Different transcription regulation routes are exerted by L- and D-amino acid enantiomers of peptide hormones

Abstract

Abstract Conversion of one or more amino acids in eukaryotic peptides to the D-configuration is catalyzed by specific L/D peptide isomerases and it is a poorly investigated post-translational modification. No common modified amino acid and no specific modified position have been recognized and mechanisms underlying changes in the peptide function provided by this conversion were not sufficiently studied. The 72 amino acid crustacean hyperglycemic hormone (CHH) of Astacidea crustaceans exhibits a co-existence of two peptide enantiomers alternately having D- or L-phenylalanine in their third position. It is a pleiotropic hormone regulating several physiological processes in different target tissues and along different time scales. CHH enantiomers differently affect time courses and intensities of examined processes. The short-term effects of the two isomers on gene expression are presented here, examined in the hepatopancreas, gills, hemocytes and muscles of the astacid Pontastacus leptodactylus. Muscles and hemocytes were poorly affected by both isomers. Two CHH modes of action were elucidated in the hepatopancreas and the gills: specific gene induction by D-CHH only, elucidated in both organs and mutual targeted attenuation affected by both enantiomers elucidated in the gills. Consequently a two-receptor system is hypothesized for conveying the effect of the two CHH isomers.