N‐terminal amino acid sequence of an insect neurohormone, melanization and reddish coloration hormone (MRCH): heterogeneity and sequence homology with human insulin‐like growth factor II

Matsumoto, Shogo; Isogai, Akira; Suzuki, Akira

doi:10.1016/0014-5793(85)80853-x

Cited by 32 publications

(4 citation statements)

References 13 publications

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“…Two PBAN molecules, B. mori PBAN (Bom-PBAN) I and II, have been isolated from adult heads of B. mori (9) and shown to consist of 33 and 34 aa, respectively (10,11). PBAN is now known to be identical to the melanization and reddish coloration hormone, which regulates coloration of integuments associated with phase polymorphism ofthe armyworm Psedaletia separata (12,13). The myotropic neuropeptides, myotropin and pyrokinin, which stimulate muscle contraction of hindguts and oviducts, have been isolated from the brain-SG complexes of the cockroach Leucophaea maderae (14,15) and the locust Locusta migratria (16)(17)(18).…”

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confidence: 99%

Precursor polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori: characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides.

Sato

Oguchi

Menjo

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

214

114

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Peptidergic neurons, which serve as source of various endocrine neuropeptides, were identified in the suboesophageal ganglion (SG) and brain of insects. In the silkworm Bombyx mori, SG is known to secrete two neuropeptides, diapause hormone (DH) responsible for induction ofembryonic diapause and pheromone biosynthesis-activating neuropeptide, which share a pentapeptide amide, Phe-Xaa-Pro-Arg-Leu-NH2 (Xaa = Gly or Ser), at the C terminus. We have isolated cDNA clones for DH from the cDNA library of SG by using oligonucleotide probes. The molecular characterization of the cDNA reveals that the mRNA encodes an open reading frame consisting of 192 aa residues in which the 24-aa DH peptide is localized at the N-terminal region just after the signal peptide. A homology search proposed that the cDNA encodes pheromone biosynthesis-activating neuropeptide and three other neuropeptides [a-, (3-, and y-SG neuropeptide (SGNP)] in the region following DH, all of which are flanked by possible tryptic cleavage sites and share the Phe-Xaa-Pro-Arg-Leu-Gly sequence at the C terminus. Northern hybridization analysis clearly showed that the gene expression was limited to SG. We chemically synthesized a-, p-, and y-SGNP and used them to identify components in extracts of SG and to examine biological functions. a-and y-SGNP were identified in extracts of SG, and the synthetic P-and y-SGNP expressed weak DH activity.These results indicate that DH, along with four other neuropeptides, is generated from a common precursor polyprotein that is encoded by a single mRNA transcribed in neurosecretory cells of SG.

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confidence: 99%

Precursor polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori: characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides.

Sato

Oguchi

Menjo

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

214

114

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“…From the elution pattern of PTTH activities at steps 15 and 16, 22K-PTTH seems to be highly heterogeneous. This is not surprising, however, because such heterogeneity has been generally found in other insect peptide hormones: 4K~PTTH,16) adipokinetic hormone,17,18) melanization and reddish coloration hormone, 19,20) periplanetin,21) and hyperglycemic hormone. 22 ) The isolated hormone was carefully apportioned for analyses: a small sample was used Amino acid for bioassay and rechromatography, about 1flg for amino acid analysis and all the remainder for sequencing.…”

Section: Chemical Characterization Of 22k-ptthmentioning

confidence: 87%

Isolation and Partial Characterization of a Prothoracicotropic Hormone of the Silkworm, Bombyx mori

Kataoka

Nagasawa

Isogai

et al. 1987

Agricultural and Biological Chemistry

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“…However, with a few remarkable exceptions (PTTH-family of Bomby:r; mori: Nagasawa et al, 1986;Kataoka et al, 1987a; Eclosion Hormone of Bomby:r; mori and Manduca sexta: Kono et al, 1987;Kataoka et al, 1987b; Melanization and Reddish Coloration Hormone of Bombyx mori: Matsumoto et al, 1985; AVP-like Insect Diuretic Hormone of Locusta migratoria: Proux et al, 1987), the primary structures of the majority of these neurohormones remain unknown. This situation is to a large extent explained by the relative paucity of biological starting material for isolation and by the lack of reliable bioassays suited for following purifications at the microscale level.…”

Section: Introductionmentioning

confidence: 99%

Production of Monoclonal Antibodies AgainstCorpora CardiacaExtracts ofLocusta Migratoria:A Potential Tool for the Isolation of Insect Neurohormones

Holder¹,

Lwoff²,

Wicker³

et al. 1988

International Journal of Invertebrate Reproduction and Developm

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Corpora cardiaca of Locusta migratoria contain the axon endings of the neurosecretory cells of the brain and store in neurosecretory granules a variety of mostly unidentified neurohormones. Homogena.tes of corpora cardiaca served to generate a. battery of monoclonal antibodies screened by their immunoreactivity to antigenic determinants present in the neurosecretory cells of the pars intercerebralis in the brain. The results are illustrated with three selected monoclonal antibodies which recognize antigens located within the neurosecretory granules of the pericarya of the pars intercerebralis, the cerebra-cardiac axon tracts and the axonic endings in the neurohaemal part of the corpora cardiaca. The apparent molecular weights of these antigenes were determined by Western blotting. vVe discuss the potential of these monoclonal antibodies for the isolation and structure determination of neuropeptides. monoclonal antibodies, neurosecretory cells, brain, immunocytochemistry, Locusta migratoria

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N‐terminal amino acid sequence of an insect neurohormone, melanization and reddish coloration hormone (MRCH): heterogeneity and sequence homology with human insulin‐like growth factor II

Cited by 32 publications

References 13 publications

Precursor polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori: characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides.

Precursor polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori: characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides.

Isolation and Partial Characterization of a Prothoracicotropic Hormone of the Silkworm, Bombyx mori

Production of Monoclonal Antibodies AgainstCorpora CardiacaExtracts ofLocusta Migratoria:A Potential Tool for the Isolation of Insect Neurohormones

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