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Cell penetration properties of maurocalcine, a natural venom peptide active on the intracellular ryanodine receptor.

Publication ,  Journal Article
Boisseau, S; Mabrouk, K; Ram, N; Garmy, N; Collin, V; Tadmouri, A; Mikati, M; Sabatier, J-M; Ronjat, M; Fantini, J; De Waard, M
Published in: Biochim Biophys Acta
March 2006

Maurocalcine (MCa) is a 33-amino acid residue peptide toxin initially isolated from the scorpion Scorpio maurus maurus. Its structural and functional features make it resembling many Cell Penetrating Peptides. In particular, MCa exhibits a characteristic positively charged face that may interact with membrane lipids. External application of MCa is known to produce Ca2+-release from intracellular stores within seconds. 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. The binding sites for MCa have been mapped within the cytoplasmic domain of the ryanodine receptor. In this manuscript, we further investigated how MCa proceeds to cross biological membranes in order to reach its target. A biotinylated derivative of MCa (MCab) was chemically synthesized, coupled to a fluorescent streptavidin indicator (Cy3 or Cy5) and the cell penetration of the entire complex followed by confocal microscopy and FACS analysis. The data provide evidence that MCa allows the penetration of the macro proteic complex and therefore may be used as a vector for the delivery of proteins in the cytoplasm as well as in the nucleus. Using both FACS and confocal analysis, we show that the cell penetration of the fluorescent complex is observed at concentrations as low as 10 nM, is sensitive to membrane potential and is partly inhibited by heparin. We also show that MCa interacts with the disialoganglioside GD3, the most abundant charged lipid in natural membranes. Despite its action on ryanodine receptor, MCa showed no sign of cell toxicity on HEK293 cells suggesting that it may have a wider application range. These data indicate that MCa may cross the plasma membrane directly by cell translocation and has a promising future as a carrier of various drugs and agents of therapeutic, diagnostic and technological value.

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Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

March 2006

Volume

1758

Issue

3

Start / End Page

308 / 319

Location

Netherlands

Related Subject Headings

  • Scorpion Venoms
  • Ryanodine Receptor Calcium Release Channel
  • Protein Transport
  • Protein Conformation
  • Peptides
  • Peptide Fragments
  • Oncogene Protein pp60(v-src)
  • Molecular Sequence Data
  • Microscopy, Confocal
  • Membrane Potentials
 

Citation

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Boisseau, S., Mabrouk, K., Ram, N., Garmy, N., Collin, V., Tadmouri, A., … De Waard, M. (2006). Cell penetration properties of maurocalcine, a natural venom peptide active on the intracellular ryanodine receptor. Biochim Biophys Acta, 1758(3), 308–319. https://doi.org/10.1016/j.bbamem.2006.02.007
Boisseau, Sylvie, Kamel Mabrouk, Narendra Ram, Nicolas Garmy, Véronique Collin, Abir Tadmouri, Mohamad Mikati, et al. “Cell penetration properties of maurocalcine, a natural venom peptide active on the intracellular ryanodine receptor.Biochim Biophys Acta 1758, no. 3 (March 2006): 308–19. https://doi.org/10.1016/j.bbamem.2006.02.007.
Boisseau S, Mabrouk K, Ram N, Garmy N, Collin V, Tadmouri A, et al. Cell penetration properties of maurocalcine, a natural venom peptide active on the intracellular ryanodine receptor. Biochim Biophys Acta. 2006 Mar;1758(3):308–19.
Boisseau, Sylvie, et al. “Cell penetration properties of maurocalcine, a natural venom peptide active on the intracellular ryanodine receptor.Biochim Biophys Acta, vol. 1758, no. 3, Mar. 2006, pp. 308–19. Pubmed, doi:10.1016/j.bbamem.2006.02.007.
Boisseau S, Mabrouk K, Ram N, Garmy N, Collin V, Tadmouri A, Mikati M, Sabatier J-M, Ronjat M, Fantini J, De Waard M. Cell penetration properties of maurocalcine, a natural venom peptide active on the intracellular ryanodine receptor. Biochim Biophys Acta. 2006 Mar;1758(3):308–319.

Published In

Biochim Biophys Acta

DOI

ISSN

0006-3002

Publication Date

March 2006

Volume

1758

Issue

3

Start / End Page

308 / 319

Location

Netherlands

Related Subject Headings

  • Scorpion Venoms
  • Ryanodine Receptor Calcium Release Channel
  • Protein Transport
  • Protein Conformation
  • Peptides
  • Peptide Fragments
  • Oncogene Protein pp60(v-src)
  • Molecular Sequence Data
  • Microscopy, Confocal
  • Membrane Potentials