Cookies help us deliver our services. By using our services, you agree to our use of cookies. More information

Difference between revisions of "Kiss 2014 FASEB J"

From Bioblast
Line 1: Line 1:
{{Publication
{{Publication
|title=Kiss G, Konrad C, Pour-Ghaz I, Mansour JJ, Németh B, Starkov AA, Adam-Vizi V, Chinopoulos C (2014) Diaphorases provide NAD+ in anoxia. FASEB J [Epub ahead of print].
|title=Kiss G, Konrad C, Pour-Ghaz I, Mansour JJ, Németh B, Starkov AA, Adam-Vizi V, Chinopoulos C (2014) Diaphorases provide NAD+ in anoxia. FASEB J 28:1682-97.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/24391134 PMID: 24391134]
|info=[http://www.ncbi.nlm.nih.gov/pubmed/24391134 PMID: 24391134]
|authors=Kiss G, Konrad C, Pour-Ghaz I, Mansour JJ, Németh B, Starkov AA, Adam-Vizi V, Chinopoulos C
|authors=Kiss G, Konrad C, Pour-Ghaz I, Mansour JJ, Németh B, Starkov AA, Adam-Vizi V, Chinopoulos C
Line 23: Line 23:
|area=Respiration
|area=Respiration
|instruments=Oxygraph-2k, O2k-Fluorometer
|instruments=Oxygraph-2k, O2k-Fluorometer
|additional=Labels, [Epub ahead of print]
|additional=Labels
}}
}}
* >> O2k-Fluorometry protocol for [[Magnesium green]]
* >> O2k-Fluorometry protocol for [[Magnesium green]]

Revision as of 15:02, 26 February 2015

Publications in the MiPMap
Kiss G, Konrad C, Pour-Ghaz I, Mansour JJ, Németh B, Starkov AA, Adam-Vizi V, Chinopoulos C (2014) Diaphorases provide NAD+ in anoxia. FASEB J 28:1682-97.

» PMID: 24391134

Kiss G, Konrad C, Pour-Ghaz I, Mansour JJ, Németh B, Starkov AA, Adam-Vizi V, Chinopoulos C (2014) FASEB J

Abstract: Substrate-level phosphorylation mediated by succinyl-CoA ligase in the mitochondrial matrix produces highenergy phosphates in the absence of oxidative phosphorylation. Furthermore, when the electron transport chain is dysfunctional, provision of succinyl-CoA by the α-ketoglutarate dehydrogenase complex (KGDHC) is crucial for maintained operation of succinyl-CoA ligase yielding ATP, preventing the adenine nucleotide translocase from reversing. Here we addressed the source of NAD+ supply for KGDHC under anoxic conditions and inhibition of complex I. Using pharmacological tools, specific substrates and by examining tissues from pigeon liver exhibiting no diaphorase activity we show that mitochondrial diaphorases in the mouse liver contributed up to 81% to the NAD+ pool during respiratory inhibition. Under these conditions, KGDHC function, essential for the provision of succinyl-CoA to succinyl-CoA ligase, is supported by NAD+ derived from diaphorases. By this, diaphorases contribute to the maintenance of substrate-level phosphorylation during respiratory inhibition, which is manifested in the forward operation of adenine nucleotide translocase. Finally, we show that reoxidation of the reducible substrates for the diaphorases is mediated by complex III of the respiratory chain. Keywords: succinyl-CoA ligase; adenine nucleotide translocase; DT-diaphorase; reducing equivalent

O2k-Network Lab: HU Budapest Chinopoulos C, HU Budapest Tretter L


Labels: MiParea: Respiration 





HRR: Oxygraph-2k, O2k-Fluorometer 

Labels