Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-4-12
pubmed:abstractText
Glutamine synthetase (GS) is the only enzyme that can synthesize glutamine, but it also functions to detoxify glutamate and ammonia. Organs with high cellular concentrations of GS appear to function primarily to remove glutamate or ammonia, whereas those with a low cellular concentration appear to primarily produce glutamine. To validate this apparent dichotomy and to clarify its regulation, we determined the GS concentrations in 18 organs of the mouse. There was a >100-fold difference in GS mRNA, protein, and enzyme-activity levels among organs, whereas there was only a 20-fold difference in the GS protein:mRNA ratio, suggesting extensive transcriptional and posttranscriptional regulation. In contrast, only small differences in the GS enzyme activity : protein ratio were found, indicating that posttranslational regulation is of minor importance. The cellular concentration of GS was determined by relating the relative differences in cellular GS concentration, detected using image analysis of immunohistochemically stained tissue sections, to the biochemical data. There was a >1000-fold difference in cellular concentrations of GS between GS-positive cells in different organs, and cellular concentrations were up to 20x higher in subpopulations of cells within organs than in whole organs. GS activity was highest in pericentral hepatocytes (approximately 485 micromol.g(-1).min-(1), followed in descending order by epithelial cells in the epididymal head, Leydig cells in the testicular interstitium, epithelial cells of the uterine tube, acid-producing parietal cells in the stomach, epithelial cells of the S3 segment of the proximal convoluted tubule of the kidney, astrocytes of the central nervous tissue, and adipose tissue. GS activity in muscle amounted to only 0.4 micromol.g(-1).min(-1). Our findings confirmed the postulated dichotomy between cellular concentration and GS function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0829-8211
pubmed:author
pubmed:issnType
Print
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
215-31
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16609703-Adipose Tissue, pubmed-meshheading:16609703-Animals, pubmed-meshheading:16609703-Base Sequence, pubmed-meshheading:16609703-Epididymis, pubmed-meshheading:16609703-Female, pubmed-meshheading:16609703-Glutamate-Ammonia Ligase, pubmed-meshheading:16609703-Immunohistochemistry, pubmed-meshheading:16609703-Intestines, pubmed-meshheading:16609703-Kidney, pubmed-meshheading:16609703-Liver, pubmed-meshheading:16609703-Male, pubmed-meshheading:16609703-Mice, pubmed-meshheading:16609703-Organ Specificity, pubmed-meshheading:16609703-RNA, Messenger, pubmed-meshheading:16609703-RNA Processing, Post-Transcriptional, pubmed-meshheading:16609703-Stomach, pubmed-meshheading:16609703-Testis, pubmed-meshheading:16609703-Transcription, Genetic, pubmed-meshheading:16609703-Uterus
pubmed:year
2006
pubmed:articleTitle
Cellular concentrations of glutamine synthetase in murine organs.
pubmed:affiliation
Department of Anatomy and Embryology, University of Maastricht, Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't