Isolation, identification and synthesis of PDVDHFLRFamide (SchistoFLRFamide) in Locusta migratoria and its association with the male accessory glands, the salivary glands, the heart, and the oviduct

• Published in: Peptides (New York, N.Y. : 1980) Vol. 14; no. 3; pp. 409 - 421
• Main Authors: Schoofs, Liliane, Holman, G.Mark, Paemen, Liesbeth, Veelaert, Dirk, Amelinckx, Marc, De Loof, Arnold
• Format: Journal Article
• Language: English
• Published: New York, NY Elsevier Inc 01.05.1993; Elsevier Science
• Subjects: Amino Acid Sequence; Animals; Biochemistry. Physiology. Immunology; Biological and medical sciences; Female; Fundamental and applied biological sciences. Psychology; Genitalia, Male - chemistry; Grasshoppers - chemistry; Heart; Identification of insect neuropeptides; Immunohistochemistry; Insect Hormones - analysis; Insect Hormones - chemical synthesis; Insect Hormones - isolation & purification; Insecta; Invertebrates; Locusta migratoria; Male; Male accessory glands; Membrane Potentials - physiology; Molecular Sequence Data; Myocardium - chemistry; Nervous system; Neuropeptides - analysis; Neuropeptides - chemical synthesis; Neuropeptides - isolation & purification; Neurotransmitter; Oviduct; Oviducts - chemistry; Physiology. Development; Salivary glands; Salivary Glands - chemistry; SchistoFLRFamide; Staining and Labeling; Heart; Salivary glands; Neurotransmitter; SchistoFLRFamide; Nervous system; Identification of insect neuropeptides; Male accessory glands; Oviduct; Locusta migratoria; Purification; Insecta; Orthoptera; Salivary gland; Neuropeptide; Biological activity; Acrididae; Arthropoda; Acridoidea; Invertebrata; Aminoacid sequence; Male accessory sex organ
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/0196-9781(93)90126-2

An amidated decapeptide, exhibiting strong inhibitory activity of spontaneous visceral muscle movements, was isolated from 9000 brain-corpora cardiaca-corpora allata-subesophageal ganglion complexes of the migratory locust, Locusta migratoria. During the process of HPLC purifications, the biological activity of the fractions was monitored using the isolated hindgut of the cockroach Leucophaea maderae. The primary structure of this myotropic peptide is Pro-Asp-Val-Asp-His-Val-Phe-Leu-Arg-Phe-NH 2 and is identical to SchistoFLRFamide isolated from the grasshopper, Schistocerca gregaria. It shares the carboxy-terminal sequence FLRFamide with several identified peptides from different phyla. At this moment, six decapeptides isolated from different insect species are identical at 7 of the 10 amino acid residues (X-D-V-X-H-X-FLRFamide). The cockroach, fly, and locust peptides differ only by the N- terminal amino acid residue. Synthetic SchistoFLRFamide showed biological as well as chemical characteristics indistinguishable from the native peptide. It provoked a decrease in frequency and amplitude of contractions of the locust oviduct. By means of a polyclonal antiserum directed against the carboxy terminal of SchistoFLRFamide, we demonstrated that the male accessory glands, the heart, the oviduct, and the salivary glands were innervated by axons containing SchistoFLRFamide-like immunoreactivity. Administration of SchistoFLRFamide elicited an immediate effect on the basal membrane potential of the opalescent tubule gland cells.