Different transcription regulation routes are exerted by L- and D-amino acid enantiomers of peptide hormones.
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.
Israel Oceanographic and Limnological Research, P.O.B. 8030, Haifa 31080, Israel. tom@ocean.org.il.
Moshe
M
Tom
Department of Life Sciences, University of Trieste, Via Licio Giorgieri 5, Trieste, 34127, Italy.
Chiara
C
Manfrin
Department of Life Sciences, University of Trieste, Via Licio Giorgieri 5, Trieste, 34127, Italy.
Alessandro
A
Mosco
Department of Life Sciences, University of Trieste, Via Licio Giorgieri 5, Trieste, 34127, Italy.
Marco
M
Gerdol
Department of Life Sciences, University of Trieste, Via Licio Giorgieri 5, Trieste, 34127, Italy.
Gianluca
G
De Moro
Department of Life Sciences, University of Trieste, Via Licio Giorgieri 5, Trieste, 34127, Italy.
Alberto
A
Pallavicini
Department of Life Sciences, University of Trieste, Via Licio Giorgieri 5, Trieste, 34127, Italy.
Piero Giulio
PG
Giulianini
D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D060829:Arthropod Proteins / Q000235:genetics* / Q000378:metabolism; D003400:Astacoidea / Q000235:genetics / Q000502:physiology*; D005260:Female; D015870:Gene Expression / Q000502:physiology*; D005880:Gills / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D006434:Hemocytes / Q000378:metabolism; D043143:Hepatopancreas / Q000378:metabolism; D007447:Invertebrate Hormones / Q000235:genetics* / Q000378:metabolism; D007536:Isomerism; D008969:Molecular Sequence Data; D009132:Muscles / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000235:genetics* / Q000378:metabolism; D010455:Peptides / Q000494:pharmacology; D020033:Protein Isoforms / Q000235:genetics; D011499:Protein Processing, Post-Translational / Q000235:genetics*; D017423:Sequence Analysis, RNA
D000596:Amino Acids; D060829:Arthropod Proteins; D007447:Invertebrate Hormones; D009419:Nerve Tissue Proteins; D010455:Peptides; D020033:Protein Isoforms; C015947:hyperglycemic hormone, crustacean; D005947:Glucose
Crustacea; Crustacean hyperglycemic hormone (CHH); Digital analysis of gene expression; Pontastacus leptodactylus; Post-translational modification; d/l-peptide enantiomers