Biology:GLS2
 Generic protein structure example |
Glutaminase 2 (liver, mitochondrial) is a protein that in humans is encoded by the GLS2 gene.[1]
Structure
The GLS2 gene is on the 12th chromosome in humans, with its specific location being 12q13.3. It contains 19 exons.[1]
Function
GLS2 is a part of the glutaminase family. The protein encoded by this gene is a mitochondrial phosphate-activated glutaminase that catalyzes the hydrolysis of glutamine to stoichiometric amounts of glutamate and ammonia. Originally thought to be liver-specific, this protein has been found in other tissues as well. Alternative splicing results in multiple transcript variants that encode different isoforms.
Clinical significance
GLS2 has interesting molecular relationships with tumor progression and cancer. Glutaminase 2 negatively regulates the PI3K/AKT signaling and shows tumor suppression activity in human hepatocellular carcinoma.[2] Additionally, silencing of GLS and overexpression of GLS2 genes cooperate in decreasing the proliferation and viability of glioblastoma cells.[3]
References
- ↑ 1.0 1.1 "Entrez Gene: Glutaminase 2 (liver, mitochondrial)". https://www.ncbi.nlm.nih.gov/gene/27165.
- ↑ "Glutaminase 2 negatively regulates the PI3K/AKT signaling and shows tumor suppression activity in human hepatocellular carcinoma". Oncotarget 5 (9): 2635–47. May 2014. doi:10.18632/oncotarget.1862. PMID 24797434.
- ↑ "Silencing of GLS and overexpression of GLS2 genes cooperate in decreasing the proliferation and viability of glioblastoma cells". Tumour Biology 35 (3): 1855–62. Mar 2014. doi:10.1007/s13277-013-1247-4. PMID 24096582.
Further reading
- "Human metabolic individuality in biomedical and pharmaceutical research". Nature 477 (7362): 54–60. Sep 2011. doi:10.1038/nature10354. PMID 21886157. Bibcode: 2011Natur.477...54S.
- "Knock-down of glutaminase 2 expression decreases glutathione, NADH, and sensitizes cervical cancer to ionizing radiation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1833 (12): 2996–3005. Dec 2013. doi:10.1016/j.bbamcr.2013.08.003. PMID 23954443.
- "Glutaminase 2, a novel p53 target gene regulating energy metabolism and antioxidant function". Proceedings of the National Academy of Sciences of the United States of America 107 (16): 7455–60. Apr 2010. doi:10.1073/pnas.1001006107. PMID 20378837. Bibcode: 2010PNAS..107.7455H.
- "Nuclear localization of L-type glutaminase in mammalian brain". The Journal of Biological Chemistry 277 (41): 38939–44. Oct 2002. doi:10.1074/jbc.C200373200. PMID 12163477.
- "Nine loci for ocular axial length identified through genome-wide association studies, including shared loci with refractive error". American Journal of Human Genetics 93 (2): 264–77. Aug 2013. doi:10.1016/j.ajhg.2013.06.016. PMID 24144296.
- "Increased plasma glutamate by antipsychotic medication and its relationship to glutaminase 1 and 2 genotypes in schizophrenia -- Juntendo University Schizophrenia Projects (JUSP)". Progress in Neuro-Psychopharmacology & Biological Psychiatry 31 (7): 1410–8. Oct 2007. doi:10.1016/j.pnpbp.2007.06.009. PMID 17669570.
- "Genome-wide association study identifies multiple loci influencing human serum metabolite levels". Nature Genetics 44 (3): 269–76. Mar 2012. doi:10.1038/ng.1073. PMID 22286219.
- "Transfection of a human glioblastoma cell line with liver-type glutaminase (LGA) down-regulates the expression of DNA-repair gene MGMT and sensitizes the cells to alkylating agents". Journal of Neurochemistry 123 (3): 428–36. Nov 2012. doi:10.1111/j.1471-4159.2012.07917.x. PMID 22888977.
- "Co-expression of glutaminase K and L isoenzymes in human tumour cells". The Biochemical Journal 386 (Pt 3): 535–42. Mar 2005. doi:10.1042/BJ20040996. PMID 15496140.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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