Glutamate-anaplerotic pathway control state: Difference between revisions
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{{MitoPedia | {{MitoPedia | ||
|abbr=G | |abbr=G | ||
|description='''G''': [[Glutamate]] as the sole fuel substrate is transported by the electroneutral glutamate-/OH- exchanger, and is oxidised via glutamate dehydrogenase in the mitochondrial matrix. | |description=[[File:G.jpg|left|200px|G]] '''G''': [[Glutamate]] as the sole fuel substrate is transported by the electroneutral glutamate-/OH- exchanger, and is oxidised via glutamate dehydrogenase in the mitochondrial matrix. | ||
|info=Gnaiger 2014 MitoPathways - Chapter 3.3 | |info=Gnaiger 2014 MitoPathways - Chapter 3.3 | ||
}} | }} | ||
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== Details == | == Details == | ||
In human skeletal muscle mitochondria, [[OXPHOS]] capacity with glutamate alone is 50% to 85% of respiration with [[Glutamate&Malate]]. Accumulation of fumarate inhibits succinate dehydrogenase and glutamate dehydrogenase. | :::: In human skeletal muscle mitochondria, [[OXPHOS]] capacity with glutamate alone is 50% to 85% of respiration with [[Glutamate&Malate]]. Accumulation of fumarate inhibits succinate dehydrogenase and glutamate dehydrogenase. | ||
Glutamate derived from hydrolyzation of glutamine is an important aerobic substrate in cultured cells. Mitochondrial glutamate dehydrogenase is particularly active in astrocytes, preventing glutamate induced neurotoxicity. mtNAD-malic enzyme supports an anaplerotic pathway when carbohydrate is limiting. | |||
:::: Glutamate derived from hydrolyzation of glutamine is an important aerobic substrate in cultured cells. Mitochondrial glutamate dehydrogenase is particularly active in astrocytes, preventing glutamate induced neurotoxicity. mtNAD-malic enzyme supports an anaplerotic pathway when carbohydrate is limiting. |
Revision as of 19:00, 25 February 2016
- high-resolution terminology - matching measurements at high-resolution
Glutamate-anaplerotic pathway control state
Description
G: Glutamate as the sole fuel substrate is transported by the electroneutral glutamate-/OH- exchanger, and is oxidised via glutamate dehydrogenase in the mitochondrial matrix.
Abbreviation: G
Reference: Gnaiger 2014 MitoPathways - Chapter 3.3
MitoPedia O2k and high-resolution respirometry: "SUIT state" is not in the list (O2k hardware, DatLab, Oroboros QM, O2k-Open Support, O2k-Respirometry, O2k-FluoRespirometry) of allowed values for the "MitoPedia O2k and high-resolution respirometry" property.
SUIT state"SUIT state" is not in the list (O2k hardware, DatLab, Oroboros QM, O2k-Open Support, O2k-Respirometry, O2k-FluoRespirometry) of allowed values for the "MitoPedia O2k and high-resolution respirometry" property.
G(L)
G(P)
G(E)
Details
- In human skeletal muscle mitochondria, OXPHOS capacity with glutamate alone is 50% to 85% of respiration with Glutamate&Malate. Accumulation of fumarate inhibits succinate dehydrogenase and glutamate dehydrogenase.
- Glutamate derived from hydrolyzation of glutamine is an important aerobic substrate in cultured cells. Mitochondrial glutamate dehydrogenase is particularly active in astrocytes, preventing glutamate induced neurotoxicity. mtNAD-malic enzyme supports an anaplerotic pathway when carbohydrate is limiting.