Novel Form of Phosphate Activated Glutaminase in Cultured Astrocytes and Human Neuroblastoma Cells, PAG in Brain Pathology and Localization in the Mitochondria

• Published in: Neurochemical research Vol. 33; no. 7; pp. 1341 - 1345
• Main Authors: Kvamme, E., Nissen-Meyer, L. S. H., Roberg, B. Å., Torgner, I. Aa
• Format: Journal Article
• Language: English
• Published: Boston Springer US 01-07-2008; Springer Nature B.V
• Subjects: Astrocytes - enzymology; Biochemistry; Biomedical and Life Sciences; Biomedicine; Brain - enzymology; Brain - pathology; Brain Neoplasms - enzymology; Cell Biology; Cell Line, Tumor; Cells, Cultured; Glutaminase - chemistry; Glutaminase - metabolism; Humans; Immunohistochemistry; Mitochondria - enzymology; Mitochondria - pathology; Mitochondrial Membranes - enzymology; Neuroblastoma - enzymology; Neurochemistry; Neurology; Neurosciences; Original Paper; Submitochondrial localization; Phosphate activated glutaminase; Brain pathology; Astrocytes; Brain glutaminase; Neuroblastoma cells
• ISSN: 0364-3190; 1573-6903
• DOI: 10.1007/s11064-008-9589-9

A novel form of phosphate activated glutaminase (PAG), catalyzing the synthesis of glutamate from glutamine, has been detected in cultured astrocytes and SH-SY5Y neuroblastoma cells. This enzyme form is different from that of the kidney and liver isozymes. In these cells we found high enzyme activity, but no or very weak immunoreactivity against the kidney type of PAG, and no immunoreactivity against the liver type. PAG was also investigated in brain under pathological conditions. In patients with Down’s syndrome the immunoreactivity in the frontoparietal cortex was significantly reduced. The findings leading to our conclusion of a functionally active PAG on the outer face of the inner mitochondrial membrane are discussed, and a model is presented.