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Volumn 28, Issue 12, 1998, Pages 935-945

Biochemical analysis of a blood meal-induced Aedes aegypti glutamine synthetase gene

Author keywords

Aedes aegypti; Midgut glutamine synthetase; Peritrophic matrix

Indexed keywords

COMPLEMENTARY DNA; ENZYME INHIBITOR; GLUTAMATE AMMONIA LIGASE; METHIONINE SULFOXIMINE;

EID: 0032436037     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0965-1748(98)00073-3     Document Type: Article
Times cited : (26)

References (52)
  • 3
    • 0017669931 scopus 로고
    • Autogenous regulation of the synthesis of glutamine synthetase in Klebsiella aerogenes
    • Bender R.A., Magasanik B. Autogenous regulation of the synthesis of glutamine synthetase in Klebsiella aerogenes. J. Bacteriol. 132:1977;106-112.
    • (1977) J. Bacteriol. , vol.132 , pp. 106-112
    • Bender, R.A.1    Magasanik, B.2
  • 4
    • 0020756652 scopus 로고
    • Peritrophic membranes and protease activity in the midgut of the malaria mosquito, Anopheles stephensi (Liston) (Insecta: Diptera) under normal and experimental conditions
    • Berner R., Rudin W., Hecker H. Peritrophic membranes and protease activity in the midgut of the malaria mosquito, Anopheles stephensi (Liston) (Insecta: Diptera) under normal and experimental conditions. J. Ultrastruc. Res. 83:1983;195-204.
    • (1983) J. Ultrastruc. Res. , vol.83 , pp. 195-204
    • Berner, R.1    Rudin, W.2    Hecker, H.3
  • 5
    • 0000003821 scopus 로고
    • The midgut ultrastructure of hematophagous insects
    • Billingsley P.F. The midgut ultrastructure of hematophagous insects. Annu. Rev. Entomol. 35:1990;219-248.
    • (1990) Annu. Rev. Entomol. , vol.35 , pp. 219-248
    • Billingsley, P.F.1
  • 6
    • 0026250976 scopus 로고
    • Blood digestion in the mosquito, Anopheles stephensi Liston (Diptera: Culicidae): Activity and distribution of trypsin, aminopeptidase, and alpha-glucosidase in the midgut
    • Billingsley P.F., Hecker H. Blood digestion in the mosquito, Anopheles stephensi Liston (Diptera: Culicidae): activity and distribution of trypsin, aminopeptidase, and alpha-glucosidase in the midgut. J. Med. Entomol. 28:1991;865-871.
    • (1991) J. Med. Entomol. , vol.28 , pp. 865-871
    • Billingsley, P.F.1    Hecker, H.2
  • 7
    • 0028708679 scopus 로고
    • Genetic, molecular and developmental analysis of the glutamine synthetase isozymes of Drosophila melanogaster
    • Caggese C., Barsanti P., Viggiano L., Bozzetti M.P., Caizzi R. Genetic, molecular and developmental analysis of the glutamine synthetase isozymes of Drosophila melanogaster. Genetica. 94:1994;275-281.
    • (1994) Genetica , vol.94 , pp. 275-281
    • Caggese, C.1    Barsanti, P.2    Viggiano, L.3    Bozzetti, M.P.4    Caizzi, R.5
  • 8
    • 0025271344 scopus 로고
    • Homologous nuclear genes encode cytoplasmic and mitochondrial glutamine synthetase in Drosophila melanogaster
    • Caizzi R., Bozzetti M.P., Caggese C., Ritossa F. Homologous nuclear genes encode cytoplasmic and mitochondrial glutamine synthetase in Drosophila melanogaster. J. Mol. Biol. 212:1990;17-26.
    • (1990) J. Mol. Biol. , vol.212 , pp. 17-26
    • Caizzi, R.1    Bozzetti, M.P.2    Caggese, C.3    Ritossa, F.4
  • 9
    • 0023664018 scopus 로고
    • Comparison of the consensus sequence flanking translational start sites in Drosophila and vertebrates
    • Cavener D.R. Comparison of the consensus sequence flanking translational start sites in Drosophila and vertebrates. Nucleic Acids Res. 15:1987;1353-1361.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 1353-1361
    • Cavener, D.R.1
  • 10
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • ChoMcZynski, P.1    Sacchi, N.2
  • 11
    • 0002272352 scopus 로고
    • Brugia pahangi: Exsheathment and midgut penetration in Aedes aegypti
    • Christensen B.M., Sutherland D.R. Brugia pahangi: exsheathment and midgut penetration in Aedes aegypti. Trans. Am. Microsc. Soc. 103:1984;423-433.
    • (1984) Trans. Am. Microsc. Soc. , vol.103 , pp. 423-433
    • Christensen, B.M.1    Sutherland, D.R.2
  • 13
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereaux J.P., Gaeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:1984;387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereaux, J.P.1    Gaeberli, P.2    Smithies, O.3
  • 14
    • 0013533430 scopus 로고
    • Subcellular fractionation of fleshfly flight muscle in attempts to isolate synaptosomes and to establish the location of glutamate enzymes.
    • Donnellan J.F., Jenner D.W., Ramsey A. Subcellular fractionation of fleshfly flight muscle in attempts to isolate synaptosomes and to establish the location of glutamate enzymes. Insect Biochem. 4:1974;243-265.
    • (1974) Insect Biochem. , vol.4 , pp. 243-265
    • Donnellan, J.F.1    Jenner, D.W.2    Ramsey, A.3
  • 15
    • 0000516891 scopus 로고
    • Purification and properties of glutamine synthetase from fleshfly flight muscle
    • Dowton M., Kennedy I.R. Purification and properties of glutamine synthetase from fleshfly flight muscle. Insect Biochem. 15:1985;763-770.
    • (1985) Insect Biochem. , vol.15 , pp. 763-770
    • Dowton, M.1    Kennedy, I.R.2
  • 16
    • 0030152880 scopus 로고    scopus 로고
    • Mosquito dopa decarboxylase cDNA characterization and blood-meal-induced ovarian expression
    • Ferdig M.T., Li J., Severson D.W., Christensen B.M. Mosquito dopa decarboxylase cDNA characterization and blood-meal-induced ovarian expression. Insect Mol. Biol. 5:1996;119-126.
    • (1996) Insect Mol. Biol. , vol.5 , pp. 119-126
    • Ferdig, M.T.1    Li, J.2    Severson, D.W.3    Christensen, B.M.4
  • 17
    • 0013533431 scopus 로고
    • The prerequisites for the formation of a peritrophic membrane in Culicidae family
    • Freyvogel T.A., Jaquet C. The prerequisites for the formation of a peritrophic membrane in Culicidae family. Acta Trop. 22:1965;148-154.
    • (1965) Acta Trop. , vol.22 , pp. 148-154
    • Freyvogel, T.A.1    Jaquet, C.2
  • 18
    • 0001119092 scopus 로고
    • The formation of peritrophic membranes in Culicidae
    • Freyvogel T.A., Staubli W. The formation of peritrophic membranes in Culicidae. Acta Trop. 22:1965;118-147.
    • (1965) Acta Trop. , vol.22 , pp. 118-147
    • Freyvogel, T.A.1    Staubli, W.2
  • 20
    • 0022501578 scopus 로고
    • Mosquito trypsin: Immunocytochemical localization in the midgut of blood-fed Aedes aegypti (L.)
    • Graf R., Raikhel A.S., Brown M.R., Lea A.O., Briegel H. Mosquito trypsin: immunocytochemical localization in the midgut of blood-fed Aedes aegypti (L.). Cell & Tissue Res. 245:1986;19-27.
    • (1986) Cell & Tissue Res. , vol.245 , pp. 19-27
    • Graf, R.1    Raikhel, A.S.2    Brown, M.R.3    Lea, A.O.4    Briegel, H.5
  • 21
    • 0025857170 scopus 로고
    • Malaria parasite chitinase and penetration of the mosquito peritrophic membrane
    • Huber M., Cabib E., Miller L.H. Malaria parasite chitinase and penetration of the mosquito peritrophic membrane. Proc. Natl Acad. Sci. USA. 88:1991;2807-2810.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2807-2810
    • Huber, M.1    Cabib, E.2    Miller, L.H.3
  • 22
    • 0016423816 scopus 로고
    • Metal ion requirement by glutamine synthetase of Escherichia coli in catalysis of gamma-glutamyl transfer
    • Hunt J.B., Smyrniotis P.Z., Ginsburg A., Stadtman E.R. Metal ion requirement by glutamine synthetase of Escherichia coli in catalysis of gamma-glutamyl transfer. Arch. Biochem. Biophys. 166:1975;102-124.
    • (1975) Arch. Biochem. Biophys. , vol.166 , pp. 102-124
    • Hunt, J.B.1    Smyrniotis, P.Z.2    Ginsburg, A.3    Stadtman, E.R.4
  • 23
    • 0021964151 scopus 로고
    • Primary structure of peptides from bovine brain glutamine synthetase: Comparison with sequences of glutamine synthetases from other organisms
    • Johnson R.J., Piskiewicz D. Primary structure of peptides from bovine brain glutamine synthetase: comparison with sequences of glutamine synthetases from other organisms. Biochim. Biophys. Acta. 827:1985;439-446.
    • (1985) Biochim. Biophys. Acta , vol.827 , pp. 439-446
    • Johnson, R.J.1    Piskiewicz, D.2
  • 24
    • 0023832094 scopus 로고
    • Sequence of peptides from Saccharomyces cerevisiae glutamine synthetase N-terminal peptide and ATP-binding domain
    • Kim K.H., Rhee S.G. Sequence of peptides from Saccharomyces cerevisiae glutamine synthetase N-terminal peptide and ATP-binding domain. J. Biol. Chem. 263:1988;833-838.
    • (1988) J. Biol. Chem. , vol.263 , pp. 833-838
    • Kim, K.H.1    Rhee, S.G.2
  • 25
    • 0023665902 scopus 로고
    • An analysis of 5′-coding sequences from 699 vertebrate messenger RNA′s
    • Kozak M. An analysis of 5′-coding sequences from 699 vertebrate messenger RNA′s. Nucleic Acids Res. 15:1987;8125-8148.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125-8148
    • Kozak, M.1
  • 26
    • 0025452262 scopus 로고
    • Substitute blood meal for investigating and maintaining Aedes aegypti (Diptera; Culicidae)
    • Kogan P.H. Substitute blood meal for investigating and maintaining Aedes aegypti (Diptera; Culicidae). J. Med. Entomol. 27:1990;709-712.
    • (1990) J. Med. Entomol. , vol.27 , pp. 709-712
    • Kogan, P.H.1
  • 27
    • 0024380839 scopus 로고
    • Mouse glutamine synthetase is encoded by a single gene that can be expressed in a localized fashion
    • Kuo C.F., Darnell J.E. Jr. Mouse glutamine synthetase is encoded by a single gene that can be expressed in a localized fashion. J. Mol. Biol. 208:1989;45-56.
    • (1989) J. Mol. Biol. , vol.208 , pp. 45-56
    • Kuo, C.F.1    Darnell J.E., Jr.2
  • 28
    • 85052779910 scopus 로고
    • Glutamine synthetase
    • E. Kvamme (Ed.) CRC Press, Boca Raton, FL
    • Cooper, A.J.L., 1988. Glutamine synthetase. In: Glutamine and Glutamate in Mammals, vol. 1. E. Kvamme (Ed.) CRC Press, Boca Raton, FL, pp. 7-31.
    • (1988) In: Glutamine and Glutamate in Mammals , vol.1 , pp. 7-31
    • Cooper, A.J.L.1
  • 29
    • 0022555842 scopus 로고
    • Complex transcriptional units: Diversity in gene expression by alternative RNA processing
    • Leff S.E., Rosenfeld M.G. Complex transcriptional units: diversity in gene expression by alternative RNA processing. Ann. Rev. Biochem. 55:1986;1353-1361.
    • (1986) Ann. Rev. Biochem. , vol.55 , pp. 1353-1361
    • Leff, S.E.1    Rosenfeld, M.G.2
  • 30
    • 0001453426 scopus 로고
    • Reversibility of the enzymatic synthesis of glutamine
    • Levintow L., Meister A. Reversibility of the enzymatic synthesis of glutamine. J. Biol. Chem. 209:1954;265.
    • (1954) J. Biol. Chem. , vol.209 , pp. 265
    • Levintow, L.1    Meister, A.2
  • 31
    • 0017859652 scopus 로고
    • Carbamoylphosphate synthetase I of rat-liver mitochondria
    • Lusty C.J. Carbamoylphosphate synthetase I of rat-liver mitochondria. Eur. J. Biochem. 85:1978;373-383.
    • (1978) Eur. J. Biochem. , vol.85 , pp. 373-383
    • Lusty, C.J.1
  • 34
    • 0023902475 scopus 로고
    • Polyadenylation of mRNA precursors
    • Manley J.L. Polyadenylation of mRNA precursors. Biochim. Biophys. Acta. 950:1988;1-12.
    • (1988) Biochim. Biophys. Acta , vol.950 , pp. 1-12
    • Manley, J.L.1
  • 35
    • 0014526454 scopus 로고
    • Identification of L-methionine S-sulfoximine as the diastereoisomer of L-methionine SR-sulfoximine that inhibits glutamine synthetase
    • Manning J.M., Moore S., Rowe W.B., Meister A. Identification of L-methionine S-sulfoximine as the diastereoisomer of L-methionine SR-sulfoximine that inhibits glutamine synthetase. Biochemistry. 8:1969;2681-2685.
    • (1969) Biochemistry , vol.8 , pp. 2681-2685
    • Manning, J.M.1    Moore, S.2    Rowe, W.B.3    Meister, A.4
  • 36
    • 0022903413 scopus 로고
    • Microfilarial perforation of the midgut of a mosquito
    • Perrone J.B., Spielman A. Microfilarial perforation of the midgut of a mosquito. J. Parasitol. 72:1986;723-727.
    • (1986) J. Parasitol. , vol.72 , pp. 723-727
    • Perrone, J.B.1    Spielman, A.2
  • 37
    • 0023947408 scopus 로고
    • Time and site of assembly of the peritrophic membrane of the mosquito Aedes aegypti
    • Perrone J.B., Spielman A. Time and site of assembly of the peritrophic membrane of the mosquito Aedes aegypti. Cell Tissue Res. 252:1988;473-478.
    • (1988) Cell Tissue Res. , vol.252 , pp. 473-478
    • Perrone, J.B.1    Spielman, A.2
  • 38
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by the endoplasmic reticulum and golgi
    • Pfeffer S.R., Rothman J.E. Biosynthetic protein transport and sorting by the endoplasmic reticulum and golgi. Ann. Rev. Biochem. 56:1987;829-852.
    • (1987) Ann. Rev. Biochem. , vol.56 , pp. 829-852
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 39
    • 0024420362 scopus 로고
    • The structure of the chicken glutamine synthetase-encoding gene
    • Pu H.F., Young A.P. The structure of the chicken glutamine synthetase-encoding gene. Gene. 81:1989;169-175.
    • (1989) Gene , vol.81 , pp. 169-175
    • Pu, H.F.1    Young, A.P.2
  • 40
    • 0015517893 scopus 로고
    • The formation of the peritrophic membrane in adult Aedes triseriatus (Say) (Diptera: Culicidae)
    • Richardson M.W., Romoser W.S. The formation of the peritrophic membrane in adult Aedes triseriatus (Say) (Diptera: Culicidae). J. Med. Entomol. 9:1972;495-500.
    • (1972) J. Med. Entomol. , vol.9 , pp. 495-500
    • Richardson, M.W.1    Romoser, W.S.2
  • 41
    • 0014528061 scopus 로고
    • Preparation and studies on the characterization of sheep brain glutamine synthetase
    • Ronzio R.A., Wilk S., Rowe W.B., Meister A. Preparation and studies on the characterization of sheep brain glutamine synthetase. Biochemistry. 8:1969;2670-2674.
    • (1969) Biochemistry , vol.8 , pp. 2670-2674
    • Ronzio, R.A.1    Wilk, S.2    Rowe, W.B.3    Meister, A.4
  • 42
    • 0015919544 scopus 로고
    • Studies on the inhibition of glutamine synthetase by methionine sulfone
    • Rowe W.B., Meister A. Studies on the inhibition of glutamine synthetase by methionine sulfone. Biochemistry. 12:1973;1578-1582.
    • (1973) Biochemistry , vol.12 , pp. 1578-1582
    • Rowe, W.B.1    Meister, A.2
  • 43
    • 0014525407 scopus 로고
    • Inhibition of glutamine synthetase by methionine sulfoximine: Studies on methionine sulfoximine phosphate
    • Rowe W.B., Ronzio R.A., Meister A. Inhibition of glutamine synthetase by methionine sulfoximine: studies on methionine sulfoximine phosphate. Biochemistry. 8:1969;2674-2680.
    • (1969) Biochemistry , vol.8 , pp. 2674-2680
    • Rowe, W.B.1    Ronzio, R.A.2    Meister, A.3
  • 44
    • 0000213932 scopus 로고
    • Studies on the feeding response of mosquitoes to nutritive solutions in a new membrane feeder
    • Rutledge L.C., Ward R.A., Gould D.J. Studies on the feeding response of mosquitoes to nutritive solutions in a new membrane feeder. Mosquito News. 24:1964;407-419.
    • (1964) Mosquito News , vol.24 , pp. 407-419
    • Rutledge, L.C.1    Ward, R.A.2    Gould, D.J.3
  • 45
    • 0027308860 scopus 로고
    • Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease
    • Shahabuddin M., Toyoshima T., Aikawa M., Kaslow D.C. Transmission-blocking activity of a chitinase inhibitor and activation of malarial parasite chitinase by mosquito protease. Proc. Natl Acad. Sci. USA. 90:1993;4266-4270.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4266-4270
    • Shahabuddin, M.1    Toyoshima, T.2    Aikawa, M.3    Kaslow, D.C.4
  • 46
    • 0014199244 scopus 로고
    • Regulation of glutamine synthetase, IX. Reactivity of the sulfhydryl groups of the enzyme from Escherichia coli
    • Shapiro B.M., Stadtman E.R. Regulation of glutamine synthetase, IX. Reactivity of the sulfhydryl groups of the enzyme from Escherichia coli. J. Biol. Chem. 242:1967;5069-5079.
    • (1967) J. Biol. Chem. , vol.242 , pp. 5069-5079
    • Shapiro, B.M.1    Stadtman, E.R.2
  • 48
    • 0020123367 scopus 로고
    • The biosynthetic pathway of the asparagine-linked oligosaccharides of glycoproteins
    • Staneloni R.J., Leloir L.F. The biosynthetic pathway of the asparagine-linked oligosaccharides of glycoproteins. Crit. Rev. Biochem. 12:1982;289-326.
    • (1982) Crit. Rev. Biochem. , vol.12 , pp. 289-326
    • Staneloni, R.J.1    Leloir, L.F.2
  • 49
    • 0027171548 scopus 로고
    • CDNA clones from the olfactory organ of the spiny lobster encode a protein related to eukaryotic glutamine synthetase
    • Trapido-Rosenthal H.G., Linser P.J., Greenberg R.M., Gleeson R.A., Carr W.E. cDNA clones from the olfactory organ of the spiny lobster encode a protein related to eukaryotic glutamine synthetase. Gene. 129:1993;275-278.
    • (1993) Gene , vol.129 , pp. 275-278
    • Trapido-Rosenthal, H.G.1    Linser, P.J.2    Greenberg, R.M.3    Gleeson, R.A.4    Carr, W.E.5
  • 51
    • 0015864754 scopus 로고
    • St. Louis encephalitis virus: An ultrastructural study of infection in a mosquito vector
    • Whitfield S.G., Murphy F.A., Sudia W.D. St. Louis encephalitis virus: an ultrastructural study of infection in a mosquito vector. Virology. 56:1973;70-87.
    • (1973) Virology , vol.56 , pp. 70-87
    • Whitfield, S.G.1    Murphy, F.A.2    Sudia, W.D.3
  • 52
    • 0021673231 scopus 로고
    • Role of the conserved AAUAAA sequence: Four AAUAAA point mutants prevent messenger RNA 3′end formation
    • Wickens M., Stephenson P. Role of the conserved AAUAAA sequence: four AAUAAA point mutants prevent messenger RNA 3′end formation. Science. 226:1984;1045-1051.
    • (1984) Science , vol.226 , pp. 1045-1051
    • Wickens, M.1    Stephenson, P.2


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