RT Journal Article SR Electronic T1 Different transcription regulation routes are exerted by l- and d-amino acid enantiomers of peptide hormones JF The Journal of Experimental Biology JO J. Exp. Biol. FD The Company of Biologists Ltd SP 4337 OP 4346 DO 10.1242/jeb.109140 VO 217 IS 24 A1 Tom, Moshe A1 Manfrin, Chiara A1 Mosco, Alessandro A1 Gerdol, Marco A1 De Moro, Gianluca A1 Pallavicini, Alberto A1 Giulianini, Piero Giulio YR 2014 UL http://jeb.biologists.org/content/217/24/4337.abstract AB Conversion of one or more amino acids in eukaryotic peptides to the d-enantiomer configuration is catalyzed by specific l/d-peptide isomerases and it is a poorly investigated post-translational modification. No common modified amino acid or specific modified position has been recognized, and mechanisms underlying changes in the peptide function provided by this conversion are not widely studied. The 72 amino acid crustacean hyperglycemic hormone (CHH) in Astacidea crustaceans exhibits a co-existence of two peptide enantiomers with either d- or l-phenylalanine as their third residue. 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 were examined in the hepatopancreas, gills, hemocytes and muscles of the astacid Pontastacus leptodactylus. Gene expression in muscles and hemocytes was not affected by either of the isomers. Two modes of action for CHH were elucidated in the hepatopancreas and the gills: specific gene induction in both organs by d-CHH, and targeted attenuation caused by both enantiomers in the gills. Consequently, a two-receptor system is proposed for conveying the effect of the two CHH isomers.