Application of 2D BN/SDS-PAGE coupled with mass spectrometry for identification of VDAC-associated protein complexes related to mitochondrial binding sites for type I brain hexokinase

Two types of binding sites for hexokinase, designated as Type A or Type B sites, have been shown to coexist on brain mitochondria. The ratio of these sites varies between species. HK1 attaches by reversibly binding to the voltage dependent anion channel (VDAC). Regarding the nature of hexokinase bin...

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Published inMitochondrion Vol. 13; no. 6; pp. 823 - 830
Main Authors Crepaldi, Carla Rossini, Vitale, Phelipe Augusto Mariano, Tesch, Andrea Cristina, Laure, Hélen Julie, Rosa, José César, de Cerqueira César, Marcelo
Format Journal Article
LanguageEnglish
Published Netherlands 01.11.2013
Subjects
Animals
Binding Sites
Blotting, Western
Brain - enzymology
Brain - metabolism
Cattle
Electrophoresis, Polyacrylamide Gel - methods
Hexokinase - metabolism
Mass Spectrometry - methods
Rats
Voltage-Dependent Anion Channels - metabolism
VDAC
Mitochondria
BN/SDS PAGE
Interactome
Hexokinase
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Summary:Two types of binding sites for hexokinase, designated as Type A or Type B sites, have been shown to coexist on brain mitochondria. The ratio of these sites varies between species. HK1 attaches by reversibly binding to the voltage dependent anion channel (VDAC). Regarding the nature of hexokinase binding sites, we investigated if it was linked to distinct VDAC interactomes. We approached this question by 2D BN/SDS-PAGE of mitochondria, followed by mass spectrometry. Our results are consistent with the possibility that the ratio of Type A/Type B sites is due to differential VDAC interactions in bovine and rat neuronal cells.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:1567-7249
1872-8278
DOI:10.1016/j.mito.2013.05.009