Locustatachykinin I and II, two novel insect neuropeptides with homology to peptides of the vertebrate tachykinin family

• Published in: FEBS letters Vol. 261; no. 2; pp. 397 - 401
• Main Authors: Schoofs, Liliane, Holman, G.Mark, Hayes, Timothy K., Nachman, Ronald J., De Loof, Arnold
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 26.02.1990; Elsevier
• Subjects: Acrididae; Amino Acid Sequence; Amino Acids - analysis; Aminoacids, peptides. Hormones. Neuropeptides; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Biological Assay; Brain Chemistry; Chromatography, High Pressure Liquid; Cockroaches; Fundamental and applied biological sciences. Psychology; Grasshoppers - analysis; Homology; Insect Hormones - isolation & purification; Insect Hormones - pharmacology; Insect neuropeptide; Insect Proteins; Locusta migratoria; Locustatachykinin; locustatachykinin II; Molecular Sequence Data; Muscle contraction; Muscle Contraction - drug effects; Myotropin; Neuropeptides - isolation & purification; Neuropeptides - pharmacology; Orthoptera; Proteins; Sequence Homology, Nucleic Acid; Substance P; Tachykinin; Tachykinins; Locustatachykinin; Myotropin; Insect neuropeptide; Substance P; Homology; Locusta migratoria; Tachykinin; Muscle contraction; Insecta; Orthoptera; HPLC chromatography; Neuropeptide; Acrididae; Characterization; Molecular evolution; Arthropoda; Acridoidea; Invertebrata; Comparative study
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(90)80601-E

Two myotropic peptides termed locustatachykinin I (Gly-Pro-Ser-Gly-Phe-Tyr-Gly-Val-Arg-NH 2) and locustatachykinin II (Ala-Pro-Leu-Ser-Gly-Phe-Tyr-Gly-Val-Arg-NH 2) were isolated from brain-corpora cardiaca-corpora allata-suboesophageal ganglion extracts of the locust, Locusta migratoria. Both peptides exhibit sequence homologies with the vertebrate tachykinins. Sequence homology is greater with the fish and amphibian tachykinins (up to 45%) than with the mammalian tachykinins. In addition, the intestinal myotropic activity of the locustatachykinins is analogous to that of vertebrate tachykinins. The peptides discovered in this study may just be the first in a whole series of substances from arthropod species to be identified as tachykinin family peptides. Moreover, both chemical and biological similarities of vertebrate and insect tachykinins substantiate the evidence for a long evolutionary history of the tachykinin peptide family.