Effect of selected alcohol dehydrogenase inhibitors on human hepatic lactate dehydrogenase activity — anin vitro study

Dudka, Jarosław; Burdan, Franciszek; Szumiło, Justyna; Tokarska, Edyta; Korobowicz, Agnieszka; Klepacz, Robert; Gieroba, Renata; Madej, B; Korobowicz, E

doi:10.1002/jat.1094

Cited by 9 publications

(6 citation statements)

References 24 publications

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“…The experiment was approved by the Local Ethical Committee. The samples were collected during the medical autopsy according to national law (Dudka et al 2004a & b).…”

Section: Methodsmentioning

confidence: 99%

Activity of NADPH‐Cytochrome P‐450 Reductase of the Human Heart, Liver and Lungs in the Presence of (‐)‐Epigallocatechin Gallate, Quercetin and Resveratrol: An in vitro Study

Dudka

Jodynis‐Liebert

Korobowicz

et al. 2005

Basic Clin Pharma Tox

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NADPH-cytochrome P-450 reductase (P-450 reductase) plays a crucial role in the metabolism of many endogenic compounds and xenobiotics detoxication. The enzyme is also involved in the toxicity of some clinically important antitumour drugs (doxorubicin) and pesticides (paraquat). P-450 reductase activates them to their more toxic metabolites via one electron reduction which triggers free radical cascade. In some cases however, such transformation is essential to produce therapeutic effect in anticancer drugs. The main purpose of the paper was to evaluate the effect of three natural compounds found in human diet: (-)-epigallocatechin gallate (EGCG), quercetin and resveratrol on P-450 reductase activity. The activity of the enzyme was determined spectrophotometrically by measurement of the rate of cytochrome c reduction at 550 nm, in vitro, using human heart, liver and lung microsomes. It was found that quercetin increased the P-450 reductase activity in human organs at all tested doses. The activity of microcosms in all organs was enhanced according to the concentrations of quercetin, which increased the activity in the order lungϾheartϾliver. Addition of EGCG to the reaction mixture enhanced the P-450 reductase activity in the following order: liverϾheartϾlung. However, no significant effect of resveratrol on P-450 reductase activity was observed. It seems that the presence of quercetin and EGCG in the diet may increase P-450 reductase activity during doxorubicin therapy with subsequent increased risk of toxicity. A beneficial effect may be obtained in anticancer therapy with bioreductive agents like tirapazamine.

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“…The experiment was approved by the Local Ethical Committee. The samples were collected during the medical autopsy according to national law (Dudka et al 2004a & b).…”

Section: Methodsmentioning

confidence: 99%

Activity of NADPH‐Cytochrome P‐450 Reductase of the Human Heart, Liver and Lungs in the Presence of (‐)‐Epigallocatechin Gallate, Quercetin and Resveratrol: An in vitro Study

Dudka

Jodynis‐Liebert

Korobowicz

et al. 2005

Basic Clin Pharma Tox

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“…Under these experimental conditions, cells were preincubated for 30 min in the presence of the ADH inhibitor 4‐methylpyrazole (4‐MP) (Cheung et al. 2003; Dudka et al. 2005; Lawrencia et al.…”

Section: Resultsmentioning

confidence: 99%

“…Inhibition of ADH by 4‐MP is concentration‐dependent, with a range of action from 1 μM up to 1000 μM in different tissues (Xie & Hurley 1999; Cheung et al. 2003; Dudka et al. 2004, 2005).…”

Section: Discussionmentioning

confidence: 99%

Increased calcium influx in the presence of ethanol in mouse pancreatic acinar cells

Castillo-Vaquero

Salido

González

2010

Int J Experimental Path

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The effects of alcohol on Ca(2+) signalling remains poorly understood. Here we have investigated the effects of acute ethanol exposure on Ca(2+) influx in mouse pancreatic acinar cells. Cells were loaded with fura-2 and the changes in fluorescence were monitored by spectrofluorimetry and imaging analysis. Stimulation of cells with 20 pM cholecystokinin evoked an oscillatory pattern in [Ca(2+)](c), both in the presence and in the absence of extracellular Ca(2+). Stimulation of cells with cholecystokinin in the presence of 50 mM ethanol led to a transformation of physiological oscillations into a single transient increase in [Ca(2+)](c). This effect was observed when Ca(2+) was present in the extracellular medium, and did not appear in its absence. Addition of 1 mM CaCl(2) to the extracellular medium, following release of Ca(2+) from intracellular stores by stimulation of cells with 1 nM cholecystokinin or 1 microM thapsigargin in the absence of extracellular Ca(2+), was followed by an increase in [Ca(2+)](c). Ca(2+) influx was increased in the presence of 50 mM ethanol. The anti-oxidant cinnamtannin B-1 (10 microM) or inhibition of alcohol dehydrogenase by 4-MP (1 mM), significantly reduced Ca(2+) influx evoked by cholecystokinin in the presence of ethanol. In summary, intoxicating concentrations of ethanol may lead to over stimulation of pancreatic acinar cells by cholecystokinin. This might be partially explained by the generation of reactive oxygen species and an increased Ca(2+) entry in the presence of ethanol. Potentially ethanol might lead to Ca(2+) overload, which is a common pathological precursor that is implicated in pancreatitis.

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“…However, the correct blood collection method is of the essence. We employed lithium heparin tubes during the acquisition of blood samples as the common chelating agent K3EDTA is in fact a potent inhibitor of ADH, and would therefore eradicate linear enzyme behaviour 36 . In order to secure optimal enzyme activity, the concentrations of ADH as well as its substrate, ethanol, were chosen to be well beyond their point of saturation, so that any effect of even an ever so slight variation in their respective amounts would be essentially nullified 24 .…”

Section: Discussionmentioning

confidence: 99%

The nanomolar sensing of nicotinamide adenine dinucleotide in human plasma using a cycling assay in albumin modified simulated body fluids

Brunnbauer

Leder

Kamali

et al. 2018

Sci Rep

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Nicotinamide adenine dinucleotide (NAD), a prominent member of the pyridine nucleotide family, plays a pivotal role in cell-oxidation protection, DNA repair, cell signalling and central metabolic pathways, such as beta oxidation, glycolysis and the citric acid cycle. In particular, extracellular NAD+ has recently been demonstrated to moderate pathogenesis of multiple systemic diseases as well as aging. Herein we present an assaying method, that serves to quantify extracellular NAD+ in human heparinised plasma and exhibits a sensitivity ranging from the low micromolar into the low nanomolar domain. The assay achieves the quantification of extracellular NAD+ by means of a two-step enzymatic cycling reaction, based on alcohol dehydrogenase. An albumin modified revised simulated body fluid was employed as standard matrix in order to optimise enzymatic activity and enhance the linear behaviour and sensitivity of the method. In addition, we evaluated assay linearity, reproducibility and confirmed long-term storage stability of extracellular NAD+ in frozen human heparinised plasma. In summary, our findings pose a novel standardised method suitable for high throughput screenings of extracellular NAD+ levels in human heparinised plasma, paving the way for new clinical discovery studies.

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Effect of selected alcohol dehydrogenase inhibitors on human hepatic lactate dehydrogenase activity — anin vitro study

Cited by 9 publications

References 24 publications

Activity of NADPH‐Cytochrome P‐450 Reductase of the Human Heart, Liver and Lungs in the Presence of (‐)‐Epigallocatechin Gallate, Quercetin and Resveratrol: An in vitro Study

Activity of NADPH‐Cytochrome P‐450 Reductase of the Human Heart, Liver and Lungs in the Presence of (‐)‐Epigallocatechin Gallate, Quercetin and Resveratrol: An in vitro Study

Increased calcium influx in the presence of ethanol in mouse pancreatic acinar cells

The nanomolar sensing of nicotinamide adenine dinucleotide in human plasma using a cycling assay in albumin modified simulated body fluids

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