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Volumn 121, Issue 2, 1999, Pages 497-506

Successive use of non-host plant proteinase inhibitors required for effective inhibition of Helicoverpa armigera gut proteinases and larval growth

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROPHORESIS; ENZYME ASSAY; ENZYME INHIBITOR; PROTEINASE; TRANSGENIC PLANT;

EID: 0032754118     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.121.2.497     Document Type: Article
Times cited : (137)

References (50)
  • 1
    • 0001364594 scopus 로고    scopus 로고
    • A survey of insecticide resistance in Helicoverpa armigera in the Indian subcontinent
    • Armes NJ, Jadhav DR, DeSouza KR (1996) A survey of insecticide resistance in Helicoverpa armigera in the Indian subcontinent. Bull Entomol Res 86: 499-514
    • (1996) Bull Entomol Res , vol.86 , pp. 499-514
    • Armes, N.J.1    Jadhav, D.R.2    DeSouza, K.R.3
  • 2
    • 0005883206 scopus 로고
    • Extracellular proteinase from Penicillium notatum
    • Belew M, Porath J (1970) Extracellular proteinase from Penicillium notatum. Methods Enzymol 19: 576-581
    • (1970) Methods Enzymol , vol.19 , pp. 576-581
    • Belew, M.1    Porath, J.2
  • 3
    • 33746959991 scopus 로고
    • Colorado potato beetles (Leptinotarsa decemlineata) adapt to proteinase inhibitors induced in potato leaves by methyl jasmonate
    • Bolter CJ, Jongsma MA (1995) Colorado potato beetles (Leptinotarsa decemlineata) adapt to proteinase inhibitors induced in potato leaves by methyl jasmonate. J Insect Physiol 41: 1071-1078
    • (1995) J Insect Physiol , vol.41 , pp. 1071-1078
    • Bolter, C.J.1    Jongsma, M.A.2
  • 4
    • 0027714645 scopus 로고
    • Insect pest control by copying nature using genetically engineered crops
    • Boulter D (1993) Insect pest control by copying nature using genetically engineered crops. Phytochemistry 34: 1453-1466
    • (1993) Phytochemistry , vol.34 , pp. 1453-1466
    • Boulter, D.1
  • 5
    • 0031177988 scopus 로고    scopus 로고
    • Differentially regulated inhibitor-sensitive and insensitive protease genes from the phytophagous insect pest, Helicoverpa armigera, are members of complex multigene families
    • Bown DP, Wilkinson HS, Gatehouse JA (1997) Differentially regulated inhibitor-sensitive and insensitive protease genes from the phytophagous insect pest, Helicoverpa armigera, are members of complex multigene families. Insect Biochem Mol Biol 27: 625-638
    • (1997) Insect Biochem Mol Biol , vol.27 , pp. 625-638
    • Bown, D.P.1    Wilkinson, H.S.2    Gatehouse, J.A.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principal of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0000668775 scopus 로고
    • Are insects resistant to plant proteinase inhibitors?
    • Broadway RM (1995) Are insects resistant to plant proteinase inhibitors? J Insect Physiol 41: 107-116
    • (1995) J Insect Physiol , vol.41 , pp. 107-116
    • Broadway, R.M.1
  • 8
    • 0002338378 scopus 로고    scopus 로고
    • Dietary proteinase inhibitors alter complement of midgut proteases
    • Broadway RM (1996) Dietary proteinase inhibitors alter complement of midgut proteases. Arch Insect Biochem Physiol 32: 39-53
    • (1996) Arch Insect Biochem Physiol , vol.32 , pp. 39-53
    • Broadway, R.M.1
  • 9
    • 0031238904 scopus 로고    scopus 로고
    • Dietary regulation of serine proteinases that are resistant to serine proteinase inhibitors
    • Broadway RM (1997) Dietary regulation of serine proteinases that are resistant to serine proteinase inhibitors. J Insect Physiol 43: 855-874
    • (1997) J Insect Physiol , vol.43 , pp. 855-874
    • Broadway, R.M.1
  • 10
    • 0001260377 scopus 로고
    • Plant proteinase inhibitors: Mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua
    • Broadway RM, Duffey SS (1986) Plant proteinase inhibitors: mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua. J Insect Physiol 32: 827-833
    • (1986) J Insect Physiol , vol.32 , pp. 827-833
    • Broadway, R.M.1    Duffey, S.S.2
  • 11
    • 0019967719 scopus 로고
    • Proteolytic activity of rumen microorganisms and effect of proteinase inhibitors
    • Brock RM, Forsberg CW, Buchanan-Smith JG (1982) Proteolytic activity of rumen microorganisms and effect of proteinase inhibitors. Appl Environ Microbiol 44: 561-569
    • (1982) Appl Environ Microbiol , vol.44 , pp. 561-569
    • Brock, R.M.1    Forsberg, C.W.2    Buchanan-Smith, J.G.3
  • 12
    • 0001185115 scopus 로고
    • The interaction of a range of serine proteinase inhibitors with bovine trypsin and Costelytra zealandica trypsin
    • Christeller JT, Shaw BD (1989) The interaction of a range of serine proteinase inhibitors with bovine trypsin and Costelytra zealandica trypsin. Insect Biochem 19: 233-241
    • (1989) Insect Biochem , vol.19 , pp. 233-241
    • Christeller, J.T.1    Shaw, B.D.2
  • 13
    • 0000051893 scopus 로고    scopus 로고
    • Opposite effects on Spodoptera littoralis larvae of high expression level of a trypsin proteinase inhibitor in transgenic plants
    • DeLeo F, Bonade-Bottino MA, Ceci LR, Gallerani R, Jouanin L (1998) Opposite effects on Spodoptera littoralis larvae of high expression level of a trypsin proteinase inhibitor in transgenic plants. Plant Physiol 118: 997-1004
    • (1998) Plant Physiol , vol.118 , pp. 997-1004
    • DeLeo, F.1    Bonade-Bottino, M.A.2    Ceci, L.R.3    Gallerani, R.4    Jouanin, L.5
  • 14
    • 0000651050 scopus 로고
    • Butterflies and plants: A study in evolution
    • Ehrlich PR, Raven PH (1964) Butterflies and plants: a study in evolution. Evolution 18: 586-608
    • (1964) Evolution , vol.18 , pp. 586-608
    • Ehrlich, P.R.1    Raven, P.H.2
  • 15
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger BF, Kokowesky N, Cohen W (1964) The preparation and properties of two new chromogenic substrates of trypsin. Arch Biochem Biophys 95: 271-278
    • (1964) Arch Biochem Biophys , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowesky, N.2    Cohen, W.3
  • 16
    • 0031014713 scopus 로고    scopus 로고
    • Activity staining of protein inhibitors of proteases on gelatin containing polyacrylamide gel electrophoresis
    • Felicioli R, Garzelli B, Vaccari L, Melfi D, Balestreri E (1997) Activity staining of protein inhibitors of proteases on gelatin containing polyacrylamide gel electrophoresis. Anal Biochem 244: 176-178
    • (1997) Anal Biochem , vol.244 , pp. 176-178
    • Felicioli, R.1    Garzelli, B.2    Vaccari, L.3    Melfi, D.4    Balestreri, E.5
  • 17
  • 20
    • 0031984542 scopus 로고    scopus 로고
    • Amylase inhibitors of pigeonpea (Cajanus cajan L.) seeds
    • Giri AP, Kachole MS (1998) Amylase inhibitors of pigeonpea (Cajanus cajan L.) seeds. Phytochemistry 47: 197-202
    • (1998) Phytochemistry , vol.47 , pp. 197-202
    • Giri, A.P.1    Kachole, M.S.2
  • 21
    • 0001068883 scopus 로고
    • Wound induced proteinase inhibitor in plant leaves: A possible defence mechanism
    • Green TR, Ryan CA (1972) Wound induced proteinase inhibitor in plant leaves: a possible defence mechanism. Science 175: 776-777
    • (1972) Science , vol.175 , pp. 776-777
    • Green, T.R.1    Ryan, C.A.2
  • 22
    • 0031807040 scopus 로고    scopus 로고
    • Characterization of Helicoverpa armigera gut proteinases and their interaction with proteinase inhibitors using gel-X-ray film contact print technique
    • Harsulkar AM, Giri AP, Gupta VS, Sainani MN, Deshpande VV, Patankar AG, Ranjekar PK (1998) Characterization of Helicoverpa armigera gut proteinases and their interaction with proteinase inhibitors using gel-X-ray film contact print technique. Electrophoresis 19: 1397-1402
    • (1998) Electrophoresis , vol.19 , pp. 1397-1402
    • Harsulkar, A.M.1    Giri, A.P.2    Gupta, V.S.3    Sainani, M.N.4    Deshpande, V.V.5    Patankar, A.G.6    Ranjekar, P.K.7
  • 23
    • 0000334222 scopus 로고
    • Transgenic plants conferring insect tolerance: Proteinase inhibitor approach
    • SD Kung, R Wu, eds, Academic Press, San Diego
    • Hilder VA, Gatehouse MR, Boulter D (1993) Transgenic plants conferring insect tolerance: proteinase inhibitor approach. In SD Kung, R Wu, eds, Transgenic Plants, Vol 1. Engineering and Utilization. Academic Press, San Diego, pp 317-338
    • (1993) Transgenic Plants, Vol 1. Engineering and Utilization , vol.1 , pp. 317-338
    • Hilder, V.A.1    Gatehouse, M.R.2    Boulter, D.3
  • 24
    • 0030293867 scopus 로고    scopus 로고
    • An octadecanoid pathway mutant (JL5) of tomato is compromised in signaling for defense against insect attack
    • Howe GA, Lightner J, Browse J, Ryan CA (1996) An octadecanoid pathway mutant (JL5) of tomato is compromised in signaling for defense against insect attack. Plant Cell 8: 2067-2077
    • (1996) Plant Cell , vol.8 , pp. 2067-2077
    • Howe, G.A.1    Lightner, J.2    Browse, J.3    Ryan, C.A.4
  • 25
    • 0030160355 scopus 로고    scopus 로고
    • Protective mechanism of the Mexican bean weevil against high levels of α-amylase inhibitor in the common bean
    • Ishimoto M, Chrispeels MJ (1996) Protective mechanism of the Mexican bean weevil against high levels of α-amylase inhibitor in the common bean. Plant Physiol 111: 393-401
    • (1996) Plant Physiol , vol.111 , pp. 393-401
    • Ishimoto, M.1    Chrispeels, M.J.2
  • 26
    • 0000371962 scopus 로고
    • When is it coevolution?
    • Janzen DH (1980) When is it coevolution? Evolution 34: 611-612
    • (1980) Evolution , vol.34 , pp. 611-612
    • Janzen, D.H.1
  • 27
    • 0001669768 scopus 로고
    • The partial purification and characterisation of serine protease activity in midgut of larval Helicoverpa armigera
    • Johnston KA, Lee MJ, Gatehouse JA, Anstee JH (1991) The partial purification and characterisation of serine protease activity in midgut of larval Helicoverpa armigera. Insect Biochem 21:389-397
    • (1991) Insect Biochem , vol.21 , pp. 389-397
    • Johnston, K.A.1    Lee, M.J.2    Gatehouse, J.A.3    Anstee, J.H.4
  • 28
    • 0029128219 scopus 로고
    • Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of gut proteinase activity insensitive to inhibition
    • Jongsma MA, Bakker PL, Peters J, Bosch D, Stiekema WJ (1995) Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of gut proteinase activity insensitive to inhibition. Proc Natl Acad Sci USA 92: 8041-8045
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8041-8045
    • Jongsma, M.A.1    Bakker, P.L.2    Peters, J.3    Bosch, D.4    Stiekema, W.J.5
  • 29
    • 0031260101 scopus 로고    scopus 로고
    • The adaptation of insects to plant protease inhibitors
    • Jongsma MA, Bolter CJ (1997) The adaptation of insects to plant protease inhibitors. J Insect Physiol 43: 885-895
    • (1997) J Insect Physiol , vol.43 , pp. 885-895
    • Jongsma, M.A.1    Bolter, C.J.2
  • 30
    • 0030248562 scopus 로고    scopus 로고
    • Combating inhibitor-insensitive proteases of insect pests
    • Jongsma MA, Stiekema WJ, Bosch D (1996) Combating inhibitor-insensitive proteases of insect pests. Trends Biotech 14: 331-333
    • (1996) Trends Biotech , vol.14 , pp. 331-333
    • Jongsma, M.A.1    Stiekema, W.J.2    Bosch, D.3
  • 32
    • 0343230391 scopus 로고    scopus 로고
    • Low trypsin and chymotrypsin inhibitors mutants in winged bean (Psophocarpus tetragonolobus [L.] D.C.)
    • Kothekar VS, Harsulkar AM, Khandelwal AR (1996) Low trypsin and chymotrypsin inhibitors mutants in winged bean (Psophocarpus tetragonolobus [L.] D.C.). J Sci Food Agric 71: 137-140
    • (1996) J Sci Food Agric , vol.71 , pp. 137-140
    • Kothekar, V.S.1    Harsulkar, A.M.2    Khandelwal, A.R.3
  • 36
    • 0031030737 scopus 로고    scopus 로고
    • Avoiding protease-mediated resistance in herbivorous pests
    • Michaud D (1997) Avoiding protease-mediated resistance in herbivorous pests. Trends Biotechnol 15: 4-6
    • (1997) Trends Biotechnol , vol.15 , pp. 4-6
    • Michaud, D.1
  • 37
    • 0029084013 scopus 로고
    • Carboxy-terminal truncation of oryzacystatin II by oryzacystatin-insensitive insect digestive proteinases
    • Michaud D, Cantin L, Vrain TC (1995) Carboxy-terminal truncation of oryzacystatin II by oryzacystatin-insensitive insect digestive proteinases. Arch Biochem Biophys 322: 469-474
    • (1995) Arch Biochem Biophys , vol.322 , pp. 469-474
    • Michaud, D.1    Cantin, L.2    Vrain, T.C.3
  • 38
    • 0029682164 scopus 로고    scopus 로고
    • Response of digestive cysteine proteinases from the Colorado potato beetle (Leptinotarsa decemlineata) and the black vine weevil (Otiorynchus sulcatus) to a recombinant form of human stefin A
    • Michaud D, Nguyen-Quoc B, Vrain TC, Fong D, Yelle S (1996) Response of digestive cysteine proteinases from the Colorado potato beetle (Leptinotarsa decemlineata) and the black vine weevil (Otiorynchus sulcatus) to a recombinant form of human stefin A. Arch Insect Biochem Physiol 31: 451-464
    • (1996) Arch Insect Biochem Physiol , vol.31 , pp. 451-464
    • Michaud, D.1    Nguyen-Quoc, B.2    Vrain, T.C.3    Fong, D.4    Yelle, S.5
  • 39
    • 84986522574 scopus 로고
    • Isolation and characterization of two trypsin-chymotrypsin inhibitors from lentil seeds (Lens culinaris Medik)
    • Mueller R, Weder JKP (1989) Isolation and characterization of two trypsin-chymotrypsin inhibitors from lentil seeds (Lens culinaris Medik). J Food Biochem 13: 39-63
    • (1989) J Food Biochem , vol.13 , pp. 39-63
    • Mueller, R.1    Weder, J.K.P.2
  • 40
    • 0030764154 scopus 로고    scopus 로고
    • Proteinase-mediated insect resistance to Bacillus thuringiensis toxins
    • Oppert B, Kramer KJ, Beeman RW, Johnson D, McGaughey WH (1997) Proteinase-mediated insect resistance to Bacillus thuringiensis toxins. J Biol Chem 272: 23473-23476
    • (1997) J Biol Chem , vol.272 , pp. 23473-23476
    • Oppert, B.1    Kramer, K.J.2    Beeman, R.W.3    Johnson, D.4    McGaughey, W.H.5
  • 41
    • 0030159151 scopus 로고    scopus 로고
    • Luminal proteinases from Plodia interpunctella and the hydrolysis of Bacillus thuringiensis CryIA(c) protoxin
    • Oppert B, Kramer KJ, Johnson D, Upton SJ, McGaughey WH (1996) Luminal proteinases from Plodia interpunctella and the hydrolysis of Bacillus thuringiensis CryIA(c) protoxin. Insect Biochem Mol Biol 26: 571-583
    • (1996) Insect Biochem Mol Biol , vol.26 , pp. 571-583
    • Oppert, B.1    Kramer, K.J.2    Johnson, D.3    Upton, S.J.4    McGaughey, W.H.5
  • 42
    • 0000259353 scopus 로고
    • Inhibition of Diabrotica larval growth by a multicystatin from potato tubers
    • Orr GL, Strickland JA, Walsh TA (1994) Inhibition of Diabrotica larval growth by a multicystatin from potato tubers. J Insect Physiol 40: 893-900
    • (1994) J Insect Physiol , vol.40 , pp. 893-900
    • Orr, G.L.1    Strickland, J.A.2    Walsh, T.A.3
  • 43
    • 0032863351 scopus 로고    scopus 로고
    • Diversity in inhibitors of trypsin and Helicoverpa armigera gut proteinases in chickpea (Cicer arietinum L.) and its wild relatives
    • Patankar AG, Harsulkar AM, Giri AP, Gupta VS, Sainani MN, Ranjekar PK, Deshpande VV (1999) Diversity in inhibitors of trypsin and Helicoverpa armigera gut proteinases in chickpea (Cicer arietinum L.) and its wild relatives. Theor Appl Genet 99: 719-726
    • (1999) Theor Appl Genet , vol.99 , pp. 719-726
    • Patankar, A.G.1    Harsulkar, A.M.2    Giri, A.P.3    Gupta, V.S.4    Sainani, M.N.5    Ranjekar, P.K.6    Deshpande, V.V.7
  • 44
    • 0028273981 scopus 로고
    • Detection of electrophoretically separated proteinase inhibitors using X-ray film
    • Pichare MM, Kachole MS (1994) Detection of electrophoretically separated proteinase inhibitors using X-ray film. J Biochem Biophys Methods 28: 215-224
    • (1994) J Biochem Biophys Methods , vol.28 , pp. 215-224
    • Pichare, M.M.1    Kachole, M.S.2
  • 46
    • 0000180578 scopus 로고
    • Proteinase inhibitors in plants: Genes for improving defenses against insect and pathogens
    • Ryan CA (1990) Proteinase inhibitors in plants: Genes for improving defenses against insect and pathogens. Annu Rev Phytopathol 28: 425-449
    • (1990) Annu Rev Phytopathol , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 48
    • 0032486466 scopus 로고    scopus 로고
    • Proteolytic enzymes from larvae of the fire ant, Solenopsis invicta: Isolation and characterization of four serine proteinases
    • Whitworth ST, Blum MS, Travis J (1998) Proteolytic enzymes from larvae of the fire ant, Solenopsis invicta: isolation and characterization of four serine proteinases. J Biol Chem 273: 14430-14434
    • (1998) J Biol Chem , vol.273 , pp. 14430-14434
    • Whitworth, S.T.1    Blum, M.S.2    Travis, J.3
  • 49
    • 0001285211 scopus 로고    scopus 로고
    • Adaptation of Helicoverpa armigera (Lepidoptera:Noctuidae) to a proteinase inhibitor expressed in transgenic tobacco
    • Wu Y, Llewellyn D, Mathews A, Dennis ES (1997) Adaptation of Helicoverpa armigera (Lepidoptera:Noctuidae) to a proteinase inhibitor expressed in transgenic tobacco. Mol Breeding 3: 371-380
    • (1997) Mol Breeding , vol.3 , pp. 371-380
    • Wu, Y.1    Llewellyn, D.2    Mathews, A.3    Dennis, E.S.4


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