Difference between revisions of "Jesina 2004 Physiol Res"

Latest revision as of 14:31, 26 March 2018

Jesina P, Kholova D, Bolehovska R, Cervinkova Z, Drahota Z, Houstek J (2004) Glycerophosphate-dependent hydrogen peroxide production by rat liver mitochondria. Physiol Res 53:305-10.

» PMID: 15209538 Open Access

Jesina P, Kholova D, Bolehovska R, Cervinkova Z, Drahota Z, Houstek J (2004) Physiol. Res.

Abstract: We studied the extent to which hormonally-induced mitochondrial glycerophosphate dehydrogenase (mGPDH) activity contributes to the supply of reducing equivalents to the mitochondrial respiratory chain in the rat liver. The activity of glycerophosphate oxidase was compared with those of NADH oxidase and/or succinate oxidase. It was found that triiodothyronine-activated mGPDH represents almost the same capacity for the saturation of the respiratory chain as Complex II. Furthermore, the increase of mGPDH activity induced by triiodothyronine correlated with an increase of capacity for glycerophosphate-dependent hydrogen peroxide production. As a result of hormonal treatment, a 3-fold increase in glycerophosphate-dependent hydrogen peroxide production by liver mitochondria was detected by polarographic and luminometric measurements. • Keywords: Rat liver mitochondria, Mitochondrial glycerophosphate dehydrogenase, Triiodothyronine, Hydrogen peroxide

• O2k-Network Lab: CZ Hradec Kralove Cervinkova Z, CZ Prague Houstek J

Labels:

Stress:Oxidative stress;RONS Organism: Rat Tissue;cell: Liver Preparation: Isolated mitochondria

HRR: Oxygraph-2k

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 {{Publication
-|title=Jesina P, Tesarova M, Fornuskova D, Vojtiskova A, Pecina P, Kaplanova V, Hansikova H, Zeman J, Houstek J (2004) Diminished synthesis of subunit a (ATP6) and altered function of ATP synthase and cytochrome c oxidase due to the mtDNA 2 bp microdeletion of TA at positions 9205 and 9206. Biochem. J. 383: 561-571.
+|title=Jesina P, Kholova D, Bolehovska R, Cervinkova Z, Drahota Z, Houstek J (2004) Glycerophosphate-dependent hydrogen peroxide production by rat liver mitochondria. Physiol Res 53:305-10.
-|authors=Jesina P, Kholova D, Bolehovska R, Cervinkova Z, Drahota Z, Houstek J
+|info=[http://www.ncbi.nlm.nih.gov/pubmed/15209538 PMID: 15209538 Open Access]
+|authors=Jesina P, Kholova D, Bolehovska R, Cervinkova Z, Drahota Z, Houstek J
 |year=2004
-|journal=Biochem. J.
+|journal=Physiol. Res.
-|abstract=Dysfunction of mitochondrial ATPase (F1Fo-ATP synthase) due to missense mutations in ATP6 [mtDNA (mitochondrial DNA)-encoded subunit a] is a frequent cause of severe mitochondrial encephalomyopathies. We have investigated a rare mtDNA mutation, i.e. a 2 bp deletion of TA at positions 9205 and 9206 (9205ΔTA), which affects the STOP codon of the ATP6 gene and the cleavage site between the RNAs for ATP6 and ''COX3'' (cytochrome c  oxidase 3). The mutation was present at increasing load in a three-generation family (in blood: 16%/82%/>98%). In the affected boy with severe encephalopathy, a homoplasmic mutation was present in blood, fibroblasts and muscle. The fibroblasts from the patient showed normal aurovertin-sensitive ATPase hydrolytic activity, a 70% decrease in ATP synthesis and an 85% decrease in COX activity. ADP-stimulated respiration and the ADP-induced decrease in the mitochondrial membrane potential at state 4 were decreased by 50%. The content of subunit a was decreased 10-fold compared with other ATPase subunits, and [35S]-methionine labelling showed a 9-fold decrease in subunit a biosynthesis. The content of COX subunits 1, 4 and 6c was decreased by 30–60%. Northern Blot and quantitative real-time reverse transcription–PCR analysis further demonstrated that the primary ATP6 – COX3 transcript is cleaved to the ATP6 and COX3 mRNAs 2–3-fold less efficiently. Structural studies by Blue-Native and two-dimensional electrophoresis revealed an altered pattern of COX assembly and instability of the ATPase complex, which dissociated into subcomplexes. The results indicate that the 9205ΔTA mutation prevents the synthesis of ATPase subunit a, and causes the formation of incomplete ATPase complexes that are capable of ATP hydrolysis but not ATP synthesis. The mutation also affects the biogenesis of COX, which is present in a decreased amount in cells from affected individuals.
+|abstract=We studied the extent to which hormonally-induced mitochondrial glycerophosphate dehydrogenase (mGPDH) activity contributes to the supply of reducing equivalents to the mitochondrial respiratory chain in the rat liver. The activity of glycerophosphate oxidase was compared with those of NADH oxidase and/or succinate oxidase. It was found that triiodothyronine-activated mGPDH represents almost the same capacity for the saturation of the respiratory chain as Complex II. Furthermore, the increase of mGPDH activity induced by triiodothyronine correlated with an increase of capacity for glycerophosphate-dependent hydrogen peroxide production. As a result of hormonal treatment, a 3-fold increase in glycerophosphate-dependent hydrogen peroxide production by liver mitochondria was detected by polarographic and luminometric measurements.
-|keywords=''ATP6'', ATP synthase, ''COX3'', cytochrome c oxidase, mitochondrial disease, mitochondrial DNA (mtDNA)
+|keywords=Rat liver mitochondria, Mitochondrial glycerophosphate dehydrogenase, Triiodothyronine, Hydrogen peroxide
-|info=[http://www.ncbi.nlm.nih.gov/pubmed/15209538 PMID: 15209538]
+|mipnetlab=CZ Hradec Kralove Cervinkova Z, CZ Prague Houstek J
+|discipline=Mitochondrial Physiology, Biomedicine
 }}
 {{Labeling
-|topics=Respiration; OXPHOS; ETS Capacity
+|injuries=Oxidative stress;RONS
+|organism=Rat
+|tissues=Liver
+|preparations=Isolated mitochondria
 |instruments=Oxygraph-2k
+|discipline=Mitochondrial Physiology, Biomedicine
 }}