Evidence for a conformational polymorphism of invertebrate neurohormones. D-amino acid residue in crustacean hyperglycemic peptides

• Published in: The Journal of biological chemistry 1994-07, Vol.269 (28), p.18295-18298
• Main Authors: SOYEZ, D, VAN HERP, F, ROSSIER, J, LE CAER, J.-P, TENSEN, C. P, LAFONT, R
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Arthropod Proteins; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; Invertebrate Hormones - chemistry; Invertebrate Hormones - isolation & purification; Mass Spectrometry; Molecular Sequence Data; Nephropidae - chemistry; Nerve Tissue Proteins - chemistry; Nerve Tissue Proteins - isolation & purification; Oligopeptides - chemical synthesis; Oligopeptides - chemistry; Peptide Fragments - chemistry; Peptide Fragments - isolation & purification; Polymorphism, Genetic; Protein Conformation; Protein hormones. Growth factors. Cytokines; Proteins; Sebaceous Glands - chemistry; Sequence Homology, Amino Acid
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(17)32303-7

Several large peptidic neurohormones have been isolated in crustaceans. In lobster and other related species, each of these neurohormones, and particularly the crustacean hyperglycemic hormone, occurs as two isoforms having the same peptidic sequence and molecular mass. We report here that these isoforms differ by the configuration of a single amino acid residue. The third residue (Phe3) of the lobster hyperglycemic hormones is in either the L- or D-configuration. In addition, we have shown that the biological activity of the two isoforms differs when considering the kinetics of their hyperglycemic effect.