Literature DB >> 14759607

All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain.

Marcelo de Cerqueira Cesar1, John E Wilson.   

Abstract

All three isoforms of the voltage-dependent anion channel (VDAC) were detected by immunoblot analysis of mitochondria isolated from rat, rabbit, and bovine brain. All three isoforms were associated with mitochondria after fractionation of rat brain extracts on sucrose density gradients. No VDAC isoforms were detected in non-mitochondrial fractions. Relative levels of the mRNAs coding the VDAC isoforms in rat, rabbit, and bovine brain were determined by RT-PCR. In all three species, the mRNA for VDAC2 was predominant. Relative to the mRNA for VDAC3, mRNAs for both VDAC1 and VDAC2 were more highly expressed in bovine brain than in rat brain. These results are consistent with the possibility that differences in 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.

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Year:  2004        PMID: 14759607     DOI: 10.1016/j.abb.2003.12.030

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN: 0003-9861            Impact factor:   4.013


  25 in total

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5.  Critical role for voltage-dependent anion channel 2 in infectious bursal disease virus-induced apoptosis in host cells via interaction with VP5.

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Review 8.  Inhibition of mitochondrial membrane permeability as a putative pharmacological target for cardioprotection.

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9.  Two-color STED microscopy reveals different degrees of colocalization between hexokinase-I and the three human VDAC isoforms.

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Journal:  PMC Biophys       Date:  2010-03-05

10.  Quinidine partially blocks mitochondrial voltage-dependent anion channel (VDAC).

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Journal:  Eur Biophys J       Date:  2020-03-09       Impact factor: 1.733

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