메뉴 건너뛰기




Volumn 28, Issue 6, 2007, Pages 1292-1298

Proregion of Acanthoscelides obtectus cysteine proteinase: A novel peptide with enhanced selectivity toward endogenous enzymes

Author keywords

Acanthoscelides obtectus; Cysteine proteinase; Plant defense; Propeptide

Indexed keywords

CATHEPSIN L; COMPLEMENTARY DNA; CYSTEINE PROTEINASE; RECOMBINANT PROTEIN; THIOREDOXIN;

EID: 34249713620     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2007.03.020     Document Type: Article
Times cited : (11)

References (34)
  • 1
    • 0037841979 scopus 로고    scopus 로고
    • Interactions between above- and belowground insect herbivores as mediated by the plant system
    • Bezemer T.M., Wagennaar R., Van Dam N.M., and Wäckers F.L. Interactions between above- and belowground insect herbivores as mediated by the plant system. OIKOS 101 (2003) 555-562
    • (2003) OIKOS , vol.101 , pp. 555-562
    • Bezemer, T.M.1    Wagennaar, R.2    Van Dam, N.M.3    Wäckers, F.L.4
  • 3
    • 0024066065 scopus 로고
    • The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode W., Engh R., Musil D., Thiele U., Huber R., Karshinov A., et al. The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J 7 (1988) 2593-2599
    • (1988) EMBO J , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshinov, A.6
  • 4
    • 0030038759 scopus 로고    scopus 로고
    • Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
    • Carmona E., Dufour E., Plouffe C., Takebe S., Mason P., Mort J.S., et al. Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases. Biochemistry 35 (1996) 8149-8157
    • (1996) Biochemistry , vol.35 , pp. 8149-8157
    • Carmona, E.1    Dufour, E.2    Plouffe, C.3    Takebe, S.4    Mason, P.5    Mort, J.S.6
  • 5
    • 0031468018 scopus 로고    scopus 로고
    • Proregion structure of members of the papain superfamily mode of inhibition of enzymatic activity
    • Cygler M., and Mort J.S. Proregion structure of members of the papain superfamily mode of inhibition of enzymatic activity. Biochimie 79 (1997) 645-652
    • (1997) Biochimie , vol.79 , pp. 645-652
    • Cygler, M.1    Mort, J.S.2
  • 6
    • 0032952098 scopus 로고    scopus 로고
    • Binding modes of a new epoxysuccinyl-peptide inhibitor of cysteine proteases. Where and how do cysteine proteases express their selectivity?
    • Czaplewski C., Grzonka Z., Jaskólski M., Kasprzykowski F., Kozak M., Politowska E., et al. Binding modes of a new epoxysuccinyl-peptide inhibitor of cysteine proteases. Where and how do cysteine proteases express their selectivity?. Biochim Biophys Acta 1431 (1999) 290-305
    • (1999) Biochim Biophys Acta , vol.1431 , pp. 290-305
    • Czaplewski, C.1    Grzonka, Z.2    Jaskólski, M.3    Kasprzykowski, F.4    Kozak, M.5    Politowska, E.6
  • 7
    • 21044458299 scopus 로고    scopus 로고
    • Molecular cloning and expression of an alpha-amylase inhibitor from rye with a potential for controlling insect pests
    • Dias S.C., Franco O.L., Magalhães C.P., Oliveira-Neto O.B., Laumann R.A., Figueira E.L.Z., et al. Molecular cloning and expression of an alpha-amylase inhibitor from rye with a potential for controlling insect pests. Protein J 24 (2005) 113-123
    • (2005) Protein J , vol.24 , pp. 113-123
    • Dias, S.C.1    Franco, O.L.2    Magalhães, C.P.3    Oliveira-Neto, O.B.4    Laumann, R.A.5    Figueira, E.L.Z.6
  • 8
    • 23244457789 scopus 로고    scopus 로고
    • Inhibition of a cathepsin L-like cysteine proteinase by a chimeric propetide-derived inhibitor
    • Godat E., Chowdhury S., Lecaille F., Belghazi M., Purisima E.O., and Lalmanach G. Inhibition of a cathepsin L-like cysteine proteinase by a chimeric propetide-derived inhibitor. Biochemistry 44 (2005) 10486-10493
    • (2005) Biochemistry , vol.44 , pp. 10486-10493
    • Godat, E.1    Chowdhury, S.2    Lecaille, F.3    Belghazi, M.4    Purisima, E.O.5    Lalmanach, G.6
  • 10
    • 0033776087 scopus 로고    scopus 로고
    • Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides
    • Guay J., Falgueyret J.P., Ducret A., Percival M.D., and Mancini J.A. Potency and selectivity of inhibition of cathepsin K, L and S by their respective propeptides. Eur J Biochem 267 (2000) 6311-6318
    • (2000) Eur J Biochem , vol.267 , pp. 6311-6318
    • Guay, J.1    Falgueyret, J.P.2    Ducret, A.3    Percival, M.D.4    Mancini, J.A.5
  • 11
    • 0033119509 scopus 로고    scopus 로고
    • Genetic engineering of crop plants for insect resistance - a critical review
    • Hilder V.A., and Bolter D. Genetic engineering of crop plants for insect resistance - a critical review. Crop Prot 18 (1999) 177-191
    • (1999) Crop Prot , vol.18 , pp. 177-191
    • Hilder, V.A.1    Bolter, D.2
  • 13
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer K.M., Peiffer S.L., and Ditomas M.E. Two distinct gene subfamilies within the family of cysteine protease genes. Proc Natl Acad Sci USA 90 (1993) 3063-3067
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    Ditomas, M.E.3
  • 14
    • 0034117738 scopus 로고    scopus 로고
    • An evolutionarily conserved tripartite tryptophan motif stabilizes the prodomains of cathepsin L-like cysteine proteases
    • Kreusch S., Fehn M., Maubach G., Nissler K., Rommerskirch W., Schilling K., et al. An evolutionarily conserved tripartite tryptophan motif stabilizes the prodomains of cathepsin L-like cysteine proteases. Eur J Biochem 267 (2000) 2965-2972
    • (2000) Eur J Biochem , vol.267 , pp. 2965-2972
    • Kreusch, S.1    Fehn, M.2    Maubach, G.3    Nissler, K.4    Rommerskirch, W.5    Schilling, K.6
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0036233856 scopus 로고    scopus 로고
    • The peptidase zymogen proregions: nature's way of preventing undesired activation and proteolysis
    • Lazure C. The peptidase zymogen proregions: nature's way of preventing undesired activation and proteolysis. Curr Pharm Design 8 (2002) 125-133
    • (2002) Curr Pharm Design , vol.8 , pp. 125-133
    • Lazure, C.1
  • 18
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille F., Kaleta J., and Bromme D. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem Rev 102 (2002) 4459-4488
    • (2002) Chem Rev , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Bromme, D.3
  • 19
    • 0642311142 scopus 로고    scopus 로고
    • Use of phage display to select novel cystatins specific for Acanthoscelides obtectus cysteine proteinases
    • Melo F.R., Mello M.O., Franco O.L., Rigden D.J., Mello L.V., Genú A.M., et al. Use of phage display to select novel cystatins specific for Acanthoscelides obtectus cysteine proteinases. Biochim Biophys Acta 1651 (2003) 146-152
    • (2003) Biochim Biophys Acta , vol.1651 , pp. 146-152
    • Melo, F.R.1    Mello, M.O.2    Franco, O.L.3    Rigden, D.J.4    Mello, L.V.5    Genú, A.M.6
  • 20
    • 0028817235 scopus 로고
    • Constitutive forms during development of the Colorado potato beetle Leptinotarsa decemlineata Say (Coleoptera: Chrysomelidae)
    • Michaud D., Bernier-Vadnais N., Overney S., and Yelle S. Constitutive forms during development of the Colorado potato beetle Leptinotarsa decemlineata Say (Coleoptera: Chrysomelidae). Insect Biochem Mol Biol 25 (1995) 1041-1048
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 1041-1048
    • Michaud, D.1    Bernier-Vadnais, N.2    Overney, S.3    Yelle, S.4
  • 21
    • 34648871470 scopus 로고    scopus 로고
    • Seasonal distribution of common bean (Phaseolus vulgaris L.) bruchid species in selected areas
    • Arusha, Tanzania
    • Nchimbi-Msolla S., and Misangu R.N. Seasonal distribution of common bean (Phaseolus vulgaris L.) bruchid species in selected areas. Proceedings: Bean Seed Workshop. Arusha, Tanzania (2001) 12-14
    • (2001) Proceedings: Bean Seed Workshop , pp. 12-14
    • Nchimbi-Msolla, S.1    Misangu, R.N.2
  • 22
    • 0037396262 scopus 로고    scopus 로고
    • Effects of proteinase inhibitors on digestive proteinases and growth of the red flour beetle Tribolium castaneum Herbst (Coleoptera: Tenebrionidae)
    • Oppert B., Morgan T.D., Hartzer K., Lenarcic B., Galesa F., Brzin J., et al. Effects of proteinase inhibitors on digestive proteinases and growth of the red flour beetle Tribolium castaneum Herbst (Coleoptera: Tenebrionidae). Comp Biochem Physiol C 134 (2003) 481-490
    • (2003) Comp Biochem Physiol C , vol.134 , pp. 481-490
    • Oppert, B.1    Morgan, T.D.2    Hartzer, K.3    Lenarcic, B.4    Galesa, F.5    Brzin, J.6
  • 23
    • 0038392947 scopus 로고    scopus 로고
    • Characterization and classification of five cysteine proteinases expressed by Paragonimus westermani adult worm
    • Park H., Kim S.L., Hong K.M., Kim M.J., Shin C.H., Ryu J.S., et al. Characterization and classification of five cysteine proteinases expressed by Paragonimus westermani adult worm. Exp Parasitol 102 (2002) 143-149
    • (2002) Exp Parasitol , vol.102 , pp. 143-149
    • Park, H.1    Kim, S.L.2    Hong, K.M.3    Kim, M.J.4    Shin, C.H.5    Ryu, J.S.6
  • 24
    • 0028673327 scopus 로고
    • Families of cysteine peptidases
    • Rawlings N.D., and Barrett A.J. Families of cysteine peptidases. Methods Enzymol 244 (1994) 461-486
    • (1994) Methods Enzymol , vol.244 , pp. 461-486
    • Rawlings, N.D.1    Barrett, A.J.2
  • 25
    • 0032980694 scopus 로고    scopus 로고
    • The propeptide of Fasciola hepatica cathepsin L is a potent and selective inhibitor of the mature enzyme
    • Roche L., Tort J., and Dalton J.P. The propeptide of Fasciola hepatica cathepsin L is a potent and selective inhibitor of the mature enzyme. Mol Biochem Parasitol 98 (1999) 271-277
    • (1999) Mol Biochem Parasitol , vol.98 , pp. 271-277
    • Roche, L.1    Tort, J.2    Dalton, J.P.3
  • 26
    • 0033553419 scopus 로고    scopus 로고
    • Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain
    • Santamaría I., Velasco G., Pendás A.M., Paz A., and López-Otín C. Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J Biol Chem 274 (1999) 13800-13809
    • (1999) J Biol Chem , vol.274 , pp. 13800-13809
    • Santamaría, I.1    Velasco, G.2    Pendás, A.M.3    Paz, A.4    López-Otín, C.5
  • 28
    • 0033101490 scopus 로고    scopus 로고
    • The involvement of cysteine proteinase and proteinase inhibitor genes in the regulation of programmed cell death in plants
    • Solomon M., Belenghi B., Delledone M., Menachen E., and Levine A. The involvement of cysteine proteinase and proteinase inhibitor genes in the regulation of programmed cell death in plants. Plant Cell 11 (1999) 431-433
    • (1999) Plant Cell , vol.11 , pp. 431-433
    • Solomon, M.1    Belenghi, B.2    Delledone, M.3    Menachen, E.4    Levine, A.5
  • 29
    • 0028944193 scopus 로고
    • Recombinant pro-regions from papain and papaya proteinase IV - are selective high affinity inhibitors of the mature papaya enzymes
    • Taylor M.A., Baker K.C., Briggs G.S., Connerton I.F., Cummings N.J., Pratt K.A., et al. Recombinant pro-regions from papain and papaya proteinase IV - are selective high affinity inhibitors of the mature papaya enzymes. Protein Eng 8 (1995) 59-62
    • (1995) Protein Eng , vol.8 , pp. 59-62
    • Taylor, M.A.1    Baker, K.C.2    Briggs, G.S.3    Connerton, I.F.4    Cummings, N.J.5    Pratt, K.A.6
  • 30
    • 0031587948 scopus 로고    scopus 로고
    • Trypsin isolated from the midgut of the tobacco hornworm, Manduca sexta is inhibited by synthetic pro-peptides in vitro
    • Taylor M.A., and Lee M.J. Trypsin isolated from the midgut of the tobacco hornworm, Manduca sexta is inhibited by synthetic pro-peptides in vitro. Biochem Biophys Res Commun 235 (1997) 606-609
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 606-609
    • Taylor, M.A.1    Lee, M.J.2
  • 31
    • 0029977174 scopus 로고    scopus 로고
    • Midgut proteinases in three divergent species of Coleoptera
    • Terra W.R., and Cristofoletti P.T. Midgut proteinases in three divergent species of Coleoptera. Comp Biochem Physiol 113 (1996) 725-730
    • (1996) Comp Biochem Physiol , vol.113 , pp. 725-730
    • Terra, W.R.1    Cristofoletti, P.T.2
  • 32
    • 0032407452 scopus 로고    scopus 로고
    • The proregion of papaya proteinase IV inhibits Colorado potato beetle digestive cysteine proteinases
    • Visal S., Taylor M.J., and Michaud D. The proregion of papaya proteinase IV inhibits Colorado potato beetle digestive cysteine proteinases. FEBS Lett 434 (1998) 401-405
    • (1998) FEBS Lett , vol.434 , pp. 401-405
    • Visal, S.1    Taylor, M.J.2    Michaud, D.3
  • 33
    • 0035951780 scopus 로고    scopus 로고
    • Cathepsin B-like cysteine proteases confer intestinal cysteine protease activity in Haemonchus contortus
    • Shompole S., and Jasmer D.P. Cathepsin B-like cysteine proteases confer intestinal cysteine protease activity in Haemonchus contortus. J Biol Chem 276 (2001) 2928-2934
    • (2001) J Biol Chem , vol.276 , pp. 2928-2934
    • Shompole, S.1    Jasmer, D.P.2
  • 34
    • 0036254611 scopus 로고    scopus 로고
    • Novel cysteine proteinase inhibitors homologous to the proregions of cysteine proteinases
    • Yamamoto Y., Kurata M., Watabe S., Murakami R., and Takahashi S.Y. Novel cysteine proteinase inhibitors homologous to the proregions of cysteine proteinases. Curr Protein Pept Sci 3 (2002) 231-238
    • (2002) Curr Protein Pept Sci , vol.3 , pp. 231-238
    • Yamamoto, Y.1    Kurata, M.2    Watabe, S.3    Murakami, R.4    Takahashi, S.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.