Titration of lysine residues on adenine nucleotide translocase by fluorescamine induces permeability transition. (31st December 2013)

• Record Type: Journal Article
• Authors: Buelna‐Chontal, Mabel; Pavón, Natalia; Correa, Francisco; Hernández‐Esquivel, Luz; Chávez, Edmundo
• Is Part Of: Cell biology international. Volume 38:Number 3(2014)
• Page Start: 287
• Page End: 295
• Publication Date: 2013-12-31
• Subjects: Cytology -- Periodicals; Cells -- Periodicals; 571.605
• DOI: 10.1002/cbin.10142
• Languages: English
• ISSNs: 1065-6995

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <sec id="cbin10142-sec-0001" sec-type="section"> <p>Chemical modification of primary amino groups of mitochondrial membrane proteins by the fluorescent probe fluorescamine induces non‐specific membrane permeabilisation. Titration of the lysine ϵ‐amino group promoted efflux of accumulated Ca²⁺, collapse of transmembrane potential and mitochondrial swelling. Ca²⁺ release was inhibited by cyclosporin A. Considering the latter, we assumed that fluorescamine induces permeability transition. Carboxyatractyloside also inhibited the reaction. Using a polyclonal antibody for adenine nucleotide translocase, Western blot analysis showed that the carrier appeared labelled with the fluorescent probe. The results point out the importance of the ϵ‐amino group of lysine residues, located in the adenine nucleotide carrier, on the modulation of membrane permeability, since its blockage suffices to promote opening of the non‐specific nanopore.</p> </sec> </abstract>