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Title: Is glutamine oxidation necessary to support intestinal functions

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6858234

Glutamine (GLN) is known to be a major oxidative substrate in the small intestine, but the role of GLN oxidation in the support of the critical intestinal functions of nutrient absorption and DNA synthesis is not known. In the presence and absence of GLN, rates of active transport of 3-O-methylglucose (MG) and histidine(HIS) were determined in everted sacs of rat jejunum. 10 mM MG was absorbed at equivalent rates when incubated with 10 mM GLN, 10 mM B-hydroxybutyrate (BHB) or Krebs Ringer phosphate with no added substrate. Absorption of HIS was also independent of the presence of GLN as an oxidative substrate. The dependence of DNA synthesis on GLN oxidation was determined by measuring /sup 3/H-methyl-thymidine (/sup 3/HTdR) incorporation in isolated crypt cells incubated in Media 199 which includes purines and pyrimidines to support DNA synthesis, but no GLN. The addition of 10 mM GLN to crypt cells from rats refed after a fast resulted in a 57% increase (p<0.03) in /sup 3/HTdR incorporation compared to cells with no added substrates. When either 20 mM aminooxyacetate, an inhibitor of GLN oxidation, or 0.2 mM BHB were added with the GLN, rates of /sup 3/HTdR incorporation decreased to basal values. These studies demonstrate that the jejunum can support short term active transport from endogenous fuel supplies other than GLN. However, elevated rates of /sup 3/HTdR incorporation appear to be dependent on the oxidation of GLN by jejunal crypt cells.

Research Organization:
Univ. of California, Berkeley
OSTI ID:
6858234
Report Number(s):
CONF-8604222-; TRN: 87-010468
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 45:4; Conference: 70. annual meeting of the Federation of American Society for Experimental Biology, St. Louis, MO, USA, 13 Apr 1986
Country of Publication:
United States
Language:
English