Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/349006
Type: Artigo
Title: Relationship between expression of voltage-dependent anion channel (VDAC) isoforms and type of hexokinase binding sites on brain mitochondria
Author: Poleti, M.D.
Tesch, A.C.
Crepaldi, C.R.
Souza, G.H.M.F.
Eberlin, M.N.
De Cerqueira César, M.
Abstract: 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.
Subject: Apoptose
Cérebro
Glicólise
Mitocôndria
Country: Estados Unidos
Editor: Springer
Rights: Fechado
Identifier DOI: 10.1007/s12031-009-9278-4
Address: https://link.springer.com/article/10.1007%2Fs12031-009-9278-4
Date Issue: 2010
Appears in Collections:IQ - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
2-s2.0-77950188612.pdf309.09 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.