Two Novel Ergtoxins, Blockers of K+-channels, Purified from the Mexican Scorpion Centruroides elegans elegans

Voltage-gated potassium channels of the ether-a-go-go related gene (ERG) family are implicated in many important cellular processes. Three such genes have been cloned ( erg1 , erg2 and erg3 ) and shown to be expressed in the central nervous system (CNS) of mammalians. This communication describes th...

Full description

Saved in:
Bibliographic Details
Published in:Neurochemical research 2008-08, Vol.33 (8), p.1525-1533
Main Authors: Restano-Cassulini, Rita, Olamendi-Portugal, Timoteo, Zamudio, Fernando, Becerril, Baltazar, Possani, Lourival Domingos
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biochemistry
Biomedical and Life Sciences
Biomedicine
Cell Biology
CHO Cells
Cricetinae
Cricetulus
Ether-A-Go-Go Potassium Channels - genetics
Ether-A-Go-Go Potassium Channels - metabolism
Humans
Molecular Sequence Data
Neurochemistry
Neurology
Neurosciences
Original Paper
Patch-Clamp Techniques
Peptides - genetics
Peptides - isolation & purification
Peptides - metabolism
Potassium Channel Blockers - isolation & purification
Potassium Channel Blockers - metabolism
Rats
Scorpion Venoms - genetics
Scorpion Venoms - isolation & purification
Scorpion Venoms - metabolism
Scorpions - chemistry
Sequence Alignment
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Voltage-gated potassium channels of the ether-a-go-go related gene (ERG) family are implicated in many important cellular processes. Three such genes have been cloned ( erg1 , erg2 and erg3 ) and shown to be expressed in the central nervous system (CNS) of mammalians. This communication describes the isolation and characterization of two isoforms of scorpion toxin (CeErg4 and CeErg5, systematic nomenclature γ-KTx1.7 and γ-KTx1.8, respectively) that can discriminate the various subtypes of ERG channels of human and rat. These peptides were purified from the venom of the Mexican scorpion Centruroides elegans elegans . They contain 42 amino acid residues, tightly folded by four disulfide bridges. Both peptides block in a reversible manner human and rat ERG1 channels, but have no effect on human ERG2. They also block completely and irreversibly the rat ERG2 and the human ERG3 channels hence are excellent tools for the discrimination of the various sub-types of ion-channels studied.
ISSN:0364-3190
1573-6903
DOI:10.1007/s11064-008-9634-8