Isolation, sequence determination, physical and physiological characterization of the neuroparsins and ovary maturing parsins of Schistocerca gregaria

• Published in: Insect biochemistry and molecular biology 1998-09, Vol.28 (9), p.641-650
• Main Authors: Girardie, Josiane, Huet, Jean-Claude, Atay-Kadiri, Zineb, Saghir Ettaouil, Delbecque, Jean-Paul, Fournier, Bernard, Jean-Claude Pernollet, Girardie, Adrien
• Format: Article
• Language: English
• Subjects: Aging; Amino Acid Sequence; Animals; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Female; Grasshoppers - chemistry; Grasshoppers - growth & development; Insect Hormones - chemistry; Insect Hormones - isolation & purification; Insect Proteins - chemistry; Insect Proteins - isolation & purification; Mass Spectrometry; Molecular Sequence Data; Nerve Tissue Proteins - chemistry; Nerve Tissue Proteins - isolation & purification; Nervous System - chemistry; Nervous System - growth & development; neurohormone sequence; neuroparsins; ovary maturing parsins; pars intercerebralis-corpora cardiaca system; Peptide Fragments - chemistry; Schistocerca gregaria
• ISSN: 0965-1748; 1879-0240
• DOI: 10.1016/S0965-1748(98)00053-8

Neurosecretory products immunologically related to either neuroparsin (NP) or ovary maturing parsin (OMP) of Locusta migratoria (Lom) were purified from the nervous corpora cardiaca of Schistocerca gregaria (Scg). The determination of both their molecular masses by mass spectrometry and their sequences by automated Edman degradation established that they are members of the NP and OMP families respectively. NP molecules of Schistocerca (Scg NPs) consisted of two major forms having about the same molecular masses as NPA and NPB of Locusta and 88% primary structure similarity. They had also the same antidiuretic activity. OMP molecules of Schistocerca (Scg OMPs) were composed in young adults of four isoforms: two long isoforms corresponding to Lom OMP, and differing by a tripeptide insertion (Pro–Ala–Ala) at position 21 and two short isoforms deprived of the 13-residue N-terminal peptide of Lom OMP and differing by the same tripeptide insertion. The PAA isoforms were observed in low amounts as compared to the other isoforms. In mature adults, only the two short isoforms were present. The complete sequence of PAA Scg OMP presents a large degree of sequence homology with Lom OMP (83%). The mixed Scg OMPs had the same biological effects as Lom OMPs. They induced precocious occurrence of both ecdysteroids and vitellogenin in the haemolymph and stimulated oöcyte growth.