Glycosylated Voltage-Gated Sodium Channels |
| title_full | Mining the Virgin Land of Neurotoxicology: A Novel Paradigm of Neurotoxic Peptides Action on Glycosylated Voltage-Gated Sodium Channels |
| title_fullStr | Mining the Virgin Land of Neurotoxicology: A Novel Paradigm of Neurotoxic Peptides Action on Glycosylated Voltage-Gated Sodium Channels |
| title_full_unstemmed | Mining the Virgin Land of Neurotoxicology: A Novel Paradigm of Neurotoxic Peptides Action on Glycosylated Voltage-Gated Sodium Channels |
| title_short | Mining the Virgin Land of Neurotoxicology: A Novel Paradigm of Neurotoxic Peptides Action on Glycosylated Voltage-Gated Sodium Channels |
| title_sort | mining the virgin land of neurotoxicology a novel paradigm of neurotoxic peptides action on glycosylated voltage gated sodium channels |
| url | http://dx.doi.org/10.1155/2012/843787 |
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