Document Detail


Isolation and structural characterization of an insulin-related molecule, a predominant neuropeptide from Locusta migratoria.
MedLine Citation:
PMID:  1935945     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Neurohaemal lobes of corpora cardiaca of Locusta migratoria are an established storage site for neurohormones produced by the neurosecretory cells of the brain. As previously reported [Hietter, H., Van Dorsselaer, A., Green, B., Denoroy, L., Hoffmann, J.A. & Luu, B. (1990) Eur. J. Biochem. 187, 241-247], the isolation and characterization of a novel 5-kDa peptide from these lobes served as the basis for oligonucleotide screening of cDNA libraries prepared from poly(A) RNA from neurosecretory cells of the central nervous system. From subsequent cDNA cloning studies [Lagueux, M., Lwoff, L., Meister, M., Goltzené, F. & Hoffmann, J.A. (1990) Eur. J. Biochem. 187, 249-254], the existence of a 145-residue precursor protein was deduced, which contained, in addition to the 5-kDa peptide, amino-acid sequences with homology to the A and B chains of an insulin-related peptide. In the present study we have isolated the native molecule from corpora cardiaca of Locusta and characterized, by Edman degradation and plasma-desorption mass spectrometry, the two chains as follows: A chain, Gly-Val-Phe-Asp-Glu-Cys-Cys-Arg-Lys-Ser-Cys-Ser-Ile-Ser-Glu-Leu-Gln-Thr- Tyr-Cys - Gly (Ile, isoleucine); B chain, Ser-Gly-Ala-Pro-Gln-Pro-Val-Ala-Arg-Tyr-Cys-Gly-Glu-Lys-Leu-Ser-Asn-Ala- Leu-Lys - Leu-Val-Cys-Arg-Gly-Asn-Tyr-Asn-Thr-Met-Phe. Taken in conjunction with the previous cloning studies, our data lead to a clear picture of the processing of Locusta preproinsulin. They indicate that locusta corpora cardiaca contain remarkably large amounts of one single insulin form, in contrast to multiple insulin isoforms of Bombyx mori, the only other insect species from which insulin-related peptides have been isolated and characterized [Nagasawa, H., Kataoka, H., Isogai, A., Tamura, S., Suzuki, A., Mizoguchi, A., Fujiwara, Y., Suzuki, A., Takahashi, S. & Ishizaki, H. (1986) Proc. Natl Acad. Sci. USA 83, 5840-5843].
Authors:
C Hetru; K W Li; P Bulet; M Lagueux; J A Hoffmann
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  201     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1991 Oct 
Date Detail:
Created Date:  1991-12-03     Completed Date:  1991-12-03     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  495-9     Citation Subset:  IM    
Affiliation:
Laboratoire de Biologie Générale de l'Université Louis Pasteur, Unité de Recherche Associée au CNRS, Strasbourg, France.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Chromatography, High Pressure Liquid
DNA / genetics
Female
Grasshoppers / chemistry*
Insect Hormones / chemistry,  genetics,  isolation & purification*
Insulin / chemistry,  genetics,  isolation & purification*
Mass Spectrometry
Molecular Sequence Data
Neuropeptides / chemistry,  genetics,  isolation & purification*
Proinsulin / chemistry,  genetics,  isolation & purification
Protein Conformation
Chemical
Reg. No./Substance:
0/Insect Hormones; 0/Neuropeptides; 11061-68-0/Insulin; 9007-49-2/DNA; 9035-68-1/Proinsulin

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