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Volumn 43, Issue 8, 2013, Pages 675-682

Aldehyde dehydrogenase 3 converts farnesal into farnesoic acid in the corpora allata of mosquitoes

Author keywords

Aedes aegypti; Aldehyde dehydrogenase 3; Aldo keto reductase; Corpora allata; Farnesal; Juvenile hormone; Mosquito; RNAi

Indexed keywords

ALDEHYDE DEHYDROGENASE; DRUG DERIVATIVE; FARNESAL; FARNESAL DEHYDROGENASE; FARNESOIC ACID; FARNESOL; JUVENILE HORMONE; MESSENGER RNA; UNSATURATED FATTY ACID;

EID: 84879475606     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2013.04.002     Document Type: Article
Times cited : (34)

References (49)
  • 1
    • 34547106607 scopus 로고    scopus 로고
    • Dual subcellular localization in the endoplasmic reticulum and peroxisomes and a vital role in protecting against oxidative stress of fatty aldehyde dehydrogenase are achieved by alternative splicing
    • Ashibe B., Hirai T., Higashi K., Sekimizu K., Motojima K.J. Dual subcellular localization in the endoplasmic reticulum and peroxisomes and a vital role in protecting against oxidative stress of fatty aldehyde dehydrogenase are achieved by alternative splicing. J.Biol. Chem. 2007, 282:20763-20773.
    • (2007) J.Biol. Chem. , vol.282 , pp. 20763-20773
    • Ashibe, B.1    Hirai, T.2    Higashi, K.3    Sekimizu, K.4    Motojima, K.J.5
  • 2
    • 0020989036 scopus 로고
    • Farnesol and farnesal dehydrogenase(s) in corpora allata of the tobacco hornworm moth, Manduca sexta
    • Baker F.C., Mauchamp B., Tsai L.W., Schooley D.A. Farnesol and farnesal dehydrogenase(s) in corpora allata of the tobacco hornworm moth, Manduca sexta. J.Lipid Res. 1983, 24:1586-1594.
    • (1983) J.Lipid Res. , vol.24 , pp. 1586-1594
    • Baker, F.C.1    Mauchamp, B.2    Tsai, L.W.3    Schooley, D.A.4
  • 3
    • 12744262788 scopus 로고    scopus 로고
    • The mevalonate pathway and the synthesis of juvenile hormone in insects
    • Bellés X., Martin D., Piulachs M.-D. The mevalonate pathway and the synthesis of juvenile hormone in insects. Annu. Rev. Entomol. 2005, 50:181-199.
    • (2005) Annu. Rev. Entomol. , vol.50 , pp. 181-199
    • Bellés, X.1    Martin, D.2    Piulachs, M.-D.3
  • 4
    • 3543025169 scopus 로고    scopus 로고
    • Reduced juvenile hormone synthesis in mosquitoes with low teneral reserves prevents ovarian previtellogenic development in Aedes aegypti
    • Caroci A., Li Y., Noriega F.G. Reduced juvenile hormone synthesis in mosquitoes with low teneral reserves prevents ovarian previtellogenic development in Aedes aegypti. J.Exp. Biol. 2004, 207:2685-2690.
    • (2004) J.Exp. Biol. , vol.207 , pp. 2685-2690
    • Caroci, A.1    Li, Y.2    Noriega, F.G.3
  • 5
    • 84931378058 scopus 로고    scopus 로고
    • Juvenile hormone biosynthetic enzymes as targets for insecticide discovery
    • Springer, I. Ishayya, S.R. Palli, A.R. Horowitz (Eds.)
    • Cusson M., Sen S.E., Shinoda T. Juvenile hormone biosynthetic enzymes as targets for insecticide discovery. Advanced Technologies for Managing Insect Pests 2013, 31-55. Springer. I. Ishayya, S.R. Palli, A.R. Horowitz (Eds.).
    • (2013) Advanced Technologies for Managing Insect Pests , pp. 31-55
    • Cusson, M.1    Sen, S.E.2    Shinoda, T.3
  • 6
    • 0016990971 scopus 로고
    • The origin and evolution of protein superfamilies
    • Dayhoff M.O. The origin and evolution of protein superfamilies. Fed. Proc. 1976, 35:2132-2138.
    • (1976) Fed. Proc. , vol.35 , pp. 2132-2138
    • Dayhoff, M.O.1
  • 9
    • 0007361946 scopus 로고
    • Partitioning of long-chain alcohols into lipid bilayers: implications for mechanisms of general anesthesia
    • Franks N.P., Lieb W.R. Partitioning of long-chain alcohols into lipid bilayers: implications for mechanisms of general anesthesia. Proc. Natl. Acad. Sci. U.S.A. 1986, 83:5116-5120.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 5116-5120
    • Franks, N.P.1    Lieb, W.R.2
  • 10
    • 84873816282 scopus 로고    scopus 로고
    • The juvenile hormones
    • Elsevier, L.I. Gilbert (Ed.)
    • Goodman W.G., Cusson M. The juvenile hormones. Insect Endocrinology 2012, 310-365. Elsevier. L.I. Gilbert (Ed.).
    • (2012) Insect Endocrinology , pp. 310-365
    • Goodman, W.G.1    Cusson, M.2
  • 11
    • 1642529589 scopus 로고    scopus 로고
    • CYP15A1, the cytochrome P450 that catalyzes epoxidation of methyl farnesoate to juvenile hormone III in cockroach corpora allata
    • Helvig C., Koener J.F., Unnithan G.C., Feyereisen R. CYP15A1, the cytochrome P450 that catalyzes epoxidation of methyl farnesoate to juvenile hormone III in cockroach corpora allata. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:4024-4029.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 4024-4029
    • Helvig, C.1    Koener, J.F.2    Unnithan, G.C.3    Feyereisen, R.4
  • 12
    • 0031005062 scopus 로고    scopus 로고
    • The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold
    • Hempel J., Wang B.-C. The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold. Nat. Struct. Mol. Biol. 1997, 4:317-326.
    • (1997) Nat. Struct. Mol. Biol. , vol.4 , pp. 317-326
    • Hempel, J.1    Wang, B.-C.2
  • 13
    • 33847410620 scopus 로고    scopus 로고
    • Role of juvenile hormone and allatotropin on nutrient allocation, ovarian development and survivorship in mosquitoes
    • Hernandez-Martinez S., Mayoral J.G., Li Y., Noriega F.G. Role of juvenile hormone and allatotropin on nutrient allocation, ovarian development and survivorship in mosquitoes. J.Insect Physiol. 2007, 53:230-234.
    • (2007) J.Insect Physiol. , vol.53 , pp. 230-234
    • Hernandez-Martinez, S.1    Mayoral, J.G.2    Li, Y.3    Noriega, F.G.4
  • 14
    • 79957547123 scopus 로고    scopus 로고
    • Comparative studies of vertebrate aldehyde dehydrogenase 3: sequences, structures, phylogeny and evolution. Evidence for a mammalian origin for the ADLH3A1 gene
    • Holmes R.S., Hempel J. Comparative studies of vertebrate aldehyde dehydrogenase 3: sequences, structures, phylogeny and evolution. Evidence for a mammalian origin for the ADLH3A1 gene. Chem. Biol. Interact. 2011, 191:113-121.
    • (2011) Chem. Biol. Interact. , vol.191 , pp. 113-121
    • Holmes, R.S.1    Hempel, J.2
  • 15
    • 0022530641 scopus 로고
    • Some properties of the fatty alcohol oxidation system and reconstitution of microsomal oxidation activity in intestinal mucosa
    • Ichihara K., Kusunose E., Noda Y., Kusunose M. Some properties of the fatty alcohol oxidation system and reconstitution of microsomal oxidation activity in intestinal mucosa. Biochim. Biophys. Acta 1986, 878:412-418.
    • (1986) Biochim. Biophys. Acta , vol.878 , pp. 412-418
    • Ichihara, K.1    Kusunose, E.2    Noda, Y.3    Kusunose, M.4
  • 16
    • 0025611278 scopus 로고
    • The enzymes of detoxication
    • Jakoby W.B., Ziegler D.M. The enzymes of detoxication. J.Biol. Chem. 1990, 265:20715-20718.
    • (1990) J.Biol. Chem. , vol.265 , pp. 20715-20718
    • Jakoby, W.B.1    Ziegler, D.M.2
  • 17
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D.T. Protein secondary structure prediction based on position-specific scoring matrices. J.Mol. Biol. 1999, 292:195-202.
    • (1999) J.Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 19
    • 0030936743 scopus 로고    scopus 로고
    • Human liver fatty aldehyde dehydrogenase: microsomal localization, purification, and biochemical characterization
    • Kelson T.L., Secor McVoy J.R., Rizzo W.B. Human liver fatty aldehyde dehydrogenase: microsomal localization, purification, and biochemical characterization. Biochim. Biophys. Acta 1997, 1335:99-110.
    • (1997) Biochim. Biophys. Acta , vol.1335 , pp. 99-110
    • Kelson, T.L.1    Secor McVoy, J.R.2    Rizzo, W.B.3
  • 20
    • 0001337667 scopus 로고    scopus 로고
    • Endocrine aspects of mosquito reproduction
    • Klowden M.J. Endocrine aspects of mosquito reproduction. Arch. Insect Biochem. Physiol. 1997, 35:491-512.
    • (1997) Arch. Insect Biochem. Physiol. , vol.35 , pp. 491-512
    • Klowden, M.J.1
  • 23
    • 0026655335 scopus 로고
    • Aldehyde dehydrogenases and their role in carcinogenesis
    • Lindahl R. Aldehyde dehydrogenases and their role in carcinogenesis. Crit. Rev. Biochem. Mol. Biol. 1992, 27:283-335.
    • (1992) Crit. Rev. Biochem. Mol. Biol. , vol.27 , pp. 283-335
    • Lindahl, R.1
  • 26
    • 0015548810 scopus 로고
    • Farnesol metabolism in Drosophila melanogaster: ontogeny and tissue distribution of octanol dehydrogenase and aldehyde oxidase
    • Madhavan K., Conscience-Egli M., Sieber F., Ursprung H. Farnesol metabolism in Drosophila melanogaster: ontogeny and tissue distribution of octanol dehydrogenase and aldehyde oxidase. J.Insect Physiol. 1973, 19:235-241.
    • (1973) J.Insect Physiol. , vol.19 , pp. 235-241
    • Madhavan, K.1    Conscience-Egli, M.2    Sieber, F.3    Ursprung, H.4
  • 27
    • 0028068939 scopus 로고
    • Microsomal aldehyde dehydrogenase is localized to the endoplasmic reticulum via its carboxyl-terminal 35 amino acids
    • Masaki R., Yamamoto A., Tashiro Y. Microsomal aldehyde dehydrogenase is localized to the endoplasmic reticulum via its carboxyl-terminal 35 amino acids. J.Cell. Biol. 1994, 126:1407-1420.
    • (1994) J.Cell. Biol. , vol.126 , pp. 1407-1420
    • Masaki, R.1    Yamamoto, A.2    Tashiro, Y.3
  • 30
    • 0023090971 scopus 로고
    • The oxidation of a, b-unsaturated aldehyde products of lipid peroxidation by rat liver aldehyde dehydrogenases
    • Mitchell D.Y., Petersen D.R. The oxidation of a, b-unsaturated aldehyde products of lipid peroxidation by rat liver aldehyde dehydrogenases. Toxicol. Appl. Pharmacol. 1987, 87:403-410.
    • (1987) Toxicol. Appl. Pharmacol. , vol.87 , pp. 403-410
    • Mitchell, D.Y.1    Petersen, D.R.2
  • 31
    • 0025935386 scopus 로고
    • Molecular cloning, sequencing, and expression of cDNA for rat liver microsomal aldehyde dehydrogenase
    • Miyauchi K., Masaki R., Taketani S., Yamamoto A., Akayama M., Tashiro Y. Molecular cloning, sequencing, and expression of cDNA for rat liver microsomal aldehyde dehydrogenase. J.Biol. Chem. 1991, 266:19536-19542.
    • (1991) J.Biol. Chem. , vol.266 , pp. 19536-19542
    • Miyauchi, K.1    Masaki, R.2    Taketani, S.3    Yamamoto, A.4    Akayama, M.5    Tashiro, Y.6
  • 32
    • 78649710230 scopus 로고    scopus 로고
    • Dynamic metabolons
    • Moller B.L. Dynamic metabolons. Science 2010, 330:1328-1329.
    • (2010) Science , vol.330 , pp. 1328-1329
    • Moller, B.L.1
  • 33
    • 0032940782 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis in plants: carbon partitioningwithin the cytoplasmic pathway
    • Newman J.D., Chappell J. Isoprenoid biosynthesis in plants: carbon partitioningwithin the cytoplasmic pathway. Crit. Rev. Biochem. Mol. Biol. 1999, 34:95-106.
    • (1999) Crit. Rev. Biochem. Mol. Biol. , vol.34 , pp. 95-106
    • Newman, J.D.1    Chappell, J.2
  • 34
    • 3142575614 scopus 로고    scopus 로고
    • Nutritional regulation of JH synthesis: a mechanism to control reproductive maturation in mosquitoes?
    • Noriega F.G. Nutritional regulation of JH synthesis: a mechanism to control reproductive maturation in mosquitoes?. Insect Biochem. Mol. Biol. 2004, 34:687-693.
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , pp. 687-693
    • Noriega, F.G.1
  • 35
    • 79959784972 scopus 로고    scopus 로고
    • Acoordinated expression of biosynthetic enzyme controls the flux of juvenile hormone precursorsin the corpora allata of mosquitoes
    • Nouzova M., Edwards M.J., Mayoral J.G., Noriega F.G. Acoordinated expression of biosynthetic enzyme controls the flux of juvenile hormone precursorsin the corpora allata of mosquitoes. Insect Biochem. Mol. Biol. 2011, 9:660-669.
    • (2011) Insect Biochem. Mol. Biol. , vol.9 , pp. 660-669
    • Nouzova, M.1    Edwards, M.J.2    Mayoral, J.G.3    Noriega, F.G.4
  • 36
    • 67649472570 scopus 로고    scopus 로고
    • Transmembrane protein topology prediction using support vector machines
    • Nugent T., Jones D.T. Transmembrane protein topology prediction using support vector machines. BMC Bioinform. 2009, 10:159.
    • (2009) BMC Bioinform. , vol.10 , pp. 159
    • Nugent, T.1    Jones, D.T.2
  • 39
    • 38249009566 scopus 로고
    • Differential stimulation of juvenile hormone III biosynthesis induced by mevalonate and mevalonolactone in Blatella germanica (L.)
    • Piulachs M.D., Couillaud F. Differential stimulation of juvenile hormone III biosynthesis induced by mevalonate and mevalonolactone in Blatella germanica (L.). J.Insect Physiol. 1992, 38:555-560.
    • (1992) J.Insect Physiol. , vol.38 , pp. 555-560
    • Piulachs, M.D.1    Couillaud, F.2
  • 40
    • 84865190584 scopus 로고    scopus 로고
    • Aquantitative assay for the juvenile hormone and their precursors using fluorescent tags
    • Rivera-Perez C., Nouzova M., Noriega F.G. Aquantitative assay for the juvenile hormone and their precursors using fluorescent tags. PLoS ONE 2012, 7:e43784.
    • (2012) PLoS ONE , vol.7
    • Rivera-Perez, C.1    Nouzova, M.2    Noriega, F.G.3
  • 41
    • 0025919757 scopus 로고
    • + oxidoreductase in cultured fibroblast
    • + oxidoreductase in cultured fibroblast. J.Clin. Invest. 1991, 88:1643-1648.
    • (1991) J.Clin. Invest. , vol.88 , pp. 1643-1648
    • Rizzo, W.B.1    Craft, D.A.2
  • 42
    • 0033624142 scopus 로고    scopus 로고
    • Sjogren-Larsson syndrome: accumulation of free fatty alcohols in cultured fibroblast and plasma
    • Rizzo W.B., Craft D.A. Sjogren-Larsson syndrome: accumulation of free fatty alcohols in cultured fibroblast and plasma. J.Lipid Res. 2000, 41:1077-1081.
    • (2000) J.Lipid Res. , vol.41 , pp. 1077-1081
    • Rizzo, W.B.1    Craft, D.A.2
  • 43
    • 0035969896 scopus 로고    scopus 로고
    • Fatty aldehyde dehydrogenase: genomic structure, expression and mutation analysis in Sjogren-Larsson syndrome
    • Rizzo W.B., Lin Z., Carney G. Fatty aldehyde dehydrogenase: genomic structure, expression and mutation analysis in Sjogren-Larsson syndrome. Chem. Biol. Interact. 2001, 130-132:297-307.
    • (2001) Chem. Biol. Interact. , pp. 297-307
    • Rizzo, W.B.1    Lin, Z.2    Carney, G.3
  • 45
    • 0142027812 scopus 로고    scopus 로고
    • Juvenile hormone acid methyltransferase: a key regulatory enzyme for insect metamorphosis
    • Shinoda T., Itoyama K. Juvenile hormone acid methyltransferase: a key regulatory enzyme for insect metamorphosis. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:11986-11991.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 11986-11991
    • Shinoda, T.1    Itoyama, K.2
  • 46
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum Parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum Parsimony methods. Mol. Biol. Evol. 2011, 28:2731-2739.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 47
    • 0001198289 scopus 로고
    • Structure and regulation of the corpus allatum
    • Tobe S.S., Stay B. Structure and regulation of the corpus allatum. Adv. Ins. Phys. 1985, 18:305-431.
    • (1985) Adv. Ins. Phys. , vol.18 , pp. 305-431
    • Tobe, S.S.1    Stay, B.2
  • 49
    • 0029143223 scopus 로고
    • Mechanism of farnesol cytotoxicity: further evidence for the role of PKC-dependent signal transduction in farnesol-induced apoptotic cell death
    • Voziyan P.A., Haug J.S., Melnykovych G. Mechanism of farnesol cytotoxicity: further evidence for the role of PKC-dependent signal transduction in farnesol-induced apoptotic cell death. Biochem. Biophys. Res. Commun. 1995, 212:479-486.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 479-486
    • Voziyan, P.A.1    Haug, J.S.2    Melnykovych, G.3


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