scholarly journals Quantitative Analysis of the High Temperature-induced Glycolytic Flux Increase inSaccharomyces cerevisiaeReveals Dominant Metabolic Regulation

2008 ◽  
Vol 283 (35) ◽  
pp. 23524-23532 ◽  
Author(s):  
Jarne Postmus ◽  
André B. Canelas ◽  
Jildau Bouwman ◽  
Barbara M. Bakker ◽  
Walter van Gulik ◽  
...  
2012 ◽  
Vol 12 (5) ◽  
pp. 571-581 ◽  
Author(s):  
Jarne Postmus ◽  
Ronald Aardema ◽  
Leo J. Koning ◽  
Chris G. Koster ◽  
Stanley Brul ◽  
...  

Metabolites ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 346
Author(s):  
Adrian Benito ◽  
Nabil Hajji ◽  
Kevin O’Neill ◽  
Hector C. Keun ◽  
Nelofer Syed

Metabolic regulation of immune cells has arisen as a critical set of processes required for appropriate response to immunological signals. While our knowledge in this area has rapidly expanded in leukocytes, much less is known about the metabolic regulation of brain-resident microglia. In particular, the role of alternative nutrients to glucose remains poorly understood. Here, we use stable-isotope (13C) tracing strategies and metabolomics to characterize the oxidative metabolism of β-hydroxybutyrate (BHB) in human (HMC3) and murine (BV2) microglia cells and the interplay with glucose in resting and LPS-activated BV2 cells. We found that BHB is imported and oxidised in the TCA cycle in both cell lines with a subsequent increase in the cytosolic NADH:NAD+ ratio. In BV2 cells, stimulation with LPS upregulated the glycolytic flux, increased the cytosolic NADH:NAD+ ratio and promoted the accumulation of the glycolytic intermediate dihydroxyacetone phosphate (DHAP). The addition of BHB enhanced LPS-induced accumulation of DHAP and promoted glucose-derived lactate export. BHB also synergistically increased LPS-induced accumulation of succinate and other key immunometabolites, such as α-ketoglutarate and fumarate generated by the TCA cycle. Finally, BHB upregulated the expression of a key pro-inflammatory (M1 polarisation) marker gene, NOS2, in BV2 cells activated with LPS. In conclusion, we identify BHB as a potentially immunomodulatory metabolic substrate for microglia that promotes metabolic reprogramming during pro-inflammatory response.


2018 ◽  
Vol 33 (7) ◽  
pp. 1184-1195 ◽  
Author(s):  
Jianhong Yang ◽  
Xiaomeng Li ◽  
Huili Lu ◽  
Jinwu Xu ◽  
Haixia Li

Information learnt from spectra at room temperature is transferred to assist in building a better regression model at high temperature.


2008 ◽  
Vol 452 (2) ◽  
pp. 446-450 ◽  
Author(s):  
Qiuguo Xiao ◽  
Ling Huang ◽  
Hui Ma ◽  
Xinhua Zhao

2002 ◽  
Vol 30 (2) ◽  
pp. 264-270 ◽  
Author(s):  
G. Wegener ◽  
U. Krause

Glycolytic flux in white muscle can be increased several-hundredfold by exercise. Phosphofructokinase (PFK; EC 2.7.1.11) is a key regulatory enzyme of glycolysis, but how its activity in muscle is controlled is not fully understood. In order not to neglect integrative aspects of metabolic regulation, we have studied in frogs (Rana temporaria) a physiological form of muscle work (swimming) that can be triggered like a reflex. We analysed swimming to fatigue in well rested frogs, recovery from exercise, and repeated exercise after 2 h of recovery. At various times, gastrocnemius muscles were tested for glycolytic intermediates and effectors of PFK. All metabolites responded similarly to the two periods of exercise, with the notable exception of fructose 2,6-bisphosphate (F2,6P2), which we proved to be a most potent activator of frog muscle PFK. The first bout of exercise triggered a more than 10-fold increase in F2,6P2; PFK activity and the content of F2,6P2 in muscle were well correlated. F2,6P2 decreased to pre-exercise levels in fatigued frogs and it virtually disappeared during recovery. Varying by a factor of 70, F2,6P2 was the most dynamic of all metabolites in muscle. Even more surprisingly, F2,6P2 did not respond at all to a second bout of exercise. Other activators of PFK, such as Pi, AMP and ADP, are increased as a consequence of increased ATP turnover in contracting muscle cells. This does not apply to F2,6P2, which is likely to respond to extracellular signals and could be involved in mechanisms by which muscle metabolism is integrated into the metabolism of the whole body. Whether this phenomenon exists in vertebrates other than the frog, and maybe even in humans, and how the content of F2,6P2 in muscle is controlled are intriguing open questions.


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