Imprinting effects of three amino acids (alanine, lysine and glycine) and their oligopeptides in Tetrahymena pyriformis. Data from the hormone and hormone receptor evolution

György Csaba, Péter Kovács, Béla Noszál

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3 Citations (Scopus)


Hormonal imprinting takes place at the first encounter of the hormone and receptor, and results in a changed binding capacity and reaction of the cell and its progeny generations. The imprinting effect of three amino acids and their oligopeptides is studied using fluorescent-labelled peptides. Glycine and lysine could provoke positive imprinting (increased binding in the progeny generations) for their own peptides, but alanine could not. Mostly positive imprinting was provoked by glycine and lysine peptides for their own peptides of different chain length. The optimal chain length provoking self-imprinting was four for glycine, two for lysine and three for alanine. Except in this case, alanine was neutral or provoked mostly negative imprinting. After reaching the optimal chain length, there is a decline in binding. Evolutionary conclusions are discussed.

Original languageEnglish
Pages (from-to)339-342
Number of pages4
JournalCell biology international
Issue number5
Publication statusPublished - May 1996



  • Hormonal imprinting
  • Hormone evolution
  • Oligopeptides
  • Receptor evolution
  • Tetrahymena

ASJC Scopus subject areas

  • Cell Biology

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