ArticleNeurochemical research2010
Kinetics of a novel isoform of phosphate activated glutaminase (PAG) in SH-SY5Y neuroblastoma cells.
Article in Neurochemical research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Glutamate‑mediated effects of caffeine and interferon‑γ on mercury-induced toxicity.International journal of molecular medicine · 2017Article
- Fatty acid biosynthesis from glutamate and glutamine is specifically induced in neuronal cells under hypoxia.Journal of neurochemistry · 2014Article
- THDP17 decreases ammonia production through glutaminase inhibition. A new drug for hepatic encephalopathy therapy.PloS one · 2014Article
- Analysis of glutamine dependency in non-small cell lung cancer: GLS1 splice variant GAC is essential for cancer cell growth.Cancer biology & therapy · 2012Article
- The unipolar brush cell: a remarkable neuron finally receiving deserved attention.Brain research reviews · 2011Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have recently found that the neuroblastoma cell line SH-SY5Y expresses a novel form of phosphate activated glutaminase (PAG) which deamidates glutamine to glutamate and ammonia at high rates. Glutamate production is enhanced during the exponential phase of growth, and decreases when cell proliferation stops. Neuroblastoma PAG exists in a soluble and membrane associated form, and both the phosphate and the glutamine kinetics, as well as the effects of ammonia and glutamate are different from those of the known forms of PAG. Neuroblastoma PAG is mitochondrial, and our immunoblotting analyses of isolated mitochondria shows that our C-terminal antibody reacts with a protein of 65 kDa, while our N-terminal antibody primarily labels a protein of 58 kDa and to a minor degree one of 65 kDa. This strongly suggests that neuroblastoma cells mainly contain an active isoform of PAG lacking the C-terminal end, probably the GAC form.
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