Formaldehyde metabolism and formaldehyde-induced stimulation of lactate production and glutathione export in cultured neurons

2013 ◽  
Vol 125 (2) ◽  
pp. 260-272 ◽  
Author(s):  
Ketki Tulpule ◽  
Michaela C. Hohnholt ◽  
Ralf Dringen
2020 ◽  
Vol 16 (4) ◽  
pp. 401-408
Author(s):  
Farideh Bahrami ◽  
Zahra Bahari ◽  
Reihaneh Abolghasemi ◽  
Lida Golmanesh ◽  
Gholam Hossein Meftahi

2008 ◽  
Vol 63 (9-10) ◽  
pp. 773-779 ◽  
Author(s):  
Ana Maneva ◽  
Borislava Taleva

The aim of the present study was to assess if some flavonic compounds (quercetin, piceatannol and apigenin) and ascorbic acid could interfere with the Lf stimulatory effect on the erythrocyte function. Quercetin (1.5 μm) and piceatannol (30 μm) showed an additive effect on Lf stimulation of Na+/K+-ATPase when used together with Lf. The enhancement of Lf stimulation on Na+/K+-ATPase in the presence of flavonoids was probably due to their antioxidative properties and/or to their involvement in the erythrocyte signaling. None of the estimated flavonoids showed an effect on Lf stimulation of the lactate production. Quercetin itself enhanced the ATPase activity but did not affect the lactate formation. Apigenin (1.5 μm) enhanced reliably the lactate generation, but it did not exert any effect on the ATPase activity. High concentration of ascorbic acid (60 mm) did not change the Lf stimulatory effect on Na+/K+-ATPase, but decreased the Lf-specific-binding. A significantly strong inhibitory effect on the Lf-specific binding exerted the electron acceptors NAD+ (2 mm) and FAD (2 mm). These effects concern most likely the competition with Lf for electron(s) which is (are) provided from the erythrocyte intercellular electron transport chain(s).


2007 ◽  
Vol 90 (9) ◽  
pp. 093901 ◽  
Author(s):  
Jun Suzurikawa ◽  
Hirokazu Takahashi ◽  
Ryohei Kanzaki ◽  
Masayuki Nakao ◽  
Yuzo Takayama ◽  
...  

2015 ◽  
Vol 253 ◽  
pp. 272-278 ◽  
Author(s):  
Ryo Tanamoto ◽  
Yutaka Shindo ◽  
Norihisa Miki ◽  
Yoshinori Matsumoto ◽  
Kohji Hotta ◽  
...  

1980 ◽  
Vol 303 (19) ◽  
pp. 1100-1102 ◽  
Author(s):  
Donald S. Fraley ◽  
Sheldon Adler ◽  
Frank J. Bruns ◽  
Barbara Zett

1985 ◽  
Vol 69 (4) ◽  
pp. 435-440 ◽  
Author(s):  
A. Bevington ◽  
A. J. Asbury ◽  
C. J. Preston ◽  
R. G. G. Russell

1. Orthophosphate (Pi), adenosine 5′-diphosphate (ADP), adenosine 5′-triphosphate (ATP) and 2,3-diphosphoglycerate (2,3-DPG) were measured in the erythrocytes of patients in an intensive care unit. 2. The patients’ plasma concentration of Pi varied from 0.1 to 4.2 mmol/l, and the corresponding concentration in erythrocytes varied from 0.1 to 2.0 mmol/litre of cells. 3. Marked ATP depletion (less than 1 mmol/litre of cells) was only observed when erythrocyte Pi was less than 0.3 mmol/litre of cells and plasma Pi was less than 0.35 mmol/l. No dependence of 2,3-DPG concentration on the cellular concentration of Pi was detected. 4. The phosphorylation potential [ATP]/([ADP] × [Pi]) varied inversely with the erythrocyte concentration of Pi. Hence the calculated free energy of hydrolysis of ATP in the cell increased from −58 kJ/mol in the most hypophosphataemic samples to −51 kJ/mol in the most hyperphosphataemic. Such changes may adversely affect cell function by altering the steady state mass-action ratios of ATPase reactions. 5. When erythrocytes from normal donors were incubated in solutions containing 1 or 5 mmol/l Pi, the cellular concentrations of Pi stabilized at 1.09 and 2.85 mmol/litre of cells respectively. The corresponding rates of lactate production were 2.09 and 3.11 mmol h−1 litre−1 of cells. 6. In spite of this stimulation of glycolysis (and hence of the flux through ATP synthesizing steps of the Embden-Meyerhof pathway), no significant change in ATP concentration was observed. As in the patients' cells, this indicates that, when extracellular Pi concentrations are perturbed, the concentrations, in erythrocytes, of organic phosphates are more closely regulated than the concentration of Pi.


1998 ◽  
Vol 45 (3) ◽  
pp. 825-831
Author(s):  
K Winiarska ◽  
P Bozko ◽  
T Lietz ◽  
J Bryła

The effect of 2-aminobicyclo[2.2.1]heptan-2-carboxylic acid (BCH), an L-leucine nonmetabolizable analogue and an allosteric activator of glutamate dehydrogenase, on glucose and glutamine synthesis was studied in rabbit renal tubules incubated with alanine, aspartate or proline in the presence of glycerol and octanoate, i.e. under conditions of efficient glucose formation. With alanine+glycerol+octanoate the addition of BCH resulted in a stimulation of alanine and glycerol consumption, accompanied by an increased glucose, lactate and glutamine synthesis. In contrast, when alanine was substituted by either aspartate or proline, BCH altered neither glucose formation nor glutamine and glutamate synthesis, while an accelerated glycerol utilization was accompanied by a small increase in lactate production. In view of the BCH-induced changes in intracellular metabolite levels the acceleration of gluconeogenesis by BCH in the presence of alanine+glycerol+octanoate is probably due to (i) increased uptake of alanine via alanine aminotransferase, (ii) stimulation of phosphoenolpyruvate carboxykinase, a key-enzyme of gluconeogenesis, (iii) rise of glucose-6-phosphatase activity, as well as (iv) activation of the malate-aspartate shuttle resulting in an augmented glycerol utilization for lactate and glucose synthesis.


1993 ◽  
Vol 264 (1) ◽  
pp. H163-H170 ◽  
Author(s):  
M. F. Janier ◽  
J. L. Vanoverschelde ◽  
S. R. Bergmann

To evaluate the role of adenosine receptors in the mediation of adenosine-induced protection of the heart during ischemia and reperfusion, isolated rabbit hearts were perfused at constant flow with 1 microM adenosine started before low-flow ischemia followed by reperfusion. Adenosine delayed the time of onset of ischemic contracture [to 28 +/- 19 (SD) min compared with 10 +/- 10 min in control hearts] and decreased the amplitude of ischemic contracture (29 +/- 16 vs. 48 +/- 14 mmHg; P<0.05 for each compared with controls). This protection was accompanied by an increase in tissue ATP content (1.72 +/- 0.78 vs. 0.96 +/- 0.23 mumol/g; P < 0.05) and stimulation of anaerobic glycolysis (lactate production of 0.78 +/- 0.28 mumol.g-1 x min-1 compared with 0.53 +/- 0.23 mumol.g-1 x min-1; P < 0.05). Functional recovery during reperfusion was enhanced by adenosine (developed pressure 88 +/- 16% compared with 57 +/- 23% of baseline; P < 0.05), and tissue necrosis, assessed by creatine kinase release, was decreased. The potent, nonselective adenosine receptor blocker 8-phenyltheophylline (10 microM) blocked all of the salutary effects of adenosine. Adenosine given only at reperfusion modestly attenuated reperfusion-induced contracture. The results suggest that exogenous adenosine attenuates ischemic injury by receptor-mediated stimulation of anaerobic glycolysis. During reperfusion its protective action is related to vasodilation.


2009 ◽  
Vol 94 (2) ◽  
pp. 670-677 ◽  
Author(s):  
Malcolm C. Richardson ◽  
Susan Ingamells ◽  
Chantal D. Simonis ◽  
Iain T. Cameron ◽  
Rajiv Sreekumar ◽  
...  

Abstract Context: Production of 3-carbon units (as lactate) by granulosa cells (GCs) is important in follicular and oocyte development and may be modulated by metformin. Objective: The aim of the study was to examine the action of metformin on GC lactate production and potential mediation via AMP-activated protein kinase (AMPK). Design: GCs were prepared from follicular aspirates. After exposure to metformin and other potential modulators of AMPK in culture, aspects of cellular function were examined. Setting: The study was conducted in a private fertility clinic/university academic center. Patients: Women undergoing routine in vitro fertilization participated in the study. Interventions: All agents were added in culture. Main Outcome Measures: Lactate output of GCs was measured. Cell extracts were prepared after culture, and phosphorylated forms of AMPK and acetyl CoA carboxylase (ACC) were assayed using Western analysis. Results: Metformin led to a rapid increase in lactate production by GCs [minimum effective dose, 250 μm; maximum dose studied, 1 mm (1.22-fold; P &lt; 0.01)]. This dose range of metformin was similar to that required for stimulation of phospho-AMPK in GCs [minimum effective dose, 250 μm; maximum effect, 500 μm (2.01-fold; P &lt; 0.001)]. Increasing phospho-ACC, as a representative downstream target regulated by AMPK, was apparent over a lower range (minimum effective dose, 31 μm; maximum effect, 250 μm; P &lt; 0.001). A level of metformin (125 μm) insufficient for the stimulation of lactate output when used alone potentiated the effects of suboptimal doses of insulin on lactate production. Adiponectin (2.5 μg/ml) had a small but significant effect on lactate output. Conclusions: Metformin activates AMPK in GCs, stimulating lactate production and increasing phospho-ACC. Metformin also enhances the action of suboptimal insulin concentrations to stimulate lactate production.


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