GLYCOLYSIS IS A SOURCE OF PYRUVATE FOR TRANSAMINATION OF GLUTAMINE AMINO NITROGEN IN JEJUNAL EPITHELIAL-CELLS

Citation
Jd. Cremin et Se. Fleming, GLYCOLYSIS IS A SOURCE OF PYRUVATE FOR TRANSAMINATION OF GLUTAMINE AMINO NITROGEN IN JEJUNAL EPITHELIAL-CELLS, American journal of physiology: Gastrointestinal and liver physiology, 35(3), 1997, pp. 575-588
Citations number
28
Categorie Soggetti
Physiology
ISSN journal
01931857
Volume
35
Issue
3
Year of publication
1997
Pages
575 - 588
Database
ISI
SICI code
0193-1857(1997)35:3<575:GIASOP>2.0.ZU;2-C
Abstract
Previous research has shown that glucose increases transamination of g lutamine amino nitrogen with pyruvate. It is unclear whether glucose o r glutamine provides the pyruvate used for transamination. In the curr ent study, it was hypothesized that glucose provides pyruvate for tran samination of glutamine amino nitrogen. This hypothesis was tested by tracing the metabolism of [2-C-13]glucose in these cells incubated in the presence of [2-C-13]glucose or [2-C-13]glucose and glutamine using C-13 nuclear magnetic resonance. Glutamine supplementation increased alanine production but did not affect lactate production. The 1-C-13, 2-C-13, 3-C-13, 1,2-C-13, and 2,3-C-13 isotopomers of alanine and lact ate were produced when glutamine was supplemented. Glutamine supplemen tation increased production of 2-C-13, 1,2-C-13, and 2,3-C-13 isotopom ers of alanine but did not affect the production of isotopomers of lac tate. The ratio of production of [2-C-13] alanine to [3-C-13] alanine was 37:1 when glutamine was present. The predominance of production of [2-C-13]alanine vs. all other isotopomers demonstrates that a large p roportion of the pyruvate used for transamination of glutamine amino n itrogen was derived from glycolysis.