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Difference between revisions of "Glutamate-anaplerotic pathway control state"

From Bioblast
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{{MitoPedia
{{MitoPedia
|abbr=G
|abbr=G
|description=[[File:G.jpg|left|200px|G]] '''G''': [[Glutamate]] is a [[ETS substrate types |NADH-linked type 4 substrate]]. When supplied as the sole fuel substrate, G is transported by the electroneutral glutamate-/OH- exchanger, and is oxidised via mt [[glutamate dehydrogenase]] in the mitochondrial matrix.
|description=[[File:G.jpg|left|200px|G]] '''G''': [[Glutamate]] is a [[ETS substrate types |NADH-linked type 4 substrate]]. When supplied as the sole fuel substrate in the '''glutamate pathway control state''', G is transported by the electroneutral glutamate-/OH- exchanger, and is oxidised via mt [[glutamate dehydrogenase]] in the mitochondrial matrix.
|info=[[Gnaiger 2014 MitoPathways]] - Chapter 3.3
|info=[[Gnaiger 2014 MitoPathways]] - Chapter 3.3
}}
}}
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|mitopedia concept=Respiratory state, SUIT state
|mitopedia concept=Respiratory state, SUIT state
}}
}}
{{MitoPedia methods}}
{{MitoPedia O2k and high-resolution respirometry}}
{{MitoPedia topics}}
== G(L) ==
== G(L) ==



Revision as of 10:08, 8 November 2016


high-resolution terminology - matching measurements at high-resolution


Glutamate-anaplerotic pathway control state

Description

G

G: Glutamate is a NADH-linked type 4 substrate. When supplied as the sole fuel substrate in the glutamate pathway control state, G is transported by the electroneutral glutamate-/OH- exchanger, and is oxidised via mt glutamate dehydrogenase in the mitochondrial matrix.

Abbreviation: G

Reference: Gnaiger 2014 MitoPathways - Chapter 3.3


MitoPedia concepts: Respiratory state, SUIT state 

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.