Liver mitochondrial respiratory plasticity and oxygen uptake evoked by cobalt chloride in rats with low and high resistance to extreme hypobaric hypoxia

2019 ◽  
Vol 97 (5) ◽  
pp. 392-399 ◽  
Author(s):  
Natalia Kurhaluk ◽  
Oleksaner Lukash ◽  
Valentina Nosar ◽  
Alla Portnychenko ◽  
Volodymyr Portnichenko ◽  
...  
Keyword(s):  
Oxygen Uptake ◽  
High Altitude ◽  
High Resistance ◽  
Hypobaric Hypoxia ◽  
Cobalt Chloride ◽  
Glucose And Lipid Metabolism ◽  
Transport Chain ◽  
Respiratory Plasticity ◽  
Mitochondrial Oxidation ◽  
Mitochondrial Respiratory

High-altitude intolerance and consequently high-altitude sickness, is difficult to predict. Liver is an essential organ in glucose and lipid metabolism, and may play key role in the adaptation to high altitude. In response to extreme high altitude, mitochondrial respiration exhibits changes in substrate metabolism, mitochondrial electron transport chain activity, and respiratory coupling. We determined the cobalt chloride (CoCl2) effects on liver mitochondrial plasticity and oxygen uptake in rats with low resistance (LR) and high resistance (HR) to extreme hypobaric hypoxia. The polarographic method proposed by Chance and Williams was used as a simple and effective tool to trace mitochondrial functionality and oxygen consumption. HR rats had more efficient processes of NADH- and FAD-generated mitochondrial oxidation. CoCl2 promoted more efficient NADH-generated and diminished less efficient FAD-generated mitochondrial respiratory reactions in HR rats. CoCl2 diminished both aerobic and anaerobic processes in LR rats. Glutamate and pyruvate substrates of NADH-generated mitochondrial pathways were highly affected by CoCl2. Red blood cells acted as cobalt depots in HR and LR rats. We have unveiled several mechanisms leading to differentiated mitochondrial respiratory responses to hypobaric hypoxia in LR and HR rats. Our study strongly supports the existence of adaptive liver mitochondrial plasticity to extreme hypoxia.

scholarly journals The mitochondrial oxidation of quinol monophosphates

1970 ◽  
Vol 118 (5) ◽  
pp. 719-731
Author(s):  
J. M. Young
Keyword(s):  
Electron Transport ◽  
Cytochrome C ◽  
Oxygen Uptake ◽  
Cytochrome Oxidase ◽  
Rat Liver ◽  
Mode Of Action ◽  
Electron Transport Chain ◽  
Rapid Reduction ◽  
Transport Chain ◽  
Mitochondrial Oxidation

1. Mitochondria from ox heart and rat liver catalysed a slow cyanide-sensitive oxidation of 2,3-dimethylnaphthaquinol monophosphate, duroquinol monophosphate, menadiol 1-phosphate and menadiol 4-phosphate. 2. The release of Pi was concomitant with oxygen uptake. 3. The oxidation was somewhat stimulated by Ca2+ and Pi, and weakly inhibited by 2,4-dinitrophenol. 4. The quinol monophosphates effected a rapid reduction of free cytochrome c, and consequently addition of cytochrome c greatly increased the rate of the mitochondrial oxidation of 2,3-dimethylnaphthaquinol monophosphate. 5. This quinol phosphate interacts with the electron-transport chain at the level of cytochrome c. 6. Polylysine promoted an interaction between 2,3-dimethylnaphthaquinol monophosphate and cytochrome oxidase. Thus, although polylysine blocks mitochondrial oxidations via reduced cytochrome c, the oxidation of the quinol phosphate was strongly stimulated. 7. This stimulation was most effective in the most intact mitochondrial preparations and was inhibited by ADP and by Pi. 8. The implications of these results for factors limiting the rate of quinol phosphate oxidation, the mode of action of stimulators and the mechanism of Pi formation are discussed.

Endothelin-1 gene variants and levels associate with adaptation to hypobaric hypoxia in high-altitude natives

2006 ◽  
Vol 341 (4) ◽  
pp. 1218-1224 ◽  
Author(s):  
Charu Rajput ◽  
Shehla Najib ◽  
Tsering Norboo ◽  
Farhat Afrin ◽  
M.A. Qadar Pasha
Keyword(s):  
High Altitude ◽  
Hypobaric Hypoxia ◽  
Gene Variants ◽  
Endothelin 1 ◽  
High Altitude Natives

scholarly journals Regulation of cold-induced thermogenesis by the RNA binding protein FAM195A

2021 ◽  
Vol 118 (23) ◽  
pp. e2104650118
Author(s):  
Jessica Cannavino ◽  
Mengle Shao ◽  
Yu A. An ◽  
Svetlana Bezprozvannaya ◽  
Shiuhwei Chen ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Uncoupling Protein ◽  
Rna Binding Protein ◽  
Cold Environments ◽  
Transport Chain ◽  
Brown Adipose ◽  
Mitochondrial Oxidation ◽  
Branched Chain

Homeothermic vertebrates produce heat in cold environments through thermogenesis, in which brown adipose tissue (BAT) increases mitochondrial oxidation along with uncoupling of the electron transport chain and activation of uncoupling protein 1 (UCP1). Although the transcription factors regulating the expression of UCP1 and nutrient oxidation genes have been extensively studied, only a few other proteins essential for BAT function have been identified. We describe the discovery of FAM195A, a BAT-enriched RNA binding protein, which is required for cold-dependent thermogenesis in mice. FAM195A knockout (KO) mice display whitening of BAT and an inability to thermoregulate. In BAT of FAM195A KO mice, enzymes involved in branched-chain amino acid (BCAA) metabolism are down-regulated, impairing their response to cold. Knockdown of FAM195A in brown adipocytes in vitro also impairs expression of leucine oxidation enzymes, revealing FAM195A to be a regulator of BCAA metabolism and a potential target for metabolic disorders.

Elevated plasma S100B levels in high altitude hypobaric hypoxia do not correlate with acute mountain sickness

2014 ◽  
Vol 36 (9) ◽  
pp. 779-785 ◽  
Author(s):  
Craig D. Winter ◽  
Timothy R. Whyte ◽  
John Cardinal ◽  
Stephen E. Rose ◽  
Peter K. O’Rourke ◽  
...  
Keyword(s):  
High Altitude ◽  
Hypobaric Hypoxia ◽  
Acute Mountain Sickness ◽  
Elevated Plasma ◽  
Mountain Sickness

scholarly journals Thin Air Resulting in High Pressure: Mountain Sickness and Hypoxia-Induced Pulmonary Hypertension

2017 ◽  
Vol 2017 ◽  
pp. 1-17 ◽  
Author(s):  
Jan Grimminger ◽  
Manuel Richter ◽  
Khodr Tello ◽  
Natascha Sommer ◽  
Henning Gall ◽  
...  
Keyword(s):  
Pulmonary Hypertension ◽  
High Altitude ◽  
Hypobaric Hypoxia ◽  
Current Knowledge ◽  
Treatment Options ◽  
Acute Response ◽  
Mechanisms Of Adaptation ◽  
Mountain Sickness

With rising altitude the partial pressure of oxygen falls. This phenomenon leads to hypobaric hypoxia at high altitude. Since more than 140 million people permanently live at heights above 2500 m and more than 35 million travel to these heights each year, understanding the mechanisms resulting in acute or chronic maladaptation of the human body to these circumstances is crucial. This review summarizes current knowledge of the body’s acute response to these circumstances, possible complications and their treatment, and health care issues resulting from long-term exposure to high altitude. It furthermore describes the characteristic mechanisms of adaptation to life in hypobaric hypoxia expressed by the three major ethnic groups permanently dwelling at high altitude. We additionally summarize current knowledge regarding possible treatment options for hypoxia-induced pulmonary hypertension by reviewing in vitro, rodent, and human studies in this area of research.

Diseases of high terrestrial altitudes

2010 ◽  
pp. 1402-1408
Author(s):  
Andrew J. Pollard ◽  
Buddha Basnyat ◽  
David R. Murdoch
Keyword(s):  
High Altitude ◽  
Hypobaric Hypoxia ◽  
Cell Mass ◽  
Red Cell ◽  
Physiological Changes ◽  
Exposed Individual ◽  
Extreme Altitude ◽  
First Arrival ◽  
The Individual ◽  
Over Time

Ascent to altitudes above 2500 m leads to exposure to hypobaric hypoxia. This affects performance on first arrival at high altitude and disturbs sleep, but physiological changes occur over time to defend arterial and tissue oxygenation and allow the individual to adjust. This process of acclimatization includes (1) an increase in the rate and depth of breathing; and (2) an increase in red cell mass, and in red cell 2,3-diphosphoglycerate. Acclimatization is no longer possible at extreme altitude (>5800 m) and the exposed individual will gradually deteriorate....

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