메뉴 건너뛰기




Volumn 104, Issue 6, 2009, Pages 805-812

Potential of laticifer fluids for inhibiting Aedes aegypti larval development: Evidence for the involvement of proteolytic activity

Author keywords

Aedes aegypti; Biological control; Cysteine proteinases; Larvae; Latex; Papain

Indexed keywords

AEDES AEGYPTI; CALOTROPIS; CALOTROPIS PROCERA; CARICA PAPAYA; CRYPTOSTEGIA GRANDIFLORA; EUPHORBIA; EUPHORBIA TIRUCALLI; PLUMERIA RUBRA;

EID: 70350256033     PISSN: 00740276     EISSN: 16788060     Source Type: Journal    
DOI: 10.1590/S0074-02762009000600001     Document Type: Article
Times cited : (16)

References (35)
  • 1
    • 0026497716 scopus 로고
    • Corn Kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Molecular cloning and expression studies
    • Abe M, Abe K, Kuroda S, Arai S 1992. Corn Kernel cysteine proteinase inhibitor as a novel cystatin superfamily member of plant origin. Molecular cloning and expression studies. Eur J Biochem 209: 933-937.
    • (1992) Eur J Biochem , vol.209 , pp. 933-937
    • Abe, M.1    Abe, K.2    Kuroda, S.3    Arai, S.4
  • 3
    • 0015338074 scopus 로고
    • 1 and other thiol proteinases
    • 1 and other thiol proteinases. Anal Biochem 47: 280-293.
    • (1972) Anal Biochem , vol.47 , pp. 280-293
    • Barrett, A.J.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford MM 1976. A rapid and sensitive method for the quantification of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 70350292370 scopus 로고    scopus 로고
    • Aedes aegypti: Inseticidas, mecanismos de ação e resistência
    • Braga IA, Valle D 2007. Aedes aegypti: inseticidas, mecanismos de ação e resistência. Epidemiol Serv Saude 16: 279-293.
    • (2007) Epidemiol Serv Saude , vol.16 , pp. 279-293
    • Braga, I.A.1    Valle, D.2
  • 8
    • 0036842625 scopus 로고    scopus 로고
    • Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides
    • Carlini CR, Grossi-de-Sá MF 2002. Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides. Toxicon 40: 1515-1539.
    • (2002) Toxicon , vol.40 , pp. 1515-1539
    • Carlini, C.R.1    Grossi-de-Sá, M.F.2
  • 11
    • 0032197093 scopus 로고    scopus 로고
    • Studies on laticiferous plants: Toxic effects in goats of Calotropis procera latex given by different routes of administration
    • El-Badwi, Samia MA, Adam SE, Shigidi MT, Hapke HJ 1998. Studies on laticiferous plants: toxic effects in goats of Calotropis procera latex given by different routes of administration. Dtsch Tierarztl Wochenschr 105: 425-427.
    • (1998) Dtsch Tierarztl Wochenschr , vol.105 , pp. 425-427
    • El-Badwi Samia, M.A.1    Adam, S.E.2    Shigidi, M.T.3    Hapke, H.J.4
  • 14
    • 0027191298 scopus 로고
    • The two cysteine endopeptidases of legume seeds: Purification and characterization by use of specific fluorometric assay
    • Kembhavi AA, Buttle DJ, Knight CG, Barrett AJ 1993. The two cysteine endopeptidases of legume seeds: purification and characterization by use of specific fluorometric assay. Arch Biochem Biophys 303: 208-213.
    • (1993) Arch Biochem Biophys , vol.303 , pp. 208-213
    • Kembhavi, A.A.1    Buttle, D.J.2    Knight, C.G.3    Barrett, A.J.4
  • 15
    • 0017324044 scopus 로고
    • Serine proteases: Structure and mechanism of catalysis
    • Kraut J 1977. Serine proteases: structure and mechanism of catalysis. Annu Rev Biochem 46: 331-358.
    • (1977) Annu Rev Biochem , vol.46 , pp. 331-358
    • Kraut, J.1
  • 16
    • 0014949207 scopus 로고
    • 4
    • Laemmli UK 1970. Cleavage of structural proteins during the assemble of bacteriophage T4. Nature 227: 680-688.
    • (1970) Nature , vol.227 , pp. 680-688
    • Laemmli, U.K.1
  • 17
    • 65349161507 scopus 로고    scopus 로고
    • Articulated laticifers of vegetative organs Mandevilla atroviolaceae (Apocynaceae, Apocynoideae)
    • Lopes KLB, Thadeo M, Azevedo AA, Soares AA, Meira RMSA 2009. Articulated laticifers of vegetative organs Mandevilla atroviolaceae (Apocynaceae, Apocynoideae). Botany 87: 202-209.
    • (2009) , vol.87 , pp. 202-209
    • Lopes, K.L.B.1    Thadeo, M.2    Azevedo, A.A.3    Soares, A.A.4    Meira, R.M.S.A.5
  • 18
    • 0018792070 scopus 로고
    • Purification and some properties of two proteases from papaya latex
    • Lynn KR 1979. Purification and some properties of two proteases from papaya latex. Biochim Biophys Acta 569: 193-201.
    • (1979) Biochim Biophys Acta , vol.569 , pp. 193-201
    • Lynn, K.R.1
  • 19
    • 2342519504 scopus 로고    scopus 로고
    • Kunitz-type inhibitor of coleopteran proteases, isolated from Adenanthera pavonina L. seeds and its effect on Callosobruchus maculatus
    • Macedo ML, Freire MD, Parra JRP 2004. Kunitz-type inhibitor of coleopteran proteases, isolated from Adenanthera pavonina L. seeds and its effect on Callosobruchus maculatus. J Agric Food Chem 52: 2533-2540.
    • (2004) J Agric Food Chem , vol.52 , pp. 2533-2540
    • Macedo, M.L.1    Freire, M.D.2    Parra, J.R.P.3
  • 20
    • 33745959045 scopus 로고    scopus 로고
    • Purification of papain from Carica papaya latex: Aqueous two-phase extraction versus two-step salt precipitation
    • Nitsawang S, Hatti-Kaul R, Kanasawuda P 2006. Purification of papain from Carica papaya latex: aqueous two-phase extraction versus two-step salt precipitation. Enzyme Microb Technol 39: 1103-1107.
    • (2006) Enzyme Microb Technol , vol.39 , pp. 1103-1107
    • Nitsawang, S.1    Hatti-Kaul, R.2    Kanasawuda, P.3
  • 23
    • 0141706505 scopus 로고    scopus 로고
    • A high cysteine containing thiol proteinase from the latex of Ervatamia heyneana: Purification and comparison with Ervatamin B and C from Ervatamia coronaria
    • Patel BK, Jagannadham MV 2003. A high cysteine containing thiol proteinase from the latex of Ervatamia heyneana: purification and comparison with Ervatamin B and C from Ervatamia coronaria. J Agric Food Chem 51: 6326-6334.
    • (2003) J Agric Food Chem , vol.51 , pp. 6326-6334
    • Patel, B.K.1    Jagannadham, M.V.2
  • 24
    • 0036790854 scopus 로고    scopus 로고
    • Insect feeding mobilizes a unique plant defense protease that disrupts the peritrophic matrix of caterpillars
    • Pechan T, Cohen A, Williams WP, Luthe DS 2002. Insect feeding mobilizes a unique plant defense protease that disrupts the peritrophic matrix of caterpillars. Proc Natl Acad Sci 99: 13319-13323.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 13319-13323
    • Pechan, T.1    Cohen, A.2    Williams, W.P.3    Luthe, D.S.4
  • 25
    • 0029990335 scopus 로고    scopus 로고
    • Mosquitocidal toxins genes and bacteria: The hit squad
    • Porter AG 1996. Mosquitocidal toxins genes and bacteria: the hit squad. Parasitol Today 12: 175-179.
    • (1996) Parasitol Today , vol.12 , pp. 175-179
    • Porter, A.G.1
  • 26
    • 33747823792 scopus 로고    scopus 로고
    • Latex constituents from Calotropis procera (Ait.) R.Br. display toxicity upon egg hatching and larvae of Aedes aegypti (Linn.)
    • Ramos MV, Bandeira GP, Freitas CDT, Nogueira NAP, Alencar NMN, Sousa PAS, Carvalho AFFU 2006. Latex constituents from Calotropis procera (Ait.) R.Br. display toxicity upon egg hatching and larvae of Aedes aegypti (Linn.). Mem Inst Oswaldo Cruz 101: 503-510.
    • (2006) , vol.101 , pp. 503-510
    • Ramos, M.V.1    Bandeira, G.P.2    Freitas, C.D.T.3    Nogueira, N.A.P.4    Alencar, N.M.N.5    Sousa, P.A.S.6    Carvalho, A.F.F.U.7
  • 27
    • 34447580103 scopus 로고    scopus 로고
    • Performance of distinct crop pests reared on diets enriched with latex proteins from Calotropis procera: Role of laticifer proteins in plant defense
    • Ramos MV, Freitas CDT, Stanisçuaski F, Macedo LLP, Sales MP, Sousa DP, Carlini CR 2007. Performance of distinct crop pests reared on diets enriched with latex proteins from Calotropis procera: role of laticifer proteins in plant defense. Plant Sci 173: 349-357.
    • (2007) Plant Sci , vol.173 , pp. 349-357
    • Ramos, M.V.1    Freitas, C.D.T.2    Stanisçuaski, F.3    Macedo, L.L.P.4    Sales, M.P.5    Sousa, D.P.6    Carlini, C.R.7
  • 29
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepoly-acrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 KDa
    • Schagger H, Jagow GV 1987. Tricine-sodium dodecyl sulfatepoly-acrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 KDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Jagow, G.V.2
  • 31
    • 0002061632 scopus 로고
    • Isolation and properties of crystalline mercury derivative of a lysozyme from papaya latex
    • Smith EL, Kimmel JR, Brown DM, Thompson EOP 1955. Isolation and properties of crystalline mercury derivative of a lysozyme from papaya latex. J Biol Chem 215: 67-89.
    • (1955) J Biol Chem , vol.215 , pp. 67-89
    • Smith, E.L.1    Kimmel, J.R.2    Brown, D.M.3    Thompson, E.O.P.4
  • 32
    • 0027431179 scopus 로고
    • Purification of an endoproteinase that digests the wheat "EM" protein in vitro and determination of its cleavage sites
    • Taylor RM, Cumming AC 1993. Purification of an endoproteinase that digests the wheat "EM" protein in vitro and determination of its cleavage sites. FEBS Lett 331: 76-80.
    • (1993) FEBS Lett , vol.331 , pp. 76-80
    • Taylor, R.M.1    Cumming, A.C.2
  • 34
    • 70350346169 scopus 로고    scopus 로고
    • Genebra: Dengue/dengue haemorrhagic fever
    • WHO World Health Organization, homepage on the internet, [updated 2009 May 16; cited 2009 Apr 29]. Available from
    • WHO World Health Organization 2009. [homepage on the internet]. Genebra: dengue/dengue haemorrhagic fever. [updated 2009 May 16; cited 2009 Apr 29]. Available from: http://www.who.int/ mediacentre/factsheets/ fs117/en/index.html.
    • (2009)
  • 35
    • 0000736550 scopus 로고
    • Poor correlation between the levels of proteinase inhibitors found in seeds of different cultivars of cowpea (Vigna unguiculata) and the resistance/susceptibility to predation by Callosobruchus maculatus
    • Xavier-Filho J, Campos FAP, Ary MB, Silva CP, Carvalho MMM 1989. Poor correlation between the levels of proteinase inhibitors found in seeds of different cultivars of cowpea (Vigna unguiculata) and the resistance/susceptibility to predation by Callosobruchus maculatus. J Agric Food Chem 37: 1139-1143.
    • (1989) J Agric Food Chem , vol.37 , pp. 1139-1143
    • Xavier-Filho, J.1    Campos, F.A.P.2    Ary, M.B.3    Silva, C.P.4    Carvalho, M.M.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.