Arginine-enriched solution induces a marked increase in muscle glutamine concentration and enhances muscle protein synthesis in tumor-bearing rats.

Abstract

Using a transplantable Yoshida sarcoma in a rat model of total parenteral nutrition (TPN), we measured the effectiveness of an arginine-enriched amino acid solution (AI-82) on muscle glutamine concentration and muscle protein synthesis compared with that of a conventional amino acid solution (Proteamin12). After tumor-bearing rats had been given one of two isocaloric TPN regimens for 6 days, [15N]glycine (99 atom %) containing TPN solution was infused into animals at a constant rate of 8 mg of [15N]glycine per hour for 18 hours, after which the liver, skeletal muscle (gastrocnemius muscle), and tumor protein synthesis rates were measured. A significantly increased whole muscle protein synthesis rate was observed in the AI-82 group; there was no difference in the whole liver and tumor protein synthesis rates between the two groups. When each TPN solution was administered for 1 week, muscle concentrations of arginine, ornithine, glutamine, and glutamate were considerably higher in the AI-82 group than in the Proteamin12 group, and these differences were also accompanied by a decrease in the plasma branched-chain amino acid (BCAA) (leucine, isoleucine, and valine) levels in the AI-82 group. The high levels of muscle glutamine concentration in the AI-82 group were investigated in connection with the high use of exogenous branched-chain amino acids.