Evidence map›Paper›PMID 10579630›Full record

ArticleThe Histochemical journal1999

Effects of ischaemia and reperfusion on NADH coenzyme Q reductase activity in rat liver.

W M Frederiks, K S Bosch, H Vreeling-Sindelárová

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Article in The Histochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed, 0 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

W M FrederiksDepartment of Cell Biology and Histology, University of Amsterdam, Academic Medical Center, The Netherlands.
K S Bosch
H Vreeling-Sindelárová
Academic Medical Center · NLUniversity of Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NADH coenzyme Q reductase (EC 1.6.5.3) has been suggested in the literature to be inactivated by ischaemia. In the present study, NADH coenzyme Q reductase activity was localized in unfixed cryostat sections of ischaemic rat livers and quantified using image analysis. In vitro ischaemia was induced by storage of rat liver fragments for 30, 60, and 120 min at 37 degrees C. In vivo ischaemia was provoked by clamping the afferent vessels of median and left lateral liver lobes for 60 min followed by 30, 60 and 180 min of reperfusion. NADH coenzyme Q reductase activity was demonstrated with the tetrazolium salt method in the presence of polyvinyl alcohol. Final reaction product was found in liver parenchymal cells and its distribution was homogeneous within liver lobules. Only low amounts of final reaction product were formed when the incubation was performed in the absence of the substrate NADH. A non-linear relation was found between the absorbance and incubation time when the reaction was performed in the presence of NADH. Therefore, the initial velocity was taken as the true rate of enzyme activity. A linear relationship was found for the initial velocity and section thickness up to 6 microm followed by a levelling off. Electron microscopically, NADH coenzyme Q reductase activity was localized at the outer and inner membranes of mitochondria. In vitro ischaemia up to 120 min did not affect NADH coenzyme Q reductase activity. At 30 min reperfusion after in vivo ischaemia for 60 min enzyme activity was slightly decreased in certain foci which also showed diminished lactate dehydrogenase activity. A further decrease of enzyme activities in foci was observed at 180 min reperfusion after ischaemia. It is concluded that NADH coenzyme Q reductase activity is not sensitive to ischaemia. Furthermore, it is likely that the enzyme leaks from liver parenchymal cells into the circulation during reperfusion after ischaemia.

Indexed as

ReperfusionAnimalsElectron Transport Complex IIschemiaLiverMaleNADH, NADPH OxidoreductasesRatsRats, WistarElectron Transport Complex INADH, NADPH Oxidoreductases

Identifiers

PMID10579630
OpenAlexW1488588533

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.