Hormonal influences on tryptophan binding to rat hepatic nuclei

Adv Exp Med Biol. 1999:467:369-78. doi: 10.1007/978-1-4615-4709-9_47.

Abstract

We evaluated whether selected hormones, 3,5,3'-triiodothyronine (T3), hydrocortisone (HC) or insulin, would influence the binding (saturable, stereospecific, and of high affinity) of L-tryptophan to rat hepatic nuclei or nuclear envelopes. T3 (10(-14) to 10(-10) M) appreciably inhibited in vitro L-(5-3H) tryptophan binding to hepatic nuclei and T3 (10(-16) to 10(-4) M) appreciably ameliorated the inhibitory effect of unlabeled tryptophan (10(-4) M) on such binding. In vivo tryptophan administration (1 h) stimulated hepatic protein synthesis but the addition of T3 negated such stimulation. HC (10(-12) to 10(-4) M) did not affect and insulin (10(-16) to 10(-4) M) had only a small inhibitory effect on 3H-tryptophan binding to hepatic nuclei, but each (10(-12) to 10(-4) M) when added to unlabeled tryptophan (10(-4) M) diminished the inhibitory binding effect of unlabeled tryptophan alone. Thus, T3 competes with tryptophan for hepatic nuclear tryptophan binding and also negates tryptophan's stimulatory effect on hepatic protein synthesis.

MeSH terms

  • Animals
  • Binding Sites
  • Binding, Competitive
  • Cell Nucleus / drug effects
  • Cell Nucleus / metabolism*
  • Hormones / pharmacology*
  • Hydrocortisone / pharmacology
  • Insulin / pharmacology
  • Kinetics
  • Liver / metabolism*
  • Nuclear Envelope / drug effects
  • Nuclear Envelope / metabolism*
  • Rats
  • Triiodothyronine / pharmacology
  • Tryptophan / metabolism*

Substances

  • Hormones
  • Insulin
  • Triiodothyronine
  • Tryptophan
  • Hydrocortisone