Action of Pheromone Biosynthesis Activating Neuropeptide on Pheromone Glands of &lt;i&gt;Bombyx mori&lt;/i&gt; and &lt;i&gt;Spodoptera litura&lt;/i&gt;

Fónagy, Adrien; Matsumoto, Shogo; Uchiumi, Kyoichi; Orikasa, Chitose; Mitsui, Takashi

doi:10.1584/jpestics.17.47

Cited by 52 publications

(23 citation statements)

References 7 publications

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“…In B. mori, PBAN directly acts on the pheromone gland to stimulate bombykol production (8,24). Because bombykol production occurs shortly after adult eclosion in response to PBAN (5,24), the pheromone-producing cells must be primed for pheromone production upon adult eclosion.…”

Section: Discussionmentioning

confidence: 99%

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Pheromone gland-specific fatty-acyl reductase of the silkmoth, Bombyx mori

Moto

Yoshiga

Yamamoto

et al. 2003

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

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169

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The C10-C18 unsaturated, acyclic, aliphatic compounds that contain an oxygenated functional group (alcohol, aldehyde, or acetate ester) are a major class of sex pheromones produced by female moths. In the biosynthesis of these pheromone components, the key enzyme required to produce the oxygenated functional groups is fatty-acyl reductase (FAR). This enzyme converts fatty-acyl pheromone precursors to their corresponding alcohols, which, depending on the moth species, can then be acetylated or oxidized to the corresponding aldehydes. Despite the significant role this enzyme has in generating the species-specific oxygenated constituents of lepidopteran sex pheromones, the enzyme has yet to be fully characterized and identified. In experiments designed to characterize a pheromone-gland-specific FAR in the silkmoth, Bombyx mori, we have isolated a cDNA clone encoding a protein homologous to a FAR from the desert shrub, Simmondsia chinensis, commonly known as jojoba. The deduced amino acid sequence of this clone predicts a 460-aa protein with a consensus NAD(P)H binding motif within the amino terminus. Northern blot analysis indicated that 2-kb transcripts of this gene were specifically expressed in the pheromone gland at 1 day before adult eclosion. Functional expression of this gene in the yeast Saccharomyces cerevisiae not only confirmed the long-chain FAR activity, but also indicated a distinct substrate specificity. Finally, the transformed yeast cells evoked typical mating behavior in male moths when cultured with the pheromone precursor fatty acid, (E,Z)-10,12-hexadecadienoic acid.

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Section: Discussionmentioning

confidence: 99%

“…Eggs of B. mori (Shuko ϫ Ryuhaku) were purchased from Katakura Kogyo (Matsumoto, Japan). Larvae were reared on an artificial diet as described (8).…”

Section: Methodsmentioning

confidence: 99%

Pheromone gland-specific fatty-acyl reductase of the silkmoth, Bombyx mori

Moto

Yoshiga

Yamamoto

et al. 2003

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

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169

202

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“…Insects-Larvae of the inbred p50 strain of B. mori and the B. mori racial hybrid (Shuko x Ryuhaku) were reared on an artificial diet and maintained under a 16L:8D photoperiod at 25°C (16).…”

Section: Methodsmentioning

confidence: 99%

Bombyx mori Homologs of STIM1 and Orai1 Are Essential Components of the Signal Transduction Cascade That Regulates Sex Pheromone Production

Hull

Lee

Kajigaya

et al. 2009

Journal of Biological Chemistry

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Sex pheromone production in the pheromone gland (PG) of the silkmoth, Bombyx mori, is mediated by store-operated channels (SOCs) acting downstream of pheromone biosynthesis activating neuropeptide (PBAN) binding. Although recent studies have implicated STIM1 and Orai1 as essential components of SOCs, little is known about the molecular nature of the SOCs involved in sex pheromone production. In this study we cloned silkmoth homologs of STIM1 and Orai1 and sought to determine whether they comprise the PG SOC pathway. BmSTIM1 is expressed in multiple tissues and, in the PG, is encoded by two transcripts of differing size. BmOrai1A and BmOrai1B, which are identical except for a 37-residue N-terminal truncation in BmOrai1B, arise from alternative splicing of the bmorai1 locus and are expressed as independent transcripts in various tissues. In the PG, only BmOrai1B is actively transcribed. Fluorescent chimeras demonstrated that BmSTIM1 expression is restricted to the endoplasmic reticulum, whereas both BmOrai1A and BmOrai1B localize to the cell surface. In Ca 2؉ -free medium, thapsigargin-mediated depletion of endoplasmic reticulum Ca 2؉ stores resulted in redistribution of BmSTIM1 to the plasma membrane, but only when the BmOrai1 homologs were also overexpressed. Translocation was dependent on the BmSTIM1 C terminus "CRAC activation domain." Ala mutation of Lys 380 , Lys 383 , Lys 384 , Arg 382 , and Arg 385 suggests that translocation involves electrostatic interactions. Translocation was also seen following PBAN stimulation in cells co-expressing BmSTIM1, BmOrai1B, and the PBAN receptor. In vivo RNA interference-mediated knockdown of BmSTIM1 and BmOrai1 significantly reduced sex pheromone production without affecting cell viability.

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“…mori eggs (Shuko ϫ Ryuhaku) were purchased from Katakura Kogyo (Matsumoto, Japan), and larvae were raised on an artificial diet as described (22). Bioassays were performed using 5-10 female pupae 3 days before eclosion (day Ϫ3).…”

Section: Methodsmentioning

confidence: 99%

Isolation and Characterization of a Humoral Factor That Stimulates Transcription of the Acyl-CoA-binding Protein in the Pheromone Gland of the Silkmoth, Bombyx mori

Ohnishi

Koshino

Takahashi

et al. 2005

Journal of Biological Chemistry

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Acyl-CoA binding protein (ACBP) is a highly conserved 10-kDa intracellular lipid-binding protein that binds straight-chain (C 14 -C 22 ) acyl-CoA esters with high affinity and is expressed in a wide variety of species ranging from yeast to mammals. Functionally, ACBP can act as an acyl-CoA carrier or as an acyl-CoA pool maker within the cell. Much work on the biochemical properties regarding the ACBP has been performed using various vertebrate and plant tissues, as well as different types of cells in culture, the regulatory mechanisms underlying ACBP gene expression have remained poorly understood. By exploiting the unique sex pheromone production system in the moth pheromone gland (PG), we report that transcription of a specific ACBP termed pheromone gland ACBP is triggered by a hemolymph-based humoral factor. Following purification and structure elucidation by means of high resolution electrospray ionization mass spectrometry and NMR analyses, in conjunction with stereochemical analyses using acid hydrolysates, the humoral factor was identified to be ␤-D-glucosyl-O-L-tyrosine. Examination of the hemolymph titers during development revealed that the amount of ␤-D-glucosyl-O-L-tyrosine dramatically rose prior to eclosion and reached a maximum of 5 mg/ml (about 1 mg/pupa) on the day preceding eclosion, which was consistent with the effective dose of ␤-D-glucosyl-O-L-tyrosine in stimulating pheromone gland ACBP transcription in vivo. Furthermore, in vitro assays using trimmed PG indicated that ␤-D-glucosyl-O-L-tyrosine acts directly on the PG. These results provide the first evidence that transcription of some ACBPs can be triggered by specific humoral factors.

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Action of Pheromone Biosynthesis Activating Neuropeptide on Pheromone Glands of <i>Bombyx mori</i> and <i>Spodoptera litura</i>

Cited by 52 publications

References 7 publications

Pheromone gland-specific fatty-acyl reductase of the silkmoth, Bombyx mori

Pheromone gland-specific fatty-acyl reductase of the silkmoth, Bombyx mori

Bombyx mori Homologs of STIM1 and Orai1 Are Essential Components of the Signal Transduction Cascade That Regulates Sex Pheromone Production

Isolation and Characterization of a Humoral Factor That Stimulates Transcription of the Acyl-CoA-binding Protein in the Pheromone Gland of the Silkmoth, Bombyx mori

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