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 | |
| State | Published - 2009 |
| Externally published | Yes |
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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
Cite this
Identification of a novel M-superfamily conotoxin with the ability to enhance tetrodotoxin sensitive sodium currents. / Wang, Lei; Liu, Junliang; Pi, Canhui; Zeng, Xiayun; Zhou, Maojun; Jiang, Xiaoyu; Chen, Shangwu; Ren, Zhenghua; Xu, Anlong.
In: Archives of Toxicology, Vol. 83, No. 10, 2009, p. 925-932.Research output: Contribution to journal › Article
}
TY - JOUR
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
Y1 - 2009
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.
KW - Conus litteratus
KW - M-superfamily conotoxin
KW - Post-translational modification
KW - Rat dorsal root ganglion neurons
KW - Tetrodotoxin-sensitive sodium channels
UR - http://www.scopus.com/inward/record.url?scp=70349623944&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=70349623944&partnerID=8YFLogxK
U2 - 10.1007/s00204-009-0453-8
DO - 10.1007/s00204-009-0453-8
M3 - Article
C2 - 19562324
AN - SCOPUS:70349623944
VL - 83
SP - 925
EP - 932
JO - Archiv fur Toxikologie
JF - Archiv fur Toxikologie
SN - 0003-9446
IS - 10
ER -