Transduction of the scorpion toxin maurocalcine into cells. Evidence that the toxin crosses the plasma membrane

Autor: Eric, Estève, Kamel, Mabrouk, Alain, Dupuis, Sophia, Smida-Rezgui, Xavier, Altafaj, Didier, Grunwald, Jean-Claude, Platel, Nicolas, Andreotti, Isabelle, Marty, Jean-Marc, Sabatier, Michel, Ronjat, Michel, De Waard
Rok vydání: 2005
Předmět:
Zdroj: The Journal of biological chemistry. 280(13)
ISSN: 0021-9258
Popis: Maurocalcine (MCa) is a 33 amino acid residue peptide toxin isolated from the scorpion Scorpio maurus palmatus. External application of MCa to cultured myotubes is known to produce Ca2+ release from intracellular stores. MCa binds directly to the skeletal muscle isoform of the ryanodine receptor, an intracellular channel target of the endoplasmic reticulum, and induces long-lasting channel openings in a mode of smaller conductance. Here, we investigated the way MCa proceeds to cross biological membranes in order to reach its target. A biotinylated derivative of MCa was produced (MCab) and complexed with a fluorescent indicator (streptavidine-cyanine 3) in order to follow the cell penetration of the toxin. The toxin complex efficiently penetrated in various cell types without requiring metabolic energy (low temperature) or implicating an endocytosis mechanism. MCa appeared to share the same features as the so-called Cell-Penetrating Peptides (CPP). Our results provide evidence that MCa has the ability to act as a molecular carrier and to cross cell membranes in a rapid manner (1–2 min) making this toxin the first demonstrated example of a scorpion toxin that translocates into cells.
Databáze: OpenAIRE