High impact information on GLUL

• However, there was no apparent significant difference between the two cell lines in the pattern of changes of GS activity in response to glutamine [1].
• The glutamine synthetase (GS) activity of both cell lines was elevated (up to x 9) as glutamine was depleted from normal media (GMEM + gmine) [1].
• The high activity of GS was maintained during McCoy cell growth in GMEM + gmate [1].
• In the human and mouse GS genes, extra exons are also found at the corresponding site of the intron 1 but with different sizes [2].
• An exon-trapping experiment for the GS gene in COS-7, Madin-Darby canine kidney and SK-N-SH cells revealed that the pattern of alternative splicing is variable in different cell types [2].

Biological context of GLUL

• The genomic structure of dog GS shown in the present study is basically similar to that of other mammals in that it is composed of seven exons and six introns [2].

Anatomical context of GLUL

• Ammonia is detoxified in the astrocyte (glutamine synthetase) by incorporating it into glutamine, a process that requires large amounts of glucose and ATP [3].
• GS was inhibited centrally by perfusing the ventriculocisternal space with artificial cerebrospinal fluid (CSF) containing 92.5 mmol MSO per liter at a fixed pH, perfusion rate, and pressure [4].
• Immunohistochemically, a decrease of immunostains for glutamine synthetase and glutamate transporter antibodies was seen in Alzheimer type II astrocytes and neuropil [5].
• The alterations in intracellular and circulating levels of glutamine were not accompanied by measurable changes in glutamine synthetase or glutaminase activities in skeletal muscle [6].

Associations of GLUL with chemical compounds

• The expression of glutamine synthetase (GS), catalysing the ATP-dependent conversion of glutamate and ammonia into glutamine, is transcriptionally and post-transcriptionally regulated [2].
• Uptake of glutamate, not glutamine synthetase, regulates adaptation of mammalian cells to glutamine-free medium [1].

References