Destabilization of Membranes Containing Cardiolipin or Its Precursors by Peptides Derived from Mitogaligin, a Cell Death Protein

Abstract : Galig, a gene embedded within the galectin-3 gene, induces cell death when transfected in human cells. This death is associated with cell shrinkage, nuclei condensation, and aggregation of mitochondria. Galig contains two different overlapping open reading frames encoding two unrelated proteins. Previous observations have shown that one of these proteins, named mitogaligin, binds to mitochondria and promotes the release of cytochrome c. However, the mechanism of action of this cytotoxic protein remains still obscure. The present study provides evidence that synthetic peptides enclosing the mitochondrial localization signal of mitogaligin bind to anionic biological membranes leading to membrane destabilization, aggregation, and content leakage of mitochondria or liposomes. This binding to anionic phospholipids is the most efficient when cardiolipin, a specific phospholipid of mitochondria, is inserted in the membranes. Thus, cardiolipin may constitute a target of choice for mitogaligin sorting and membrane destabilization activity.
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https://hal.archives-ouvertes.fr/hal-00159568
Contributor : Isabelle Frapart <>
Submitted on : Tuesday, July 3, 2007 - 3:23:55 PM
Last modification on : Thursday, June 20, 2019 - 7:50:03 AM

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Patrick Gonzalez, Mélanie Duneau, Stéphane Charpentier, Thierry Normand, Lucile Mollet, et al.. Destabilization of Membranes Containing Cardiolipin or Its Precursors by Peptides Derived from Mitogaligin, a Cell Death Protein. Biochemistry, American Chemical Society, 2007, 46 (25), pp.7374-7382. ⟨10.1021/bi700213p⟩. ⟨hal-00159568⟩

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