Molecular Cloning of the
            <i>Bombyx mori</i>
            Prothoracicotropic Hormone

Kawakami, Atsushi; Kataoka, Hiroshi; Oka, Tadanori; Mizoguchi, Akira; Kimura-Kawakami, Mina; Adachi, Takashi; Iwami, Masafumi; Nagasawa, Hiromichi; Suzuki, Akira; Ishizaki, Hironori

doi:10.1126/science.2315701

Cited by 212 publications

(151 citation statements)

References 9 publications

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“…This is true for the extended Phe-Met-Arg-Phe-NH, (FMRFamides) [46, 471, the drosulfakinins [48], adipokinetic hormone [49-511, prothoracicotropic hormone [52], pheromone biosynthesis-activating neuropeptide [53, 541, and diuretic hormone [55]. Eclosion hormone from Lepidoptera [ll, 131 and neuroparsin A from Locusra [56] were the simplest in this regard with only a single copy of peptide following the signal sequence.…”

Section: Discussionmentioning

confidence: 99%

Isolation, characterization and expression of the eclosion hormone gene of Drosophila melanogaster

Horodyski

Ewer

Riddiford

et al. 1993

European Journal of Biochemistry

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Eclosion hormone (EH) is a neuropeptide that triggers the performance of ecdysis behaviors at the end of a molt. We have isolated the EH gene from Drosophila melanogasfer, and localized the gene to the right arm of chromosome 3 at band position 90B1-2. The 97-amino-acid translation product contains a signal peptide followed by a 73-amino-acid prohormone. The N-terminus of the prohormone has diverged from lepidopteran EH both in its length and amino acid composition, and contains a potential endoproteolytic cleavage site. The deduced sequence of Drosophila EH is 58% identical (36 of 62 amino acids) to that of Manduca EH. The EH gene is expressed as a 0.8-kb transcript in a single pair of brain neurons which extend their processes the entire length of the central nervous system and also to the corpora cardiaca portion of the ring gland. These cells show massive depletion of immunoreactive EH at ecdysis.Over the last 10 years, work in invertebrates in general and insects in particular has led to identification of a large number of neuropeptides, many of which are expressed in a small number of cells within the central nervous system (CNS) [l, 21. These findings raise a number of important questions such as the role of these peptides in the normal physiology and development of the organism and the mechanisms that restrict peptide expression to a select set of cells within the CNS. To answer both questions, Drosophila melunogaster provides a number of distinct advantages. Mutants in a desired gene can be generated with relative ease and P-element transformation technology allows examination of regulatory regions that control peptide expression [3, 41. Consequently, we have turned to Drosophila to further our analysis of the neuropeptide eclosion hormone (EH), that triggers ecdysis of insects [5].Eclosion hormone was first found in moths [6] and later shown to be a 62-amino-acid peptide [7 -91 produced by two pairs of ventromedial neurosecretory cells in the brain [lO-131. In moths it has marked behavioral and developmental actions. It is known to act directly on the CNS to release the stereotyped motor programs that bring about the shedding of the old cuticle at the end of each molt [14]. Circulating peptide also acts on peripheral tissues to cause a diverse set of effects such as an increase in plasticity of wing cuticle [15], discharge of secretion by dermal glands [16], and the programmed degeneration of ecdysial muscles [17]. Yet the full range of EH actions are not known because it is not possible to block selectively either release or action of EH in moths. It appeared feasible to study EH in Drosophila because CNS extracts of both Calliphora [5] and Drosophila (Kimura and Truman, unpublished data) show EH activity in moth bioassays. Moreover, blood from ecdysing fleshflies, Sarcophaga bullata, stimulates premature ecdysis behavior in pharate (before ecdysis) flies [18]. The recent cloning of the EH gene from two species of moths, Munduca sexfa [ll] and Bombyx mori [13], has provided an avenue to search for t...

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Section: Discussionmentioning

confidence: 99%

Isolation, characterization and expression of the eclosion hormone gene of Drosophila melanogaster

Horodyski

Ewer

Riddiford

et al. 1993

European Journal of Biochemistry

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“…I) Although the molting hormone, ecdysteroid, is common in these two groups of arthropods, the control system for the ecdysteroid-producing gland, the Y -organ in crustaceans and the prothoracic gland in insects, is completely different; the former is inhibited by the molt-inhibiting hormone (MIH) not to produce ecdysteroids,2) while the latter is stimulated by the prothoracicotropic hormone (PTTH) to produce ecdysteroids. 3 ) These two hormones, MIH and PTTH, have recently been chemically characterized, both revealing them to be completely different from each other in both molecular size and amino acid sequence. Up to now, two MIHs have been isolated and sequenced, one (Hoa-MIH) from the American lobster, lIomarus americanlls,4) and the other (Cam-MIH) from the shore crab, Cllrcinus maenas.…”

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confidence: 99%

Isolation and Amino Acid Sequence of a Molt-inhibiting Hormone from the American Crayfish,Procambarus clarkii

Nagasawa

Yang

Shimizu

et al. 1996

Bioscience, Biotechnology, and Biochemistry

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“…By screening a cDNA expression library constructed from the Bombyx brain mRNA with a mouse polyclonal antibody raised against a synthetic peptide corresponding to the N-terminal 15 amino acids of PTTH subunit, and then with an isolated positive clone as a hybridization probe, seven PTTH cDNA clones were obtained. 26) PTTH cDNA encoded a precursor protein for PTTH subunit, consisting of the signal peptide (29 amino acids), two peptide components (21 and 57 amino acids each), and the PTTH subunit (109 amino acids), in this order from the 5' end (Fig. 8A).…”

Section: )16)mentioning

confidence: 99%

Molecular characterization of the brain secretory peptides, prothoracicotropic hormone (PTTH) and bombyxin, of the silkmoth <i>Bombyx mori</i>

Ishizaki

2004

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

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Molecular characterization of the brain secretory peptides, PTTH and bombyxin, of Bombyx mori is reviewed. PTTH is a 30-kDa homodimeric glycoprotein, the monomer of which consists of 109 amino acids. Two monomers are held together by a disulfide bond. cDNA and gene coding for PTTH were cloned and the precursor protein for PTTH monomer was deduced. A novel 5-kD brain secretory peptide named bombyxin has been discovered from Bombyx brain. Bombyxin is highly homologous to vertebrate insulin-family peptides and possesses the prothoracicotropic activity when injected into brain-removed pupae of a heterologous moth, Samia cynthia ricini, though inactive to Bombyx from which it was derived. cDNA and gene coding for bombyxin were cloned, preprobombyxin protein was deduced, and posttranslational processing to generate mature bombyxin was suggested. The Bombyx genome contains highly multiple copies of the gene coding for bombyxins. Immunohistochemically, PTTH-and bombyxin-producing brain neurosecretory cells were identified.

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Molecular Cloning of the Bombyx mori Prothoracicotropic Hormone

Cited by 212 publications

References 9 publications

Isolation, characterization and expression of the eclosion hormone gene of Drosophila melanogaster

Isolation, characterization and expression of the eclosion hormone gene of Drosophila melanogaster

Isolation and Amino Acid Sequence of a Molt-inhibiting Hormone from the American Crayfish,Procambarus clarkii

Molecular characterization of the brain secretory peptides, prothoracicotropic hormone (PTTH) and bombyxin, of the silkmoth <i>Bombyx mori</i>

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