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Volumn 19, Issue 1, 2010, Pages 99-111

A cathepsin L-like proteinase is involved in moulting and metamorphosis in Helicoverpa armigera

Author keywords

Cathepsin L like proteinase; Expression pattern; Fat body remodelling; Haemocytes; Metamorphosis

Indexed keywords

ANTIBODY; CATHEPSIN L; COMPLEMENTARY DNA; INSECT PROTEIN; PEPTIDE HYDROLASE; RECOMBINANT PROTEIN;

EID: 73649143572     PISSN: 09621075     EISSN: 13652583     Source Type: Journal    
DOI: 10.1111/j.1365-2583.2009.00952.x     Document Type: Article
Times cited : (46)

References (32)
  • 1
    • 18844372795 scopus 로고    scopus 로고
    • Synthesis of prolyl 4-hydroxylase α subunit and type IV collagen in hemocytic granular cells of silkworm, Bombyx mori: Involvement of type IV collagen in self-defense reaction and metamorphosis
    • Adachi, T., Tomita, M. Yoshizato, K. (2005) Synthesis of prolyl 4-hydroxylase α subunit and type IV collagen in hemocytic granular cells of silkworm, Bombyx mori: involvement of type IV collagen in self-defense reaction and metamorphosis. Matrix Biol 24 : 136 154.
    • (2005) Matrix Biol , vol.24 , pp. 136-154
    • Adachi, T.1    Tomita, M.2    Yoshizato, K.3
  • 2
    • 0009180589 scopus 로고
    • Introduction: The classification of proteinases
    • Barrett, A.J. (1980) Introduction: the classification of proteinases. Ciba Found Symp 75 : 1 13.
    • (1980) Ciba Found Symp , vol.75 , pp. 1-13
    • Barrett, A.J.1
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 : 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0033532165 scopus 로고    scopus 로고
    • Mosquito cathepsin B-like protease involved in embryonic degradation of vitellin is produced as a latent extraovarian precursor
    • Cho, W.L., Tsao, S.M., Hays, A.R., Walter, R., Chen, J.S., Snigirevskaya, E.S. et al. (1999) Mosquito cathepsin B-like protease involved in embryonic degradation of vitellin is produced as a latent extraovarian precursor. J Biol Chem 274 : 13311 13321.
    • (1999) J Biol Chem , vol.274 , pp. 13311-13321
    • Cho, W.L.1    Tsao, S.M.2    Hays, A.R.3    Walter, R.4    Chen, J.S.5    Snigirevskaya, E.S.6
  • 5
    • 0242684461 scopus 로고    scopus 로고
    • Midgut adaptation and digestive enzyme distribution in a phloem feeding insect, the pea aphid Acyrthosiphon pisum
    • Cristofoletti, P.T., Ribeiro, A.F., Deraison, C., Rahbe, Y. Terra, W. (2003) Midgut adaptation and digestive enzyme distribution in a phloem feeding insect, the pea aphid Acyrthosiphon pisum. J Insect Physiol 49 : 11 24.
    • (2003) J Insect Physiol , vol.49 , pp. 11-24
    • Cristofoletti, P.T.1    Ribeiro, A.F.2    Deraison, C.3    Rahbe, Y.4    Terra, W.5
  • 6
    • 23844481908 scopus 로고    scopus 로고
    • The cathepsin l-like proteinases from the midgut of Tenebrio molitor larvae: Sequence, properties, immunocytochemical localization and function
    • Cristofoletti, P.T., Ribeiro, A.F. Terra, W.R. (2005) The cathepsin l-like proteinases from the midgut of Tenebrio molitor larvae: sequence, properties, immunocytochemical localization and function. Insect Biochem Mol Biol 35 : 883 901.
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 883-901
    • Cristofoletti, P.T.1    Ribeiro, A.F.2    Terra, W.R.3
  • 7
    • 34447617384 scopus 로고    scopus 로고
    • Identification of genes differentially expressed during larval molting and metamorphosis of Helicoverpa armigera
    • Dong, D.-J., He, H.-J., Chai, L.-Q., Jiang, X.-J., Wang, J.-X. Zhao, X.-F. (2007) Identification of genes differentially expressed during larval molting and metamorphosis of Helicoverpa armigera. BMC Dev Biol 7 : 73.
    • (2007) BMC Dev Biol , vol.7 , pp. 73
    • Dong, D.-J.1    He, H.-J.2    Chai, L.-Q.3    Jiang, X.-J.4    Wang, J.-X.5    Zhao, X.-F.6
  • 8
    • 53549094681 scopus 로고    scopus 로고
    • Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation
    • Duncan, E.M., Muratore-Schroeder, T.L., Cook, R.G., Garcia, B.A., Shabanowitz, J., Hunt, D.F. et al. (2008) Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation. Cell 135 : 604 607.
    • (2008) Cell , vol.135 , pp. 604-607
    • Duncan, E.M.1    Muratore-Schroeder, T.L.2    Cook, R.G.3    Garcia, B.A.4    Shabanowitz, J.5    Hunt, D.F.6
  • 9
    • 0032963378 scopus 로고    scopus 로고
    • Two subunits of the insect 26/29-kDa proteinase are probably derived from a common precursor protein
    • Fujimoto, Y., Kobayashi, A., Kurata, S. Natori, S. (1999) Two subunits of the insect 26/29-kDa proteinase are probably derived from a common precursor protein. J Biochem 125 : 566 573.
    • (1999) J Biochem , vol.125 , pp. 566-573
    • Fujimoto, Y.1    Kobayashi, A.2    Kurata, S.3    Natori, S.4
  • 10
    • 0000968374 scopus 로고
    • Establishment of four strains of cells from insect tissue grown in vitro
    • Grace, T.D.C. (1962) Establishment of four strains of cells from insect tissue grown in vitro. Nature 195 : 788 789.
    • (1962) Nature , vol.195 , pp. 788-789
    • Grace, T.D.C.1
  • 11
    • 0030587773 scopus 로고    scopus 로고
    • The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft
    • Groves, M.R., Taylor, M.A., Scott, M., Cummings, N.J., Pickersgill, R.W. Jenkins, J.A. (1996) The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft. Structure 4 : 1193 1203.
    • (1996) Structure , vol.4 , pp. 1193-1203
    • Groves, M.R.1    Taylor, M.A.2    Scott, M.3    Cummings, N.J.4    Pickersgill, R.W.5    Jenkins, J.A.6
  • 12
    • 0032959390 scopus 로고    scopus 로고
    • Regulation of a novel pathway for cell death by lysosomal aspartic and cysteine proteinases
    • Isahara, K., Ohsawa, Y. Kanamori, S. (1999) Regulation of a novel pathway for cell death by lysosomal aspartic and cysteine proteinases. Neuroscience 91 : 233 349.
    • (1999) Neuroscience , vol.91 , pp. 233-349
    • Isahara, K.1    Ohsawa, Y.2    Kanamori, S.3
  • 13
    • 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
  • 14
    • 0036784566 scopus 로고    scopus 로고
    • Insect hemocytes and their role in immunity
    • Lavine, M.D. Strand, M.R. (2002) Insect hemocytes and their role in immunity. Insect Biochem Mol Biol 32 : 1295 1309.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 1295-1309
    • Lavine, M.D.1    Strand, M.R.2
  • 15
    • 33845622505 scopus 로고    scopus 로고
    • Cathepsin L function in insect moulting: Molecular cloning and functional analysis in cotton bollworm, Helicoverpa armigera
    • Liu, J., Shi, G.P., Zhang, W.Q., Zhang, G.R. Xu, W.H. (2006) Cathepsin L function in insect moulting: molecular cloning and functional analysis in cotton bollworm, Helicoverpa armigera. Insect Mol Biol 15 : 823 834.
    • (2006) Insect Mol Biol , vol.15 , pp. 823-834
    • Liu, J.1    Shi, G.P.2    Zhang, W.Q.3    Zhang, G.R.4    Xu, W.H.5
  • 16
    • 0028840144 scopus 로고
    • A putative digestive cysteine proteinase from Drosophila melanogaster is predominantly expressed in the embryonic and larval midgut
    • Matsumoto, I., Watanabe, H., Abe, K., Arai, S. Emori, Y. (1995) A putative digestive cysteine proteinase from Drosophila melanogaster is predominantly expressed in the embryonic and larval midgut. Eur J Biochem 227 : 582 587.
    • (1995) Eur J Biochem , vol.227 , pp. 582-587
    • Matsumoto, I.1    Watanabe, H.2    Abe, K.3    Arai, S.4    Emori, Y.5
  • 17
    • 33748641381 scopus 로고    scopus 로고
    • Fat-body remodeling in Drosophila melanogaster
    • Nelliot, A., Bond, N. Hoshizaki, D.K. (2006) Fat-body remodeling in Drosophila melanogaster. Genesis 44 : 396 400.
    • (2006) Genesis , vol.44 , pp. 396-400
    • Nelliot, A.1    Bond, N.2    Hoshizaki, D.K.3
  • 18
    • 33744497582 scopus 로고    scopus 로고
    • Apoptosis and adhesion of hemocytes during molting stage of silkworm, Bombyx mori
    • Okazaki, T., Okudaira, N., Iwabuchi, K., Fugo, H. Nagai, T. (2006) Apoptosis and adhesion of hemocytes during molting stage of silkworm, Bombyx mori. Zoolog Sci 23 : 299 304.
    • (2006) Zoolog Sci , vol.23 , pp. 299-304
    • Okazaki, T.1    Okudaira, N.2    Iwabuchi, K.3    Fugo, H.4    Nagai, T.5
  • 19
    • 0000154726 scopus 로고
    • Immunodiffusion and immunoelectrophoresis
    • In. Vol. 1. Weir, D.M. ed.), pp. Blackwell. Oxford.
    • Ouchterlony, O. Nilsson, L.A. (1978) Immunodiffusion and immunoelectrophoresis. In Immunochemistry, Vol. 1 (Weir, D.M., ed.), pp. 467 510. Blackwell, Oxford.
    • (1978) Immunochemistry , pp. 467-510
    • Ouchterlony, O.1    Nilsson, L.A.2
  • 21
    • 33646365052 scopus 로고    scopus 로고
    • Insect haemocytes: What type of cell is that?
    • Database issue
    • Brehélin, M. (2006) Insect haemocytes: what type of cell is that? J Insect Physiol 52 : 417 429.
    • (2006) J Insect Physiol , vol.52 , pp. 417-429
    • Brehélin, M.1
  • 22
    • 0001573128 scopus 로고
    • Acid cysteine proteinase from the eggs of silkmoth, Bombyx mori: Tissue distribution, developmental changes and the sites of synthesis for the enzyme
    • Takahashi, S.Y., Zhao, X.-F., Kageyama, T. Yamamoto, Y. (1992) Acid cysteine proteinase from the eggs of silkmoth, Bombyx mori: tissue distribution, developmental changes and the sites of synthesis for the enzyme. Insect Biochem Molec Biol 22 : 369 377.
    • (1992) Insect Biochem Molec Biol , vol.22 , pp. 369-377
    • Takahashi, S.Y.1    Zhao, X.-F.2    Kageyama, T.3    Yamamoto, Y.4
  • 23
    • 0031149558 scopus 로고    scopus 로고
    • Cysteine proteinase 1 (CP1), a cathepsin l-like enzyme expressed in the Drosophila melanogaster haemocyte cell line mbn-2
    • Tryselius, Y. Hultmark, D. (1997) Cysteine proteinase 1 (CP1), a cathepsin l-like enzyme expressed in the Drosophila melanogaster haemocyte cell line mbn-2. Insect Mol Biol 6 : 173 181.
    • (1997) Insect Mol Biol , vol.6 , pp. 173-181
    • Tryselius, Y.1    Hultmark, D.2
  • 24
    • 0032872258 scopus 로고    scopus 로고
    • Immunochemical analysis of cathepsin B in lung tumors: An independent prognostic factor for squamous cell carcinoma patients
    • Werle, B., Lotterle, H. Schanzenbacher, U. (1999) Immunochemical analysis of cathepsin B in lung tumors: an independent prognostic factor for squamous cell carcinoma patients. Cancer 81 : 510 519.
    • (1999) Cancer , vol.81 , pp. 510-519
    • Werle, B.1    Lotterle, H.2    Schanzenbacher, U.3
  • 25
    • 34250890062 scopus 로고    scopus 로고
    • Drosophila melanogaster embryonic haemocytes: Masters of multitasking
    • Wood, W. Jacinto, A. (2007) Drosophila melanogaster embryonic haemocytes: masters of multitasking. Nat Rev Mol Cell Biol 8 : 542 551.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 542-551
    • Wood, W.1    Jacinto, A.2
  • 26
    • 0028606210 scopus 로고
    • Molecular cloning and sequencing of cDNA that encodes cysteine proteinase in the eggs of the silkmoth, Bombyx mori
    • Yamamoto, Y., Takimoto, K., Izumi, S., Toriyama-Sakurai, M., Kageyama, T. Takahashi, S.Y. (1994) Molecular cloning and sequencing of cDNA that encodes cysteine proteinase in the eggs of the silkmoth, Bombyx mori. J Biochem 116 : 1330 1335.
    • (1994) J Biochem , vol.116 , pp. 1330-1335
    • Yamamoto, Y.1    Takimoto, K.2    Izumi, S.3    Toriyama-Sakurai, M.4    Kageyama, T.5    Takahashi, S.Y.6
  • 27
    • 0035103439 scopus 로고    scopus 로고
    • Bombyx mori prohemocyte division and differentiation in individual microcultures
    • Yamashita, M. Iwabuchi, K. (2001) Bombyx mori prohemocyte division and differentiation in individual microcultures. J Insect Physiol 47 : 325 331.
    • (2001) J Insect Physiol , vol.47 , pp. 325-331
    • Yamashita, M.1    Iwabuchi, K.2
  • 28
    • 33646578839 scopus 로고    scopus 로고
    • Cathepsin B-like proteinase is involved in the decomposition of the adult fat body of Helicoverpa armigera
    • Yang, X.-M., Hou, L.-J., Dong, D.-J., Shao, H.-L., Wang, J.-X. Zhao, X.-F. (2006) Cathepsin B-like proteinase is involved in the decomposition of the adult fat body of Helicoverpa armigera. Arch Insect Biochem Physiol 62 : 1 10.
    • (2006) Arch Insect Biochem Physiol , vol.62 , pp. 1-10
    • Yang, X.-M.1    Hou, L.-J.2    Dong, D.-J.3    Shao, H.-L.4    Wang, J.-X.5    Zhao, X.-F.6
  • 29
    • 34247143237 scopus 로고    scopus 로고
    • Expression and function of cathepsin B-Like proteinase in larval hemocytes of Helicoverpa armigera during metamorphosis
    • Yang, X.-M., Hou, L.-J., Wang, J.-X. Zhao, X.-F. (2007) Expression and function of cathepsin B-Like proteinase in larval hemocytes of Helicoverpa armigera during metamorphosis. Arch Insect Biochem Physiol 64 : 164 174.
    • (2007) Arch Insect Biochem Physiol , vol.64 , pp. 164-174
    • Yang, X.-M.1    Hou, L.-J.2    Wang, J.-X.3    Zhao, X.-F.4
  • 30
    • 0032052228 scopus 로고    scopus 로고
    • Purification and characterization of a cysteine proteinase from eggs of the cotton boll worm, Helicoverpa armigera
    • Zhao, X.-F., Wang, J.-X. Wang, Y.-C. (1998) Purification and characterization of a cysteine proteinase from eggs of the cotton boll worm, Helicoverpa armigera. Insect Biochem Mol Biol 28 : 259 264.
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 259-264
    • Zhao, X.-F.1    Wang, J.-X.2    Wang, Y.-C.3
  • 31
    • 0036899898 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the cathepsin B-like proteinase from the cotton boll worm, Helicoverpa armigera
    • Zhao, X.-F., Wang, J.-X., Xu, X.-L., Schmid, R. Wieczorek, H. (2002) Molecular cloning and characterization of the cathepsin B-like proteinase from the cotton boll worm, Helicoverpa armigera. Insect Mol Biol 11 : 567 575.
    • (2002) Insect Mol Biol , vol.11 , pp. 567-575
    • Zhao, X.-F.1    Wang, J.-X.2    Xu, X.-L.3    Schmid, R.4    Wieczorek, H.5


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