Electrophysiological characterization of a novel small peptide from the venom of Conus californicus that targets voltage-gated neuronal Ca2+ channels
| Autor: | Alexei Licea, Emilio Salceda, Rogelio O. Arellano, Enrique Soto, Rosario Vega, Omar López, Johanna Bernáldez |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Patch-Clamp Techniques
Molecular Sequence Data Mollusk Venoms Peptide Conus californicus Chemical Fractionation Biology Transfection Toxicology Xenopus laevis Calcium Channels N-Type Ganglia Spinal Conus Animals Amino Acid Sequence Conotoxin Cells Cultured Chromatography High Pressure Liquid Neurons chemistry.chemical_classification Voltage-gated ion channel Voltage-dependent calcium channel Calcium channel Conus Snail Anatomy Calcium Channel Blockers biology.organism_classification Electrophysiological Phenomena Rats chemistry Oocytes Biophysics Female Conotoxins Cysteine |
| Zdroj: | Toxicon. 57:60-67 |
| ISSN: | 0041-0101 |
| DOI: | 10.1016/j.toxicon.2010.09.015 |
| Popis: | Conus californicus belongs to a genus of marine gastropods with more than 700 extant species. C. californicus has been shown to be distantly related to all Conus species, but showing unusual biological features. We report a novel peptide isolated from C. californicus with a significant inhibitory action over neuronal voltage-gated calcium channels. The new toxin is formed by 13-amino acid residues with two disulfide bonds, whose sequence (NCPAGCRSQGCCM) is strikingly different from regular ω-conotoxins. In the HPLC purification procedure, the venom fraction eluted in the first 10-15 min produced a significant decrease (54% ± 3%) of the Ca(2+) current in Xenopus laevis oocytes transfected with purified rat-brain mRNA. A specific peptide obtained from the elution at 13 min decreased the Ca(2+) current in the adult rat dorsal-root ganglion neurons in a primary culture by 34% ± 2%. The cysteine pattern of this peptide corresponds to the framework XVI described for the M-superfamily of conopeptides and is unprecedented among Conus peptides acting on Ca(2+) channels. |
| Databáze: | OpenAIRE |
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