Relationship Between Expression of Voltage-Dependent Anion Channel (VDAC) Isoforms and Type of Hexokinase Binding Sites on Brain Mitochondria

• Published in: Journal of molecular neuroscience Vol. 41; no. 1; pp. 48 - 54
• Main Authors: Poleti, Mirele Daiana, Tesch, Andrea Cristina, Crepaldi, Carla Rossini, Souza, Gustavo Henrique Martins Ferreira, Eberlin, Marcos Nogueira, de Cerqueira César, Marcelo
• Format: Journal Article
• Language: English
• Published: New York Humana Press Inc 01-05-2010; Springer Nature B.V
• Subjects: Alzheimer's disease; Amino Acid Sequence; Animals; Anion channels; Apoptosis; Binding Sites; Biomedical and Life Sciences; Biomedicine; Brain; Brain - cytology; Brain - metabolism; Cattle; Cell Biology; Chickens; Electrophoresis, Gel, Two-Dimensional; Glycerol; Glycolysis; Hexokinase; Hexokinase - metabolism; Laboratories; Mass Spectrometry; Metabolism; Mitochondria; Mitochondria - metabolism; Mitochondrial Proteins - metabolism; Molecular Sequence Data; Nervous system; Neurochemistry; Neurology; Neurosciences; Physiology; pore-forming proteins; Protein Isoforms - genetics; Protein Isoforms - metabolism; Proteins; Proteomics; Rats; Voltage-Dependent Anion Channel 1 - genetics; Voltage-Dependent Anion Channel 1 - metabolism; Voltage-Dependent Anion Channel 2 - genetics; Voltage-Dependent Anion Channel 2 - metabolism; United States > US; Glycolysis; VDAC; Brain; Mitochondria; Hexokinase; Apoptosis
• ISSN: 0895-8696; 1559-1166
• DOI: 10.1007/s12031-009-9278-4

Voltage-dependent anion channels (VDAC) are pore-forming proteins found in the outer mitochondrial membrane of eukaryotes. VDACs are known to play an essential role in cellular metabolism and in early stages of apoptosis. In mammals, three VDAC isoforms have been identified. A proteomic approach was exploited to study the expression of VDAC isoforms in rat, bovine, and chicken brain mitochondria. Given the importance of mitochondrially bound hexokinase in regulation of aerobic glycolysis in brain, we studied the possibility that differences in the relative expression of VDAC isoforms may be a factor in determining the species-dependent ratio of type A/type B hexokinase binding sites on brain mitochondria. The spots were characterized, and the signal intensities among spots were compared. VDAC1 was the most abundantly expressed of the three isoforms. Moreover the expression of VDAC1 plus VDAC2 was significantly higher in bovine than in rat brain. Chicken brain mitochondria showed the highest VDAC1 expression and the lowest of VDAC2. Bovine brain mitochondria had the highest VDAC2 levels. We concluded that the nature of hexokinase binding site is not determined by the expression of a single VDAC isoform.