These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Metabolism of [U-13C]glutamine and [U-13C]glutamate in isolated rat brain mitochondria suggests functional phosphate-activated glutaminase activity in matrix.
    Author: Bak LK, Ziemińska E, Waagepetersen HS, Schousboe A, Albrecht J.
    Journal: Neurochem Res; 2008 Feb; 33(2):273-8. PubMed ID: 17763943.
    Abstract:
    One of the forms of phosphate activated glutaminase (PAG) is associated with the inner mitochondrial membrane. It has been debated whether glutamate formed from glutamine in the reaction catalyzed by PAG has direct access to mitochondrial or cytosolic metabolism. In this study, metabolism of [U-(13)C]glutamine (3 mM) or [U-(13)C]glutamate (10 mM) was investigated in isolated rat brain mitochondria. The presence of a functional tricarboxylic (TCA) cycle in the mitochondria was tested using [U-(13)C]succinate as substrate and extensive labeling in aspartate was seen. Accumulation of glutamine into the mitochondrial matrix was inhibited by histidine (15 mM). Extracts of mitochondria were analyzed for labeling in glutamine, glutamate and aspartate using liquid chromatography-mass spectrometry. Formation of [U-(13)C]glutamate from exogenous [U-(13)C]glutamine was decreased about 50% (P<0.001) in the presence of histidine. In addition, the (13)C-labeled skeleton of [U-(13)C]glutamine was metabolized more vividly in the tricarboxylic acid (TCA) cycle than that from [U-(13)C]glutamate, even though glutamate was labeled to a higher extent in the latter condition. Collectively the results show that transport of glutamine into the mitochondrial matrix may be a prerequisite for deamidation by PAG.
    [Abstract] [Full Text] [Related] [New Search]