Calcium Induces Mitochondrial Oxidative Stress Because of its Binding to Adenine Nucleotide Translocase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2018-12

AUTHORS

Francisco Correa, Natalia Pavón, Mabel Buelna-Chontal, Natalia Chiquete-Félix, Luz Hernández-Esquivel, Edmundo Chávez

ABSTRACT

Several studies have demonstrated that the mitochondrial membrane switches from selective to non-selective permeability because of its improved matrix Ca2+ accumulation and oxidative stress. This process, known as permeability transition, evokes severe dysfunction in mitochondria through the opening of a non-specific pore, whose chemical nature is still under discussion. There are some proposals regarding the components of the pore structure, e.g., the adenine nucleotide translocase and dimers of the F1 Fo-ATP synthase. Our results reveal that Ca2+ induces oxidative stress, which not only increases lipid peroxidation and ROS generation but also brings about both the collapse of the transmembrane potential and the membrane release of cytochrome c. Additionally, it is shown that Ca2+ increases the binding of the probe eosin-5-maleimide to adenine nucleotide translocase. Interestingly, these effects are diminished after the addition of ADP. It is suggested that pore opening is caused by the binding of Ca2+ to the adenine nucleotide translocase. More... »

PAGES

445-450

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12013-018-0856-3

DOI

http://dx.doi.org/10.1007/s12013-018-0856-3

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1106414628

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30159781


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