Imprinting effects of three amino acids (alanine, lysine and glycine) and their oligopeptides in Tetrahymena pyriformis. Data from the hormone and hormone receptor evolution.
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.
Csaba
G
G
Department of Biology, Semmelweis University of Medicine, Budapest, Hungary.
Kovács
P
P
Noszál
B
B
D000409:Alanine / Q000494:pharmacology; D000596:Amino Acids / Q000494:pharmacology*; D000818:Animals; D005075:Biological Evolution; D016650:Fluorescein-5-isothiocyanate; D005456:Fluorescent Dyes; D005998:Glycine / Q000494:pharmacology; D006728:Hormones / Q000502:physiology*; D008239:Lysine / Q000494:pharmacology; D009842:Oligopeptides / Q000494:pharmacology*; D011956:Receptors, Cell Surface / Q000502:physiology*; D013769:Tetrahymena pyriformis / Q000187:drug effects*
D000596:Amino Acids; D005456:Fluorescent Dyes; D006728:Hormones; D009842:Oligopeptides; D011956:Receptors, Cell Surface; D016650:Fluorescein-5-isothiocyanate; D008239:Lysine; D000409:Alanine; D005998:Glycine