Pheromone gland-specific fatty-acyl reductase of the silkmoth,
            <i>Bombyx mori</i>

Moto, Ken'ichi; Yoshiga, Toyoshi; Yamamoto, Masanobu; Takahashi, Shigetoshi; Okano, Kazuhiro; Ando, Tetsu; Nakata, Tadashi; Matsumoto, Shogo

doi:10.1073/pnas.1531993100

Cited by 169 publications

(216 citation statements)

References 29 publications

(45 reference statements)

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“…Transcripts encoding proteins essential to silkmoth sex pheromone production have been shown to be PG specific and undergo up-regulation in the day preceding adult emergence from the pupal stage (8,27,28). To examine the expression profile of BmSTIM1, reverse transcriptase-PCR analyses were performed using primer pairs designed to amplify the entire ORF.…”

Section: Resultsmentioning

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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Section: Resultsmentioning

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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“…For the most abundant desaturase gene, desat1, the p50 pheromonegland cDNA library described in ref. 7 was screened with a 519-bp DNA fragment of desat1 as a probe that was prepared by using the direct nucleic acid labeling and detection systems (Amersham Pharmacia). The 519-bp DNA fragment used as a probewasamplifiedbyusingtheprimers5Ј-CTAAATTACTAAA-ATGCCTCC-3Ј and 5Ј-AAATATCTGACATGTCAAGGC-3Ј, which were designed from the 2,029-bp B. mori desat1 cDNA previously cloned from the hybrid strain Shuko ϫ Ryuhaku (12).…”

Section: Methodsmentioning

confidence: 99%

“…The biosynthesis of bombykol from the intermediate palmitate (C16:acyl) is a rather simple procedure that eschews the common chain-shortening and hydroxyl group modification steps for three consecutive steps, i.e., Z11 desaturation, (E,Z)-10,12 desaturation, and fatty-acyl reduction (2,6). Among these steps, we have recently characterized the enzyme responsible for the fatty-acyl reduction, which we named pheromone gland fatty-acyl reductase (pgFAR) (7). On the other hand, the desaturases responsible for the two desaturation steps have yet to be identified and characterized.…”

mentioning

confidence: 99%

Involvement of a bifunctional fatty-acyl desaturase in the biosynthesis of the silkmoth, Bombyx mori , sex pheromone

Moto

Suzuki

Hull

et al. 2004

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

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The straight-chain C10 to C18 unsaturated aliphatic compounds containing an oxygenated functional group (aldehyde, alcohol, or acetate ester) derived from saturated C 16 or C18 fatty acids are a major class of sex pheromone components produced by female moths. In the biosynthesis of these pheromone components, various combinations of limited chain-shortening and regio-and stereospecific desaturation reactions significantly contribute to the production of a vast number of the species-specific pheromone components in Lepidoptera. Biosynthesis of the silkmoth sex pheromone bombykol, (E,Z)-10,12-hexadecadien-1-ol, involves two consecutive desaturation steps, the second of which is unique in that it generates a conjugated diene system from the ⌬11-monoene C 16 intermediate. In experiments designed to characterize the acyl-CoA desaturases responsible for bombykol biosynthesis, we have cloned three cDNAs encoding desaturase family members from the pheromone gland of the inbred strain of the silkmoth, Bombyx mori. Transcript analyses by RT-PCR and subsequent functional assays using a Bac-to-Bac baculovirus expression system revealed that desat1 is the only desaturase gene prominently expressed during pheromonogenesis and that its gene product, B. mori Desat1, possesses both Z11 desaturation and ⌬10,12-desaturation activities. Consequently, we have concluded that B. mori Desat1 is not only a bifunctional desaturase involved in bombykol biosynthesis but that it is also the enzyme responsible for both desaturation steps.

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“…The first, from the jojoba plant S. chinensis (6), identified two mouse and human proteins with ϳ30% sequence identity. The second fatty acyl-CoA reductase sequence was from the silkworm moth B. mori (7). A search for orthologs of this insect enzyme in the mammalian data base revealed the same two mouse and human proteins as did searches with the plant enzyme sequence, again with low sequence identity.…”

Section: Resultsmentioning

confidence: 94%

Mammalian Wax Biosynthesis

Cheng¹,

Russell

2004

Journal of Biological Chemistry

215

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The conversion of fatty acids to fatty alcohols is required for the synthesis of wax monoesters and ether lipids. The mammalian enzymes that synthesize fatty alcohols have not been identified. Here, an in silico approach was used to discern two putative reductase enzymes designated FAR1 and FAR2. Expression studies in intact cells showed that FAR1 and FAR2 cDNAs encoded isozymes that reduced fatty acids to fatty alcohols. Fatty acyl-CoA esters were the substrate of FAR1, and the enzyme required NADPH as a cofactor. FAR1 preferred saturated and unsaturated fatty acids of 16 or 18 carbons as substrates, whereas FAR2 preferred saturated fatty acids of 16 or 18 carbons. Confocal light microscopy indicated that FAR1 and FAR2 were localized in the peroxisome. The FAR1 mRNA was detected in many mouse tissues with the highest level found in the preputial gland, a modified sebaceous gland. The FAR2 mRNA was more restricted in distribution and most abundant in the eyelid, which contains wax-laden meibomian glands. Both FAR mRNAs were present in the brain, a tissue rich in ether lipids. The data suggest that fatty alcohol synthesis in mammals is accomplished by two fatty acyl-CoA reductase isozymes that are expressed at high levels in tissues known to synthesize wax monoesters and ether lipids.Wax esters are abundant neutral lipids that coat the surfaces of plants, insects, and mammals. They are composed of long chain alcohols esterified to fatty acids and have the chemical property of being solid at room temperature and liquid at higher temperatures. Waxes play essential biological roles in preventing water loss, abrasion, and infection and are produced commercially at levels approaching 3 billion pounds per year for use in polishes, cosmetics, and packaging. In some mammals, wax esters constitute ϳ30% of sebum and meibum, the oils secreted by the sebaceous and meibomian glands onto the surfaces of the skin and eye, respectively (1, 2).Although the enzymes of wax biosynthesis in mammals have not been isolated, the components of the pathway can be inferred from work in plants (3, 4) and mammalian tissue extracts (5). As indicated in Scheme 1, two catalytic steps are required to produce a wax monoester, including reduction of a fatty acid to a fatty alcohol and subsequently, the trans-esterification of the fatty alcohol to a fatty acid. The first step is catalyzed by the enzyme fatty acyl-CoA reductase (FAR), 1 which uses the reducing equivalents of NAD(P)H to convert a fatty acyl-CoA into a fatty alcohol and CoASH. cDNAs specifying fatty acyl-CoA reductases have been identified in the jojoba plant (6), the silkworm moth (7), wheat (8), and in a microorganism (9); however, the biochemical properties and subcellular localizations of these enzymes have not been reported.Fatty alcohols have two metabolic fates in mammals: incorporation into ether lipids or incorporation into waxes. Ether lipids account for ϳ20% of phospholipids in the human body and are synthesized in membranes by a pathway involving at least seven enzymes (10...

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

Cited by 169 publications

References 29 publications

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

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

Involvement of a bifunctional fatty-acyl desaturase in the biosynthesis of the silkmoth, Bombyx mori , sex pheromone

Mammalian Wax Biosynthesis

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