메뉴 건너뛰기




Volumn 56, Issue 20, 2008, Pages 9404-9409

Trypsin inhibitors in passion fruit (Passiflora f. edulis flavicarpa) leaves: Accumulation in response to methyl jasmonate, mechanical wounding, and herbivory

Author keywords

Herbivory; Kunitz; Methyl jasmonate; Passion fruit; Trypsin inhibitor; Wound response

Indexed keywords

ACETIC ACID DERIVATIVE; CYCLOPENTANE DERIVATIVE; JASMONIC ACID METHYL ESTER; OXYLIPIN; PLANT EXTRACT; TRYPSIN INHIBITOR; VEGETABLE PROTEIN;

EID: 55549113239     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf8013266     Document Type: Article
Times cited : (25)

References (44)
  • 1
    • 34848897179 scopus 로고    scopus 로고
    • An update on biosynthesis, signal transduction and action in plant stress response, growth and development
    • Wasternack, C. Jasmonates: An update on biosynthesis, signal transduction and action in plant stress response, growth and development. Ann. Bot. 2007, 100, 681-697.
    • (2007) Ann. Bot , vol.100 , pp. 681-697
    • Wasternack, C.J.1
  • 3
    • 0034615558 scopus 로고    scopus 로고
    • The systemin signaling pathway: Differential activation of plant defensive genes
    • Ryan, C. A. The systemin signaling pathway: differential activation of plant defensive genes. Biochim. Biophys. Acta 2000, 1477, 112-121.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 112-121
    • Ryan, C.A.1
  • 4
    • 0041569777 scopus 로고    scopus 로고
    • Jasmonates and related oxylipins in plant responses to pathogenesis and herbivory
    • Farmer, E. E.; Aimeras, E.; Krishnamurthy, V. Jasmonates and related oxylipins in plant responses to pathogenesis and herbivory. Curr. Opin. Plant Biol. 2003, 6, 372-378.
    • (2003) Curr. Opin. Plant Biol , vol.6 , pp. 372-378
    • Farmer, E.E.1    Aimeras, E.2    Krishnamurthy, V.3
  • 5
    • 0345354649 scopus 로고    scopus 로고
    • Proteinase/Inhibitor Interactions in Plant-Pest Systems: A Brief Overview
    • Ed, Eurekah.com: Georgetown, TX
    • Michaud, D., Ed. Proteinase/Inhibitor Interactions in Plant-Pest Systems: A Brief Overview. In Recombinant Protease Inhibitors in Plants; Eurekah.com: Georgetown, TX, 2000; pp 1-5.
    • (2000) Recombinant Protease Inhibitors in Plants , pp. 1-5
  • 6
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: Genes for improving defenses against insects and pathogens
    • Ryan, C. A. Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 1990, 28, 425-449.
    • (1990) Annu. Rev. Phytopathol , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 7
    • 1642464622 scopus 로고    scopus 로고
    • Evolutionary families of peptidase inhibitors
    • Rawlings, N. D.; Tolle, D. P.; Barrett, A. J. Evolutionary families of peptidase inhibitors. Biochem. J. 2004, 378, 705-716.
    • (2004) Biochem. J , vol.378 , pp. 705-716
    • Rawlings, N.D.1    Tolle, D.P.2    Barrett, A.J.3
  • 8
    • 20044366564 scopus 로고    scopus 로고
    • Proteinase inhibitors and their function in plants: A review
    • Mosolov, V. V.; Valueva, T. A. Proteinase inhibitors and their function in plants: a review. Appl. Biochem. Microbiol. 2005, 41, 261-282.
    • (2005) Appl. Biochem. Microbiol , vol.41 , pp. 261-282
    • Mosolov, V.V.1    Valueva, T.A.2
  • 9
    • 5344259633 scopus 로고    scopus 로고
    • Protein proteinase inhibitors in combat against insects, pests and pathogens: Natural and engineered phytoprotection
    • Haq, S. K.; Atif, S. M.; Khan, R. H. Protein proteinase inhibitors in combat against insects, pests and pathogens: natural and engineered phytoprotection. Arch. Biochem. Biophys. 2004, 431, 145-159.
    • (2004) Arch. Biochem. Biophys , vol.431 , pp. 145-159
    • Haq, S.K.1    Atif, S.M.2    Khan, R.H.3
  • 10
    • 0001068883 scopus 로고
    • Wound-induced proteinase inhibitor in plant leaves: A possible defense mechanism against insects
    • Green, T. R.; Ryan, C. A. Wound-induced proteinase inhibitor in plant leaves: a possible defense mechanism against insects. Science. 1972, 175, 776-777.
    • (1972) Science , vol.175 , pp. 776-777
    • Green, T.R.1    Ryan, C.A.2
  • 11
    • 0025886794 scopus 로고    scopus 로고
    • Pearce, G.; Strydom, D.; Johnson, S.; Ryan, C. A. A polypeptide from tomato leaves induces wound-inducible proteinase inhibitors proteins. Science. 1991, 253, 895-898.
    • Pearce, G.; Strydom, D.; Johnson, S.; Ryan, C. A. A polypeptide from tomato leaves induces wound-inducible proteinase inhibitors proteins. Science. 1991, 253, 895-898.
  • 12
    • 11944260974 scopus 로고
    • Octadecanoid precursors of jasmonic acid activate the synthesis of wound-inducible proteinase inhibitors
    • Farmer, E. E.; Ryan, C. A. Octadecanoid precursors of jasmonic acid activate the synthesis of wound-inducible proteinase inhibitors. Plant Cell. 1992, 4, 129-134.
    • (1992) Plant Cell , vol.4 , pp. 129-134
    • Farmer, E.E.1    Ryan, C.A.2
  • 13
    • 0030293867 scopus 로고    scopus 로고
    • An octadecanoid pathway mutant (JL5) of tomato is compromised in signaling for defense against insect attack
    • Howe, G. A.; Lightner, J.; Browse, J.; Ryan, C. A. An octadecanoid pathway mutant (JL5) of tomato is compromised in signaling for defense against insect attack. Plant Cell. 1996, 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
  • 14
    • 48449103966 scopus 로고    scopus 로고
    • Inducible direct plant defense against insect herbivores: A review
    • Chen, M. Inducible direct plant defense against insect herbivores: a review. Insect Sci. 2008, 15, 101-114.
    • (2008) Insect Sci , vol.15 , pp. 101-114
    • Chen, M.1
  • 15
    • 0001745868 scopus 로고    scopus 로고
    • Proteinase inhibitors: Plant-derived genes of insecticidal protein for developing insect-resistant transgenic plants
    • Ussuf, K. K.; Laxmi, N. H.; Mitra, R. Proteinase inhibitors: plant-derived genes of insecticidal protein for developing insect-resistant transgenic plants. Curr Sci. 2001, 80, 847-853.
    • (2001) Curr Sci , vol.80 , pp. 847-853
    • Ussuf, K.K.1    Laxmi, N.H.2    Mitra, R.3
  • 16
    • 17744380286 scopus 로고    scopus 로고
    • Multiple insect resistance in transgenic tomato plant over-expressing two families of plant proteinase inhibitors
    • Abdeen, A.; Virgos, A.; Olivella, E.; Villanueva, J.; Avile, S. X.; Gabarra, R.; Prat, S. Multiple insect resistance in transgenic tomato plant over-expressing two families of plant proteinase inhibitors. Plant Mol. Biol. 2005, 57, 189-202.
    • (2005) Plant Mol. Biol , vol.57 , pp. 189-202
    • Abdeen, A.1    Virgos, A.2    Olivella, E.3    Villanueva, J.4    Avile, S.X.5    Gabarra, R.6    Prat, S.7
  • 17
    • 43749094150 scopus 로고    scopus 로고
    • Proteinase inhibitors in plant biotechnology: A review
    • Mosolov, V. V.; Valueva, T. A. Proteinase inhibitors in plant biotechnology: a review. Appl. Biochem. Microbiol. 2008, 44, 233-240.
    • (2008) Appl. Biochem. Microbiol , vol.44 , pp. 233-240
    • Mosolov, V.V.1    Valueva, T.A.2
  • 18
    • 34447320779 scopus 로고    scopus 로고
    • Maheswaran, G.; Pridmore, L.; Franz, P.; Anderson, M. A. A proteinase inhibitor from Nicotiana alata inhibits the normal development of light-brown apple moth Epiphyas postvittana in transgenic apple plants. Plant Cell Rep. 2007, 26, 773-782.
    • Maheswaran, G.; Pridmore, L.; Franz, P.; Anderson, M. A. A proteinase inhibitor from Nicotiana alata inhibits the normal development of light-brown apple moth Epiphyas postvittana in transgenic apple plants. Plant Cell Rep. 2007, 26, 773-782.
  • 19
    • 55549114967 scopus 로고    scopus 로고
    • Matsuura, F. C. A. U.; Folegatti, M. I. S. Processamento. In Maracujá: produção e qualidade de passicultura. Cruz das Almas, BA: Embrapa Mandioca e Fruticultura; Lima, A. A.; Cunha, M. A., Eds.; Embrapa Mandioca e Fruticultura: Cruz das Almas, BA, 2004; 30, pp 307-321.
    • Matsuura, F. C. A. U.; Folegatti, M. I. S. Processamento. In Maracujá: produção e qualidade de passicultura. Cruz das Almas, BA: Embrapa Mandioca e Fruticultura; Lima, A. A.; Cunha, M. A., Eds.; Embrapa Mandioca e Fruticultura: Cruz das Almas, BA, 2004; Vol. 30, pp 307-321.
  • 20
    • 11944254202 scopus 로고
    • Interplant communication: Airbone methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves
    • Farmer, E. E.; Ryan, C. A. Interplant communication: airbone methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 7713-7716.
    • (1990) Proc. Natl. Acad. Sci. U.S.A , vol.87 , pp. 7713-7716
    • Farmer, E.E.1    Ryan, C.A.2
  • 21
    • 33749683580 scopus 로고    scopus 로고
    • Morfologia externa dos estágios imaturos de heliconíneos neotropicais: V. Agraulis vanillae maculosa (Lepidoptera, Nymphalidae, Heliconiinae
    • Silva, D. S.; Dell'Erba, R.; Kaminski, L. A.; Moreira, G. R. P. Morfologia externa dos estágios imaturos de heliconíneos neotropicais: V. Agraulis vanillae maculosa (Lepidoptera, Nymphalidae, Heliconiinae. Iheringia. Série Zoologia. 2006, 96, 219-228.
    • (2006) Iheringia. Série Zoologia , vol.96 , pp. 219-228
    • Silva, D.S.1    Dell'Erba, R.2    Kaminski, L.A.3    Moreira, G.R.P.4
  • 22
    • 50549163362 scopus 로고
    • The preparation and properties of two new chromogenic substrates of trypsin
    • Erlanger, B. F.; Kokowsky, N.; Cohen, W. The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 1961, 95, 271-278.
    • (1961) Arch. Biochem. Biophys , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 23
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemmeli, U. K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmeli, U.K.1
  • 25
    • 0009482260 scopus 로고
    • Eletrophoretic transfer of proteins from poliacrilamida gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H.; Staehelin, T.; Gordon, J. Eletrophoretic transfer of proteins from poliacrilamida gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 1979, 76, 4350-4353.
    • (1979) Proc. Natl. Acad. Sci. U.S.A , vol.76 , pp. 4350-4353
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 26
    • 0028273981 scopus 로고
    • Detection of electrophoretically separated proteinase inhibitors using X-ray film
    • Pichare, P. M.; Kachole, M. S. Detection of electrophoretically separated proteinase inhibitors using X-ray film. J. Biochem. Biophys. Methods 1994, 28, 215-224.
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 215-224
    • Pichare, P.M.1    Kachole, M.S.2
  • 27
    • 0038808217 scopus 로고    scopus 로고
    • Detection of legume protease inhibitors by the gel-X-ray film contact print technique
    • Mulimani, V. H.; Kulkarni, S.; Giri, A. P. Detection of legume protease inhibitors by the gel-X-ray film contact print technique. Biochem. Mol. Biol. Edu. 2002, 30, 40-44.
    • (2002) Biochem. Mol. Biol. Edu , vol.30 , pp. 40-44
    • Mulimani, V.H.1    Kulkarni, S.2    Giri, A.P.3
  • 28
    • 0035983830 scopus 로고    scopus 로고
    • Accumulation of chloroplast-targeted lipoxygenase in passion fruit leaves in response to methyl jasmonate
    • Rangel, M.; Machado, O. L. T.; da Cunha, M.; Jacinto, T. Accumulation of chloroplast-targeted lipoxygenase in passion fruit leaves in response to methyl jasmonate. Phytochemistry 2002, 60, 619-625.
    • (2002) Phytochemistry , vol.60 , pp. 619-625
    • Rangel, M.1    Machado, O.L.T.2    da Cunha, M.3    Jacinto, T.4
  • 29
    • 38349133334 scopus 로고    scopus 로고
    • Wound response in passion fruit (Passiflora f. edulis flavicarpa) plants: Gene characterization of a novel chloroplast-targeted allene oxide synthase up-regulated by mechanical injury and methyl jasmonate
    • Siqueira-Junior, C. L.; Jardim, B. C.; Ürményi, T. P.; Vicente, A. C. P.; Hansen, E.; Otsuki, K.; Cunha, M.; Madureira, H. C.; Carvalho, D. R.; Jacinto, T. Wound response in passion fruit (Passiflora f. edulis flavicarpa) plants: gene characterization of a novel chloroplast-targeted allene oxide synthase up-regulated by mechanical injury and methyl jasmonate. Plant Cell Rep. 2008, 27, 387-397.
    • (2008) Plant Cell Rep , vol.27 , pp. 387-397
    • Siqueira-Junior, C.L.1    Jardim, B.C.2    Ürményi, T.P.3    Vicente, A.C.P.4    Hansen, E.5    Otsuki, K.6    Cunha, M.7    Madureira, H.C.8    Carvalho, D.R.9    Jacinto, T.10
  • 30
    • 20444478946 scopus 로고    scopus 로고
    • Jasmonates as signals in the wound response
    • Howe, G. A. Jasmonates as signals in the wound response. J. Plant Growth Regul. 2004, 23, 223-237.
    • (2004) J. Plant Growth Regul , vol.23 , pp. 223-237
    • Howe, G.A.1
  • 31
    • 0025252589 scopus 로고
    • Systemically wound-responsive genes in poplar trees encode proteins similar to sweet potato sporamins and legume Kunitz trypsin inhibitors
    • Bradshaw, H. D. JR.; Hollick, J. B.; Parsons, T. J.; Clarke, H. R. G.; Gordon, M. P. Systemically wound-responsive genes in poplar trees encode proteins similar to sweet potato sporamins and legume Kunitz trypsin inhibitors. Plant Mol. Biol. 1989, 14, 51-59.
    • (1989) Plant Mol. Biol , vol.14 , pp. 51-59
    • Bradshaw, H.D.J.1    Hollick, J.B.2    Parsons, T.J.3    Clarke, H.R.G.4    Gordon, M.P.5
  • 32
    • 0030175102 scopus 로고    scopus 로고
    • A wound-inducible gene from Salix viminalis coding for a trypsin inhibitor
    • Saarikoski, P.; Clapham, D.; von Arnold, S. A wound-inducible gene from Salix viminalis coding for a trypsin inhibitor. Plant Mol. Biol. 1996, 31, 465-478.
    • (1996) Plant Mol. Biol , vol.31 , pp. 465-478
    • Saarikoski, P.1    Clapham, D.2    von Arnold, S.3
  • 33
    • 0031081795 scopus 로고    scopus 로고
    • Functional activity of sporamin from sweet potato (Ipomoea batatas Lam): A tuber storage protein with trypsin inhibitory activity
    • Yeh, K. W.; Chen, J. C.; Lin, M. I.; Chen, Y. M.; Lin, C. Y. Functional activity of sporamin from sweet potato (Ipomoea batatas Lam): A tuber storage protein with trypsin inhibitory activity. Plant Mol. Biol. 1997, 33, 565-570.
    • (1997) Plant Mol. Biol , vol.33 , pp. 565-570
    • Yeh, K.W.1    Chen, J.C.2    Lin, M.I.3    Chen, Y.M.4    Lin, C.Y.5
  • 34
    • 0034921532 scopus 로고    scopus 로고
    • A Kunitz trypsin inhibitor gene family from trembling aspen (Populus tremuloides Michx.): Cloning, functional expression, and induction by wounding and herbivory
    • Haruta, M.; Major, I. T.; Christopher, M. E.; Patton, J. J.; Constabel, C. P. A Kunitz trypsin inhibitor gene family from trembling aspen (Populus tremuloides Michx.): cloning, functional expression, and induction by wounding and herbivory. Plant Mol. Biol. 200146, 347-359.
    • (2001) Plant Mol. Biol , vol.46 , pp. 347-359
    • Haruta, M.1    Major, I.T.2    Christopher, M.E.3    Patton, J.J.4    Constabel, C.P.5
  • 35
    • 38949168852 scopus 로고    scopus 로고
    • The accumulation of a Kunitz trypsin inhibitor from chickpea (TPI-2) located in cell walls is increased in wounded leaves and elongating epicotyls
    • Jiménez, T.; Martín, I.; Hernández-Nistal, J.; Labrador, E.; Dopico, B. The accumulation of a Kunitz trypsin inhibitor from chickpea (TPI-2) located in cell walls is increased in wounded leaves and elongating epicotyls. Physiol. Plant. 2008, 132, 306-317.
    • (2008) Physiol. Plant , vol.132 , pp. 306-317
    • Jiménez, T.1    Martín, I.2    Hernández-Nistal, J.3    Labrador, E.4    Dopico, B.5
  • 36
    • 0032754118 scopus 로고    scopus 로고
    • Successive use of non-host plant proteinase inhibitors required for effective inhibition of Helicoverpa armigera gut proteinases and larval growth
    • Harsulkar, A. M.; Giri, A. P.; Patankar, A. G.; Gupta, V. S.; Sainani, M. N.; Ranjekar, P. K.; Deshpande, V. V. Successive use of non-host plant proteinase inhibitors required for effective inhibition of Helicoverpa armigera gut proteinases and larval growth. Plant Physiol 1999, 121, 497-506.
    • (1999) Plant Physiol , vol.121 , pp. 497-506
    • Harsulkar, A.M.1    Giri, A.P.2    Patankar, A.G.3    Gupta, V.S.4    Sainani, M.N.5    Ranjekar, P.K.6    Deshpande, V.V.7
  • 38
    • 17044375977 scopus 로고    scopus 로고
    • Phylogenetic analysis of Theobroma (Sterculiaceae) based on Kunitz-like trypsin inhibitor sequences
    • Silva, C. R. S.; Figueira, A. Phylogenetic analysis of Theobroma (Sterculiaceae) based on Kunitz-like trypsin inhibitor sequences. Plant Syst. Evol. 2005, 250, 93-104.
    • (2005) Plant Syst. Evol , vol.250 , pp. 93-104
    • Silva, C.R.S.1    Figueira, A.2
  • 39
    • 23944437693 scopus 로고    scopus 로고
    • Molecular population genetics of herbivore-induced protease inhibitor genes in European aspen (Populus tremula L., Salicaceae)
    • Ingvarsson, P. K. Molecular population genetics of herbivore-induced protease inhibitor genes in European aspen (Populus tremula L., Salicaceae). Mol. Biol Evol. 2005, 22, 1802-1812.
    • (2005) Mol. Biol Evol , vol.22 , pp. 1802-1812
    • Ingvarsson, P.K.1
  • 40
    • 0032159174 scopus 로고    scopus 로고
    • Characterization of LeMir, a root-knot nematode-induced gene in tomato with an encoded product secreted from the root
    • Brenner, E. D.; Lambert, K. N.; Kaloshian, I.; Williamson, V. M. Characterization of LeMir, a root-knot nematode-induced gene in tomato with an encoded product secreted from the root. Plant Physiol. 1998, 118, 237-247.
    • (1998) Plant Physiol , vol.118 , pp. 237-247
    • Brenner, E.D.1    Lambert, K.N.2    Kaloshian, I.3    Williamson, V.M.4
  • 41
    • 0032033661 scopus 로고    scopus 로고
    • Cloning of tobacco genes that elicit the hypersensitive response
    • Karrer, E. E.; Beachy, R. N.; Holt, C. A. Cloning of tobacco genes that elicit the hypersensitive response. Plant Mol Biol. 1998, 36, 681-690.
    • (1998) Plant Mol Biol , vol.36 , pp. 681-690
    • Karrer, E.E.1    Beachy, R.N.2    Holt, C.A.3
  • 42
    • 7044263069 scopus 로고    scopus 로고
    • Gene expression profiling of systemically woundinduced defenses in hybrid poplar
    • Christopher, M. E.; Miranda, M.; Major, I. T. Gene expression profiling of systemically woundinduced defenses in hybrid poplar. Planta. 2004, 219, 936-947.
    • (2004) Planta , vol.219 , pp. 936-947
    • Christopher, M.E.1    Miranda, M.2    Major, I.T.3
  • 43
    • 0027605348 scopus 로고
    • Purification and characterization from tobacco (Nicotiana tabacum) leaves of six small, wound-inducible, proteinase isoinhibitors of the potato inhibitor II family
    • Pearce, G.; Johnson, S.; Ryan, C. A. Purification and characterization from tobacco (Nicotiana tabacum) leaves of six small, wound-inducible, proteinase isoinhibitors of the potato inhibitor II family. Plant Physiol. 1993, 102, 639-644.
    • (1993) Plant Physiol , vol.102 , pp. 639-644
    • Pearce, G.1    Johnson, S.2    Ryan, C.A.3
  • 44
    • 0034965916 scopus 로고    scopus 로고
    • Wound-inducible proteinase inhibitors in pepper. Differential regulation upon wounding, systemin, and methyl jasmonate
    • Moura, D. S.; Ryan, C. A. Wound-inducible proteinase inhibitors in pepper. Differential regulation upon wounding, systemin, and methyl jasmonate. Plant Physiol. 2001, 126, 289-298.
    • (2001) Plant Physiol , vol.126 , pp. 289-298
    • Moura, D.S.1    Ryan, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.