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Comparison of Effects of L-Tryptophan and a Tryptophan Analog, D,L-ß-(1-Naphthyl)alanine, on Processes Relating to Hepatic Protein Synthesis in Rats¹

Department of Pathology, The George Washington University Medical Center, Washington, D.C. 20037

Earlier studies reported that the administration of L-tryptophan increased polyribosomal aggregation, protein synthesis and levels of cytoplasmic poly(A)mRNA in rat liver. This study was concerned with the effects of an L-tryptophan analog, D,L-ß-(1-naphthyl)alanine, in comparison with those of L-tryptophan. Both D,L-ß-(1-naphthyl)alanine and L-tryptophan bound to the L-tryptophan receptor protein and increased poly(A)polymerase and nucleoside triphosphatase activities of hepatic nuclei. However, only L-tryptophan was associated with increases in the release of labeled nuclear RNA (in vitro), in protein synthesis, in polyribosomal aggregation and in glycosylation ([¹⁴C]glucosamine incorporation into proteins) of rat liver. These results indicate that although D,L-ß-(1-naphyl)alanine affected hepatic nuclei (binding and enzyme levels), it did not stimulate nucleocytoplasmic translocation of mRNA and concomitant protein synthesis, as did L-tryptophan.

KEY WORDS: • L-tryptophan • D,L-ß-(1-naphthyl)alanine • tryptophan receptor protein • poly(A)polymerase • hepatic protein synthesis • rats

¹ This research was supported by U.S. Public Health Service Grant DK-27339 from the National Institute of Arthritis, Diabetes, and Digestive and Kidney Diseases.

Manuscript received 13 December 1989. Revision accepted 12 March 1990.

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