Effect of glutamine and chemotherapy on protein metabolism in tumor-bearing rats. 1994

A Kaibara, and S Yoshida, and K Yamasaki, and N Ishibashi, and T Kakegawa
1st Department of Surgery, School of Medicine, Kurume University, Fukuoko, Japan.

Supplemental glutamine prevents gut atrophy and enhances muscle protein synthesis in septic rats. This study investigated the effect of glutamine administration and mitomycin C treatment on protein turnover in tumor-bearing rats. AH109A rat ascites hepatoma cells (2 x 10(6)) were subcutaneously implanted in the back of male Donryu rats (n = 32, body weight 150-200 g) on Day 0. The animals were then fed rat chow ad libitum for 10 days. On Day 10, the rats were catheterized for TPN and randomized into four groups according to diet and treatment. The groups were: (i) standard total parenteral nutrition (STPN) + saline; (ii) glutamine-supplemented TPN (GTPN) + saline; (iii) STPN+mitomycin C (MMC); (iv) GTPN+MMC. GTPN was isocaloric (250 kcal/kg/day) and isonitrogenous (1.5 gN/kg/day) with STPN. The animals were maintained on TPN for 5 days and received mitomycin C (0.5 mg/kg) via the catheter every day. On the fifth day of TPN, [1-14C]leucine was given via a 5-hr continuous infusion (2.0 microCi/hr/rat) to determine the fractional synthesis rate of muscle, gut mucosa, liver, and tumor. Also, endogenous leucine production (not equal to whole body protein breakdown rate) was calculated. Body weight loss during TPN was reduced with GTPN. GTPN enhanced muscle FSR in untreated animals (STPN: 10.8 +/- 8.7%/day vs GTPN: 14.7 +/- 0.6%/day, P < 0.05) and in mitomycin C-treated animals (STPN+MMC: 9.6 +/- 0.9%/day, GTPN+MMC: 12.0 +/- 0.8%/day, P < 0.05). The whole body protein breakdown rate was reduced with GTPN. Mitomycin C reduced the mucosal fractional synthesis rate and GTPN did not prevent this reduction.(ABSTRACT TRUNCATED AT 250 WORDS)

UI MeSH Term Description Entries
D007413 Intestinal Mucosa Lining of the INTESTINES, consisting of an inner EPITHELIUM, a middle LAMINA PROPRIA, and an outer MUSCULARIS MUCOSAE. In the SMALL INTESTINE, the mucosa is characterized by a series of folds and abundance of absorptive cells (ENTEROCYTES) with MICROVILLI. Intestinal Epithelium,Intestinal Glands,Epithelium, Intestinal,Gland, Intestinal,Glands, Intestinal,Intestinal Gland,Mucosa, Intestinal
D007930 Leucine An essential branched-chain amino acid important for hemoglobin formation. L-Leucine,Leucine, L-Isomer,L-Isomer Leucine,Leucine, L Isomer
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008114 Liver Neoplasms, Experimental Experimentally induced tumors of the LIVER. Hepatoma, Experimental,Hepatoma, Morris,Hepatoma, Novikoff,Experimental Hepatoma,Experimental Hepatomas,Experimental Liver Neoplasms,Hepatomas, Experimental,Neoplasms, Experimental Liver,Experimental Liver Neoplasm,Liver Neoplasm, Experimental,Morris Hepatoma,Novikoff Hepatoma
D008297 Male Males
D009132 Muscles Contractile tissue that produces movement in animals. Muscle Tissue,Muscle,Muscle Tissues,Tissue, Muscle,Tissues, Muscle
D009363 Neoplasm Proteins Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm. Proteins, Neoplasm
D010289 Parenteral Nutrition, Total The delivery of nutrients for assimilation and utilization by a patient whose sole source of nutrients is via solutions administered intravenously, subcutaneously, or by some other non-alimentary route. The basic components of TPN solutions are protein hydrolysates or free amino acid mixtures, monosaccharides, and electrolytes. Components are selected for their ability to reverse catabolism, promote anabolism, and build structural proteins. Hyperalimentation, Parenteral,Intravenous Hyperalimentation,Nutrition, Total Parenteral,Parenteral Hyperalimentation,Total Parenteral Nutrition,Hyperalimentation, Intravenous
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D011919 Rats, Inbred Strains Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding. August Rats,Inbred Rat Strains,Inbred Strain of Rat,Inbred Strain of Rats,Inbred Strains of Rats,Rat, Inbred Strain,August Rat,Inbred Rat Strain,Inbred Strain Rat,Inbred Strain Rats,Inbred Strains Rat,Inbred Strains Rats,Rat Inbred Strain,Rat Inbred Strains,Rat Strain, Inbred,Rat Strains, Inbred,Rat, August,Rat, Inbred Strains,Rats Inbred Strain,Rats Inbred Strains,Rats, August,Rats, Inbred Strain,Strain Rat, Inbred,Strain Rats, Inbred,Strain, Inbred Rat,Strains, Inbred Rat

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