메뉴 건너뛰기




Volumn 40, Issue 1, 2009, Pages 4-19

Profiles of the body-surface proteolytic system of honey bee queens, workers and drones: Ontogenetic and seasonal changes in proteases and their natural inhibitors

Author keywords

Body surface proteolysis; Honey bee; Protease inhibitors; Proteases; Zymography

Indexed keywords

ACIDITY; AMINO ACID; DETERGENT; ELECTROKINESIS; ENZYME ACTIVITY; EXPERIMENTAL STUDY; HONEYBEE; ONTOGENY; PH; POLYMER; QUEEN; SEASONAL VARIATION; SEPARATION; SEX-RELATED DIFFERENCE;

EID: 60749089009     PISSN: 00448435     EISSN: 12979678     Source Type: Journal    
DOI: 10.1051/apido:2008057     Document Type: Article
Times cited : (29)

References (41)
  • 1
    • 85012738381 scopus 로고
    • The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin
    • Anson M.L. (1938) The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin, J. Gen. Physiol. 22, 79-89.
    • (1938) J. Gen. Physiol , vol.22 , pp. 79-89
    • Anson, M.L.1
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. (1976) A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 7, 248-254.
    • (1976) Anal. Biochem , vol.7 , pp. 248-254
    • Bradford, M.1
  • 3
    • 1642545489 scopus 로고    scopus 로고
    • Antimicrobial peptides: From invertebrates to vertebrates
    • Bulet P., Stösklin R., Menin L. (2004) Antimicrobial peptides: from invertebrates to vertebrates, Immunol. Rev. 198, 169-184.
    • (2004) Immunol. Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stösklin, R.2    Menin, L.3
  • 4
    • 39049177888 scopus 로고    scopus 로고
    • From hive minds to humans
    • Check E. (2006) From hive minds to humans, Nature 443, 893.
    • (2006) Nature , vol.443 , pp. 893
    • Check, E.1
  • 5
    • 0036890724 scopus 로고    scopus 로고
    • Molecular characterization of Lma-p54, a new epicuticular surface protein in the cockroach Leucophaea maderae (Dictyoptera, oxyhaloine)
    • Cornette R., Farine J.-P., Quennedey B., Rivière S., Brossut R. (2002) Molecular characterization of Lma-p54, a new epicuticular surface protein in the cockroach Leucophaea maderae (Dictyoptera, oxyhaloine), Insect Biochem. Mol. Biol. 32, 1635-1642.
    • (2002) Insect Biochem. Mol. Biol , vol.32 , pp. 1635-1642
    • Cornette, R.1    Farine, J.-P.2    Quennedey, B.3    Rivière, S.4    Brossut, R.5
  • 6
    • 0034769835 scopus 로고    scopus 로고
    • A community of ants, fungi and bacteria: A multilateral approach to studying symbiosis
    • Currie C.R. (2001) A community of ants, fungi and bacteria: a multilateral approach to studying symbiosis, Annu. Rev. Microbiol. 55, 357-380.
    • (2001) Annu. Rev. Microbiol , vol.55 , pp. 357-380
    • Currie, C.R.1
  • 7
    • 0033594414 scopus 로고    scopus 로고
    • Fungus-growing ants use antibiotisproducing bacteria to control garden parasites
    • Currie C.R., Scott J.A., Summerbell R.C., Malloch D. (1999) Fungus-growing ants use antibiotisproducing bacteria to control garden parasites, Nature 398, 701-704.
    • (1999) Nature , vol.398 , pp. 701-704
    • Currie, C.R.1    Scott, J.A.2    Summerbell, R.C.3    Malloch, D.4
  • 8
    • 0000511211 scopus 로고
    • The midgut endopeptidase of the honeybee (Apis mellifica): Comparison of the enzymes in different ontogenesis stages
    • Dahlman B., Jany K., Pfleiderer G. (1978) The midgut endopeptidase of the honeybee (Apis mellifica): comparison of the enzymes in different ontogenesis stages, Insect Biochem. 8, 203-211.
    • (1978) Insect Biochem , vol.8 , pp. 203-211
    • Dahlman, B.1    Jany, K.2    Pfleiderer, G.3
  • 10
    • 12444257791 scopus 로고    scopus 로고
    • Expression profiles of water-soluble proteinases during ontogenesis of Megachile rotundata: An electrophoretic investigation
    • Felicioli A., Donadio E., Balestreri E., Montagnoli G., Felicioli R., Podesta A. (2004) Expression profiles of water-soluble proteinases during ontogenesis of Megachile rotundata: an electrophoretic investigation, Apidologie 35, 595-604.
    • (2004) Apidologie , vol.35 , pp. 595-604
    • Felicioli, A.1    Donadio, E.2    Balestreri, E.3    Montagnoli, G.4    Felicioli, R.5    Podesta, A.6
  • 11
    • 0035118609 scopus 로고    scopus 로고
    • Serine proteases as mediators of mosquito immune response
    • Gorman M.J., Paskewitz S.M. (2001) Serine proteases as mediators of mosquito immune response, Insect Biochem. Mol. Biol. 31, 257-262.
    • (2001) Insect Biochem. Mol. Biol , vol.31 , pp. 257-262
    • Gorman, M.J.1    Paskewitz, S.M.2
  • 12
    • 60749100126 scopus 로고    scopus 로고
    • The "bodysurface" proteolytic system of rove beetles (Staphylinidae) as a possible bioindicator and immune system element
    • in press
    • Grzywnowicz K., Staniec B. (2008) The "bodysurface" proteolytic system of rove beetles (Staphylinidae) as a possible bioindicator and immune system element, Insect Biochem. Mol. Biol. (in press).
    • (2008) Insect Biochem. Mol. Biol
    • Grzywnowicz, K.1    Staniec, B.2
  • 14
    • 60749133572 scopus 로고
    • Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolimerized substrates
    • Heussen C., Dowdle E. (1980) Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolimerized substrates, J. Apic. Res. 23, 61-63.
    • (1980) J. Apic. Res , vol.23 , pp. 61-63
    • Heussen, C.1    Dowdle, E.2
  • 15
    • 0242581687 scopus 로고    scopus 로고
    • The immune response of Drosophila
    • Hoffman J.A. (2003) The immune response of Drosophila, Nature 426, 33-38.
    • (2003) Nature , vol.426 , pp. 33-38
    • Hoffman, J.A.1
  • 16
    • 22044433161 scopus 로고    scopus 로고
    • Differences in drone and worker physiology in honebees (Apis mellifera)
    • Hrassnigg N., Crailsheim K. (2005) Differences in drone and worker physiology in honebees (Apis mellifera), Apidologie 36, 255-277.
    • (2005) Apidologie , vol.36 , pp. 255-277
    • Hrassnigg, N.1    Crailsheim, K.2
  • 17
    • 0037290892 scopus 로고    scopus 로고
    • Drosophila immunity: Paths and patterns
    • Hultmark D. (2003) Drosophila immunity: Paths and patterns, Curr. Opin. Immunol. 15, 12-19.
    • (2003) Curr. Opin. Immunol , vol.15 , pp. 12-19
    • Hultmark, D.1
  • 18
    • 0035460364 scopus 로고    scopus 로고
    • The relationship between a leaf-rolling moth (Dactylioglypha tonica) and fungi covering the cocoon
    • Imamura N., Ishikawa T., Takeda K., Fukami H., Konno A., Nishida R. (2001) The relationship between a leaf-rolling moth (Dactylioglypha tonica) and fungi covering the cocoon, Biosci. Biotechnol. Biochem. 65, 1965-1969.
    • (2001) Biosci. Biotechnol. Biochem , vol.65 , pp. 1965-1969
    • Imamura, N.1    Ishikawa, T.2    Takeda, K.3    Fukami, H.4    Konno, A.5    Nishida, R.6
  • 20
    • 0031260101 scopus 로고    scopus 로고
    • The adaptation of insects to plant protease inhibitors
    • Jongsma M.A., Bolter C. (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.2
  • 21
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • Kanost M.R. (1999) Serine proteinase inhibitors in arthropod immunity, Dev. Comp. Immunol. 23, 291-301.
    • (1999) Dev. Comp. Immunol , vol.23 , pp. 291-301
    • Kanost, M.R.1
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0029111330 scopus 로고    scopus 로고
    • Trypsin inhibitor and trypsin-like protease activity in air- or submergence-grown rice (Oryza sativa) coleoptiles
    • Lee T.-M., Lin Y.-H. (1999) Trypsin inhibitor and trypsin-like protease activity in air- or submergence-grown rice (Oryza sativa) coleoptiles, Plant Sci. 106, 43-54.
    • (1999) Plant Sci , vol.106 , pp. 43-54
    • Lee, T.-M.1    Lin, Y.-H.2
  • 26
    • 3142609643 scopus 로고    scopus 로고
    • Potential effects of GM crops on honey bee health
    • Malone L.A. (2004) Potential effects of GM crops on honey bee health, Bee World 85, 29-36.
    • (2004) Bee World , vol.85 , pp. 29-36
    • Malone, L.A.1
  • 27
    • 0032004129 scopus 로고    scopus 로고
    • In vivo response of honey bee midgut proteases to two protease inhibitors from potato
    • Malone L.A., Burgess E.P., Christeller J.T., Gatehouse H.S. (1998) In vivo response of honey bee midgut proteases to two protease inhibitors from potato, J. Insect Physiol. 44, 141-147.
    • (1998) J. Insect Physiol , vol.44 , pp. 141-147
    • Malone, L.A.1    Burgess, E.P.2    Christeller, J.T.3    Gatehouse, H.S.4
  • 28
    • 15244353361 scopus 로고    scopus 로고
    • Clash of kingdoms or why Drosophila larvae positively respond to fungal competitors
    • Rohlfs M. (2005) Clash of kingdoms or why Drosophila larvae positively respond to fungal competitors, Front. Zool. 2, 1-7.
    • (2005) Front. Zool , vol.2 , pp. 1-7
    • Rohlfs, M.1
  • 29
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: Genes for improving defense against insects and pathogens
    • Ryan C. (1990) Protease inhibitors in plants: genes for improving defense against insects and pathogens, Annu. Rev. Phytopathol. 28, 425-449.
    • (1990) Annu. Rev. Phytopathol , vol.28 , pp. 425-449
    • Ryan, C.1
  • 31
    • 60749130593 scopus 로고    scopus 로고
    • Spectrum-Elsevier, Heidelberg, Germany
    • Tautz J. (2007) Phänomen Honigbiene, Spectrum-Elsevier, Heidelberg, Germany.
    • (2007) Phänomen Honigbiene
    • Tautz, J.1
  • 33
    • 0027999854 scopus 로고
    • Insect digestive enzymes: Properties, compartmentalization and function
    • Terra W.R., Ferreira C. (1994) Insect digestive enzymes: properties, compartmentalization and function, Comp. Biochem. Physiol. B 109, 1-62.
    • (1994) Comp. Biochem. Physiol. B , vol.109 , pp. 1-62
    • Terra, W.R.1    Ferreira, C.2
  • 34
    • 33750460281 scopus 로고    scopus 로고
    • Insight into social insects from the genome of the honeybee Apis mellifera
    • The Honeybee Genome Sequencing Consortium
    • The Honeybee Genome Sequencing Consortium (2006) Insight into social insects from the genome of the honeybee Apis mellifera, Nature 443, 931-949.
    • (2006) Nature , vol.443 , pp. 931-949
  • 35
    • 33644875278 scopus 로고    scopus 로고
    • Biochemistry of human skin - our brain on the outside
    • Tobin D.J. (2006) Biochemistry of human skin - our brain on the outside, Chem. Soc. Rev. 35, 52-67.
    • (2006) Chem. Soc. Rev , vol.35 , pp. 52-67
    • Tobin, D.J.1
  • 37
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. (2002) Antimicrobial peptides of multicellular organisms, Nature 415, 389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 38
    • 12344301866 scopus 로고    scopus 로고
    • Epidermal differentiation: The role of proteases and their inhibitors
    • Zeeuwen P.L.J.M. (2004) Epidermal differentiation: The role of proteases and their inhibitors, Eur. J. Cell Biol. 83, 761-773.
    • (2004) Eur. J. Cell Biol , vol.83 , pp. 761-773
    • Zeeuwen, P.L.J.M.1
  • 39
    • 1642435684 scopus 로고    scopus 로고
    • Microorganisms in the gut of beetles: Evidence from molecular cloning
    • Zhang N., Suh S.-O., Blackwell M. (2003) Microorganisms in the gut of beetles: evidence from molecular cloning, J. Invertebrate Pathol. 84, 226-233.
    • (2003) J. Invertebrate Pathol , vol.84 , pp. 226-233
    • Zhang, N.1    Suh, S.-O.2    Blackwell, M.3
  • 40
    • 26444456636 scopus 로고    scopus 로고
    • Purification and characterization of an irreversible serine protease inhibitor from skin secretions of Bufo andrewsi
    • Zhao Y., Jin Y., Wei S.-S., Lee W.-H., Zhang Y. (2005) Purification and characterization of an irreversible serine protease inhibitor from skin secretions of Bufo andrewsi, Toxicon 46, 635-640.
    • (2005) Toxicon , vol.46 , pp. 635-640
    • Zhao, Y.1    Jin, Y.2    Wei, S.-S.3    Lee, W.-H.4    Zhang, Y.5
  • 41
    • 33750477010 scopus 로고    scopus 로고
    • Comparative analysis of serine protease-related genes in the honey bee genome: Possible involvement in embryonic development and innate immunity
    • Zou Z., Lopez D.L., Kanost M.R., Evans J.D., Jiang H.B. (2006) Comparative analysis of serine protease-related genes in the honey bee genome: possible involvement in embryonic development and innate immunity, Insect Mol. Biol. 15, 603-614.
    • (2006) Insect Mol. Biol , vol.15 , pp. 603-614
    • Zou, Z.1    Lopez, D.L.2    Kanost, M.R.3    Evans, J.D.4    Jiang, H.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.