Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents

Lei Wang; Junliang Liu; Canhui Pi; Xiayun Zeng; Maojun Zhou; Xiaoyu Jiang; Shangwu Chen; Zhenghua Ren; Anlong Xu

doi:10.1007/s00204-009-0453-8

Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents

Lei Wang, Junliang Liu, Canhui Pi, Xiayun Zeng, Maojun Zhou, Xiaoyu Jiang, Shangwu Chen, Zhenghua Ren, Anlong Xu

Research output: Contribution to journal › Article

29 Scopus citations

Abstract

In this work, a novel M-superfamily conotoxin, designated lt3a, was purified from the crude venom of Conus litteratus. Combined with peptide sequencing, MALDI-TOF mass spectrometry and cDNA cloning techniques, the amino acid sequence of lt3a was supposed to be DγCCγ OQWCDGACDCCS, where O is hydroxyproline and γ is carboxyglutamate. The Cys framework of lt3a (-CC-C-C-CC-) is similar to that of ψ-, μ-, κM-conotoxins, which are representatives of M-conotoxins. Peptide lt3a is categorized into M1 branch based on the number of residues in the last Cys loop. Whole cell patch-clamp study on adult rat dorsal root ganglion neurons indicated that lt3a could enhance tetrodotoxin-sensitive sodium currents. This is a previously unknown function of M-superfamily conotoxins.

Original language	English (US)
Pages (from-to)	925-932
Number of pages	8
Journal	Archives of Toxicology
Volume	83
Issue number	10
DOIs	https://doi.org/10.1007/s00204-009-0453-8
State	Published - Jun 29 2009
Externally published	Yes

Keywords

Conus litteratus
M-superfamily conotoxin
Post-translational modification
Rat dorsal root ganglion neurons
Tetrodotoxin-sensitive sodium channels

ASJC Scopus subject areas

Toxicology
Health, Toxicology and Mutagenesis

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Wang, L., Liu, J., Pi, C., Zeng, X., Zhou, M., Jiang, X., Chen, S., Ren, Z., & Xu, A. (2009). Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents. Archives of Toxicology, 83(10), 925-932. https://doi.org/10.1007/s00204-009-0453-8

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abstract = "In this work, a novel M-superfamily conotoxin, designated lt3a, was purified from the crude venom of Conus litteratus. Combined with peptide sequencing, MALDI-TOF mass spectrometry and cDNA cloning techniques, the amino acid sequence of lt3a was supposed to be DγCCγ OQWCDGACDCCS, where O is hydroxyproline and γ is carboxyglutamate. The Cys framework of lt3a (-CC-C-C-CC-) is similar to that of ψ-, μ-, κM-conotoxins, which are representatives of M-conotoxins. Peptide lt3a is categorized into M1 branch based on the number of residues in the last Cys loop. Whole cell patch-clamp study on adult rat dorsal root ganglion neurons indicated that lt3a could enhance tetrodotoxin-sensitive sodium currents. This is a previously unknown function of M-superfamily conotoxins.",

keywords = "Conus litteratus, M-superfamily conotoxin, Post-translational modification, Rat dorsal root ganglion neurons, Tetrodotoxin-sensitive sodium channels",

author = "Lei Wang and Junliang Liu and Canhui Pi and Xiayun Zeng and Maojun Zhou and Xiaoyu Jiang and Shangwu Chen and Zhenghua Ren and Anlong Xu",

year = "2009",

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T1 - Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents

AU - Wang, Lei

AU - Liu, Junliang

AU - Pi, Canhui

AU - Zeng, Xiayun

AU - Zhou, Maojun

AU - Jiang, Xiaoyu

AU - Chen, Shangwu

AU - Ren, Zhenghua

AU - Xu, Anlong

PY - 2009/6/29

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N2 - In this work, a novel M-superfamily conotoxin, designated lt3a, was purified from the crude venom of Conus litteratus. Combined with peptide sequencing, MALDI-TOF mass spectrometry and cDNA cloning techniques, the amino acid sequence of lt3a was supposed to be DγCCγ OQWCDGACDCCS, where O is hydroxyproline and γ is carboxyglutamate. The Cys framework of lt3a (-CC-C-C-CC-) is similar to that of ψ-, μ-, κM-conotoxins, which are representatives of M-conotoxins. Peptide lt3a is categorized into M1 branch based on the number of residues in the last Cys loop. Whole cell patch-clamp study on adult rat dorsal root ganglion neurons indicated that lt3a could enhance tetrodotoxin-sensitive sodium currents. This is a previously unknown function of M-superfamily conotoxins.

AB - In this work, a novel M-superfamily conotoxin, designated lt3a, was purified from the crude venom of Conus litteratus. Combined with peptide sequencing, MALDI-TOF mass spectrometry and cDNA cloning techniques, the amino acid sequence of lt3a was supposed to be DγCCγ OQWCDGACDCCS, where O is hydroxyproline and γ is carboxyglutamate. The Cys framework of lt3a (-CC-C-C-CC-) is similar to that of ψ-, μ-, κM-conotoxins, which are representatives of M-conotoxins. Peptide lt3a is categorized into M1 branch based on the number of residues in the last Cys loop. Whole cell patch-clamp study on adult rat dorsal root ganglion neurons indicated that lt3a could enhance tetrodotoxin-sensitive sodium currents. This is a previously unknown function of M-superfamily conotoxins.

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KW - Post-translational modification

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KW - Tetrodotoxin-sensitive sodium channels

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