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
N1 - Funding Information:
Acknowledgments This work was supported by the State National High-Tech Development Program (863 Program) from the Ministry of Science and Technology of China (No. 2006AA090504 and No. 2008AA09Z401), National Natural Science Foundation of China (30871921), project of Guangdong Science-Tech Program (No. 2006A36501001), Guangdong Natural Science Foundation (8151027501000083). We thank Jingxing Ou of University of Aberdeen for his comments on this article.
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
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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 -