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(Reference retrieved automatically from SciELO through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Purification and characterization of avian cortical mitochondrial VDAC: identification of post-translational modifications of rat and avian neuronal porins

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Author(s):
Phelipe Augusto Mariano Vitale [1] ; Carla Rossini Crepaldi [2] ; Andréa Cristina Tesch [3] ; Ricardo de Albuquerque [4] ; Marcelo de Cerqueira César [5]
Total Authors: 5
Affiliation:
[1] Universidade de São Paulo. Faculdade de Zootecnia e Engenharia de Alimentos. Departamento de Ciências Básicas - Brasil
[2] Universidade de São Paulo. Faculdade de Zootecnia e Engenharia de Alimentos. Departamento de Ciências Básicas - Brasil
[3] Universidade de São Paulo. Faculdade de Zootecnia e Engenharia de Alimentos. Departamento de Ciências Básicas - Brasil
[4] USP. Faculdade de Medicina Veterinária e Zootecnia. Departamento de Nutrição e Produção Animal
[5] Universidade de São Paulo. Faculdade de Zootecnia e Engenharia de Alimentos. Departamento de Ciências Básicas - Brasil
Total Affiliations: 5
Document type: Journal article
Source: Pesquisa Veterinária Brasileira; v. 32, n. 12, p. 1361-1366, 2012-12-00.
Abstract

VDAC (voltage-dependent anion channel) is a pore forming protein from outer mitochondrial membrane. It has key functions on energetic metabolism, and cell death and survival. VDAC characterization is important for understanding mitochondrial interactions with cytosolic proteins, such as hexokinase (HK). HK-VDAC interaction supports preferential access to intramitochondrial ATP in neural cells. Brain HK interacts in different ways with VDAC. It results in two HK binding sites (A and B). VDAC isoforms differential metabolic roles may be explained by the presence of post-translational modifications. In this study we purified avian neuronal mitochondrial VDAC1. At same time we showed that VDACs 1 and 2 pI heterogeneity in rat and avian brains is due to phosphorylation. Purified VDAC had a molecular weight of 30 KDa. The purified VDAC submitted to phosphorylated protein staining on gel, was dephosphorylated. The knowledge of presence or absence of VDAC phosphorylation is important for understanding the molecular nature basis of A and B HK binding sites in brain mitochondria. (AU)

FAPESP's process: 09/06687-2 - Proteomic study of apoptosis in avian neurons: the role of VDAC 1 and VDAC 2
Grantee:Carla Rossini Crepaldi
Support Opportunities: Scholarships in Brazil - Master
FAPESP's process: 10/05560-6 - Interactomic analysis of hexokinase-VDAC-ANT complex in rat, bovine and chicken neuronal cells
Grantee:Marcelo de Cerqueira César
Support Opportunities: Regular Research Grants