Disease relevance of VDAC2

• Changes of voltage-dependent anion-selective channel proteins VDAC1 and VDAC2 brain levels in patients with Alzheimer's disease and Down syndrome [1].

High impact information on VDAC2

• During apoptosis, Bak and Bax form both homo- and hetero-oligomeric complexes that still retain some VDAC-2 [2].
• However, the oligomeric VDAC-2 complexes are diminished, and Bak does not interact with VDAC-2 in Bax-deficient HCT116 cells [2].
• Twelve differentially expressed cDNAs were identified and cloned, one of them having 99.4% sequence homology with isoform 2 of a voltage-dependent anion channel (VDAC-2) [3].
• In DS cerebellum, total VDAC1 protein was elevated significantly whereas VDAC2 did not show any significant alterations [1].
• VDAC1 (SWISS-PROT accession number P21796) and VDAC2 (P45880) were unambiguously identified and quantified, but VDAC3 was not found [1].

Biological context of VDAC2

• In particular, alterations in the post-translational modifications of voltage-dependent anion channel 2 (VDAC2) were found, and its relevance to regulating mitochondrial membrane permeability and activation of apoptotic pathways is discussed [4].

Other interactions of VDAC2

• Evidence of apoptosis was associated with overexpression of the heart mitochondrial voltage-dependent anion channel-2 protein and endonuclease G in tissue specimens from dogs with induced DCM [5].
• Microarray profiling of fas-resistant versus sensitive cells identified a set of genes including STATs, caspase 1, cyclin D1, Bcl-xL, VDAC2, and BAD [6].

References