PMID: 8470132Mar 1, 1993Paper

Binding of myotoxin a to cultured muscle cells

Toxicon : Official Journal of the International Society on Toxinology
B BakerJ L Middlebrook

Abstract

The binding of radiolabeled myotoxin a to various cultured cell lines was evaluated. One rat skeletal muscle-derived cell line, L8, bound substantially more myotoxin a than did all all other cell lines examined. Several biophysical parameters of myotoxin a-L8 binding were determined. Binding was saturable with a moderate binding affinity. Scatchard analysis and Hill plots indicated a single class of binding sites. The binding was reversible, as demonstrated by chase experiments. Radiolabeled myotoxin a bound to the cell surface at a site inaccessible to the general protease, pronase. Specificity and biological relevance of the binding was suggested by competition with unlabeled toxin and various peptides derived from the toxin. Biologically active peptides, corresponding to the N- and C-terminal sequence of myotoxin a, competed with radiolabeled toxin for L8 binding. It was concluded that the L8 system is a suitable cell model to study myotoxin a mechanism of action.

References

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Citations

Mar 1, 1994·Toxicon : Official Journal of the International Society on Toxinology·M L YudkowskyJ E Fletcher
Nov 1, 1994·Toxicon : Official Journal of the International Society on Toxinology·B LomonteL A Hanson
Apr 1, 1996·Toxicon : Official Journal of the International Society on Toxinology·M P O'KeefeR A Nieman
Mar 13, 2002·Journal of Molecular Graphics & Modelling·A M SiqueiraB Maigret
Mar 9, 1994·Annals of the New York Academy of Sciences·A L BieberP A d'Avis
Aug 22, 2006·Toxicon : Official Journal of the International Society on Toxinology·M Boni-MitakeJ R Rogero
Aug 25, 2016·Cellular and Molecular Life Sciences : CMLS·Irina KerkisPaulo L de Sá Junior
Oct 31, 1998·Canadian Journal of Physiology and Pharmacology·C KatagiriY Ohizumi

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