| http://purl.uniprot.org/citations/18790835 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18790835 | http://www.w3.org/2000/01/rdf-schema#comment | "Bcl-2/adenovirus E1B 19-kDa protein-interacting protein 3 (Bnip3) is a member of the Bcl-2 homology domain 3-only subfamily of proapoptotic Bcl-2 proteins and is associated with cell death in the myocardium. In this study, we investigated the potential mechanism(s) by which Bnip3 activity is regulated. We found that Bnip3 forms a DTT-sensitive homodimer that increased after myocardial ischemia-reperfusion (I/R). The presence of the antioxidant N-acetylcysteine reduced I/R-induced homodimerization of Bnip3. Overexpression of Bnip3 in cells revealed that most of exogenous Bnip3 exists as a DTT-sensitive homodimer that correlated with increased cell death. In contrast, endogenous Bnip3 existed mainly as a monomer under normal conditions in the heart. Screening of the Bnip3 protein sequence revealed a single conserved cysteine residue at position 64. Mutation of this cysteine to alanine (Bnip3C64A) or deletion of the NH2-terminus (amino acids 1-64) resulted in reduced cell death activity of Bnip3. Moreover, mutation of a histidine residue in the COOH-terminal transmembrane domain to alanine (Bnip3H173A) almost completely inhibited the cell death activity of Bnip3. Bnip3C64A had a reduced ability to interact with Bnip3, whereas Bnip3H173A was completely unable to interact with Bnip3, suggesting that homodimerization is important for Bnip3 function. A consequence of I/R is the production of reactive oxygen species and oxidation of proteins, which promotes the formation of disulfide bonds between proteins. Thus, these experiments suggest that Bnip3 functions as a redox sensor where increased oxidative stress induces homodimerization and activation of Bnip3 via cooperation of the NH2-terminal cysteine residue and the COOH-terminal transmembrane domain."xsd:string |
| http://purl.uniprot.org/citations/18790835 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajpheart.00552.2008"xsd:string |
| http://purl.uniprot.org/citations/18790835 | http://purl.uniprot.org/core/author | "Lee Y."xsd:string |
| http://purl.uniprot.org/citations/18790835 | http://purl.uniprot.org/core/author | "Huang C."xsd:string |
| http://purl.uniprot.org/citations/18790835 | http://purl.uniprot.org/core/author | "Gustafsson A.B."xsd:string |
| http://purl.uniprot.org/citations/18790835 | http://purl.uniprot.org/core/author | "Kubli D.A."xsd:string |
| http://purl.uniprot.org/citations/18790835 | http://purl.uniprot.org/core/author | "Quinsay M.N."xsd:string |
| http://purl.uniprot.org/citations/18790835 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18790835 | http://purl.uniprot.org/core/name | "Am J Physiol Heart Circ Physiol"xsd:string |
| http://purl.uniprot.org/citations/18790835 | http://purl.uniprot.org/core/pages | "H2025-31"xsd:string |
| http://purl.uniprot.org/citations/18790835 | http://purl.uniprot.org/core/title | "Bnip3 functions as a mitochondrial sensor of oxidative stress during myocardial ischemia and reperfusion."xsd:string |
| http://purl.uniprot.org/citations/18790835 | http://purl.uniprot.org/core/volume | "295"xsd:string |
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