Glutamine Synthetase, also called glutamate-ammonia ligase (GLUL), is expressed throughout the body and plays an important role in controlling body pH and in removing ammonia from the circulation. The enzyme clears L-glutamate, the major neurotransmitter in the central nervous system, from neuronal synapses.
Images: Localization of glutamine synthase in the retina. Paraffin sections of mouse (A, B), rat (C, D, G-I), or human (E, F) retina fixed in 4% paraformaldehyde were reacted with anti-glutamine synthase (red fluorescence staining in B, D, G, I, and brown immuno-peroxidase reaction [using ABC kit and visualization with DAB product in F]. Nuclei in some immunofluorescence experiments (A-D) were stained with DAPI (shown in cyan), and with nuclear fast red in E and F. On inspection at low magnification, anti- glutamine synthase reacted with a single population of cells extending from the ganglion cell layer (GCL) through the inner nuclear layer (INL). No signal was detected in controls either pre-incubated with 100ug/ml of the immunizing peptide (A) or with pre-immune serum (C, E). The pattern of staining observed in all experiments is typical of Müller cells. This finding was confirmed by co-localization (indicated by yellow in I) of glutamine synthase (red in G) with antoher marker of glutamine synthase (green in H).
Its activity is decreased in the cerebral cortex of brains affected by Alzheimer's disease, particularly in the vicinity of senile plaques. It is also decreased under conditions of glucose deprivation. The level of expression of Glutamine Synthetase is increased during ischemia in vivo or hypoxia in culture.
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