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Volumn 58, Issue 16, 2010, Pages 9190-9197

Expression of recombinant AccMRJP1 protein from royal jelly of Chinese honeybee in Pichia pastoris and its proliferation activity in an insect cell line

Author keywords

AccMRJP1; Apis cerana cerana; Eukaryotic expression; Proliferation activity; Royal jelly

Indexed keywords

ACCMRJP1; APIS CERANA CERANA; EUKARYOTIC EXPRESSION; PROLIFERATION ACTIVITY; ROYAL JELLY;

EID: 77956501263     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf1007133     Document Type: Article
Times cited : (22)

References (44)
  • 1
    • 19344364453 scopus 로고    scopus 로고
    • Screening of biological activities present in honeybee (Apis mellifera) royal jelly
    • Salazar-Olivo, L. A.; Paz-Gonzales, V. Screening of biological activities present in honeybee (Apis mellifera) royal jelly. Toxicol. in Vitro 2005, 19, 645-651.
    • (2005) Toxicol. in Vitro , vol.19 , pp. 645-651
    • Salazar-Olivo, L.A.1    Paz-Gonzales, V.2
  • 3
    • 13844292595 scopus 로고    scopus 로고
    • Effects produced by royal jelly on haematopoiesis: Relation with host resistance against Ehrlich ascites tumour challenge
    • Bincoletto, C.; Eberlin, S.; Figueiredo, C. A.; Luengo, M. B.; Queiroz, M. L. Effects produced by royal jelly on haematopoiesis: relation with host resistance against Ehrlich ascites tumour challenge. Int. Immunopharmacol. 2005, 5, 679-688.
    • (2005) Int. Immunopharmacol , vol.5 , pp. 679-688
    • Bincoletto, C.1    Eberlin, S.2    Figueiredo, C.A.3    Luengo, M.B.4    Queiroz, M.L.5
  • 7
    • 77249172692 scopus 로고    scopus 로고
    • Expression of acc-royalisin gene from royal jelly of Chinese honeybee in Escherichia coli and its antibacterial activity
    • Shen, L. R.; Ding, M. H.; Zhang, L. W.; Jin, F.; Zhang, W. G.; Li, D. Expression of acc-royalisin gene from royal jelly of Chinese honeybee in Escherichia coli and its antibacterial activity. J. Agric. Food Chem. 2010, 58, 2266-2273.
    • J. Agric. Food Chem , vol.2010 , Issue.58 , pp. 2266-2273
    • Shen, L.R.1    Ding, M.H.2    Zhang, L.W.3    Jin, F.4    Zhang, W.G.5    Li, D.6
  • 9
    • 0042385077 scopus 로고    scopus 로고
    • Royal Jelly prolongs the life span of C3H/HeJ mice: Correlation with reduced DNA damage
    • Inoue, S.; Koya-Miyata, S.; Ushio, S.; Iwaki, K.; Ikeda, M.; Kurimoto, M. Royal Jelly prolongs the life span of C3H/HeJ mice: correlation with reduced DNA damage. Exp. Gerontol. 2003, 38, 965-969.
    • (2003) . Exp. Gerontol , vol.38 , pp. 965-969
    • Inoue, S.1    Koya-Miyata, S.2    Ushio, S.3    Iwaki, K.4    Ikeda, M.5    Kurimoto, M.6
  • 10
    • 35548971161 scopus 로고    scopus 로고
    • Proteomic analysis of royal jelly from three strains of western honeybees (Apis mellifera)
    • Li, J. K.; Wang, T.; Zhang, Z. H.; Pan, Y. H. Proteomic analysis of royal jelly from three strains of western honeybees (Apis mellifera). J. Agric. Food Chem. 2007, 55, 8411-8422.
    • (2007) J. Agric. Food Chem , vol.55 , pp. 8411-8422
    • Li, J.K.1    Wang, T.2    Zhang, Z.H.3    Pan, Y.H.4
  • 11
    • 0037448609 scopus 로고    scopus 로고
    • Honeybee (Apis mellifera L.) mrjp gene family: Computational analysis of putative promoters and genomic structure of mrjp1, the gene coding for the most abundant protein of larval food
    • Malecova, B.; Ramserb, J.; O'Brienb, J. K.; Janitz, M.; Júdová, J.; Lehrach, H.; Judova, J.; Lehrach, H.; Simuth, J. Honeybee (Apis mellifera L.) mrjp gene family: computational analysis of putative promoters and genomic structure of mrjp1, the gene coding for the most abundant protein of larval food. Gene 2003, 303, 165-175.
    • (2003) Gene , vol.303 , pp. 165-175
    • Malecova, B.1    Ramserb, J.2    O'Brienb, J.K.3    Janitz, M.4    Júdová, J.5    Lehrach, H.6    Judova, J.7    Lehrach, H.8    Simuth, J.9
  • 12
    • 1642568737 scopus 로고    scopus 로고
    • The MRJP/YELLOW protein family of Apis mellifera: Identification of new members in the EST library
    • Albert, S.; Klaudiny, J. The MRJP/YELLOW protein family of Apis mellifera: Identification of new members in the EST library. J. Insect Physiol. 2004, 50, 51-59.
    • (2004) J. Insect Physiol , vol.50 , pp. 51-59
    • Albert, S.1    Klaudiny, J.2
  • 13
    • 33750454258 scopus 로고    scopus 로고
    • Evolution of the yellow/major royal jelly protein family and the emergence of social behavior in honey bees
    • Drapeau, M. D.; Albert, S.; Kucharski, R.; Prusten, C.; Meleszka,R. Evolution of the yellow/major royal jelly protein family and the emergence of social behavior in honey bees. Genome Res. 2007, 25, 1385-1394.
    • (2007) Genome Res , vol.25 , pp. 1385-1394
    • Drapeau, M.D.1    Albert, S.2    Kucharski, R.3    Prusten, C.4    Meleszkar5
  • 14
    • 0034805081 scopus 로고    scopus 로고
    • Fifty-seven kDa protein in royal jelly enhances proliferation of primary cultured rat hepatocytes and increases albumin production in the absence of serum
    • Kamakura, M.; Suenobu, N.; Fukushima, M. Fifty-seven kDa protein in royal jelly enhances proliferation of primary cultured rat hepatocytes and increases albumin production in the absence of serum. Biochem. Biophys. Res. Commun. 2001, 282, 865-874.
    • (2001) Biochem. Biophys. Res. Commun , vol.282 , pp. 865-874
    • Kamakura, M.1    Suenobu, N.2    Fukushima, M.3
  • 15
    • 0036952482 scopus 로고    scopus 로고
    • Signal transduction mechanism leading to enhanced proliferation of primary cultured adult rat hepatocytes treated with royal jelly 57-kDa protein
    • Kamakura, M. Signal transduction mechanism leading to enhanced proliferation of primary cultured adult rat hepatocytes treated with royal jelly 57-kDa protein. J. Biochem. 2002, 132, 911-912.
    • (2002) J. Biochem. , vol.132 , pp. 911-912
    • Kamakura, M.1
  • 16
    • 30144437355 scopus 로고    scopus 로고
    • The immunostimulatory effect of the recombinant apalbumin 1-major honeybee royal jelly protein-on TNFR release
    • Majtan, J.; Kovacova, E.; Bilikova, K.; Simuth, J. The immunostimulatory effect of the recombinant apalbumin 1-major honeybee royal jelly protein-on TNFR release. Int. Immunopharmacol. 2006, 6, 269-278.
    • (2006) Int. Immunopharmacol , vol.6 , pp. 269-278
    • Majtan, J.1    Kovacova, E.2    Bilikova, K.3    Simuth, J.4
  • 18
    • 3142694824 scopus 로고    scopus 로고
    • Transformation of tobacco plants with cDNA encoding honeybee royal jelly MRJP1
    • Judova, J.; Sutka, R.; Klaudiny, J.; Liskova, D.; OW, D. W.; Simuth, J. Transformation of tobacco plants with cDNA encoding honeybee royal jelly MRJP1. Biol. Plant. 2004, 48, 185-191.
    • (2004) Biol. Plant , vol.48 , pp. 185-191
    • Judova, J.1    Sutka, R.2    Klaudiny, J.3    Liskova, D.4    O, W.D.W.5    Simuth, J.6
  • 19
    • 77950530892 scopus 로고    scopus 로고
    • Reduced expression of major royal jelly protein 1 gene in the mushroom bodies of worker honeybees with reduced learning ability
    • Hojo, M.; Kagami, T.; Sasaki, T.; Nakamura, J.; Sasaki, M. Reduced expression of major royal jelly protein 1 gene in the mushroom bodies of worker honeybees with reduced learning ability. Apidologie 2010, 41, 194-202.
    • Apidologie , vol.2010 , Issue.41 , pp. 194-202
    • Hojo, M.1    Kagami, T.2    Sasaki, T.3    Nakamura, J.4    Sasaki, M.5
  • 20
    • 2942560423 scopus 로고    scopus 로고
    • Jelleines: A family of antimicrobial peptides from the royal jelly of honeybees (Apis mellifera)
    • Fontana, R.; Mendes, M. A.; de Souza, B. M.; Konno, K.; César, L. M.; Malaspina, O.; Palma, M. S. Jelleines: a family of antimicrobial peptides from the royal jelly of honeybees (Apis mellifera). Peptides 2004, 25, 919-928.
    • (2004) Peptides , Issue.25 , pp. 919-928
    • Fontana, R.1    Mendes, M.A.2    De Souza, B.M.3    Konno, K.4    César, L.M.5    Malaspina, O.6    Palma, M.S.7
  • 21
    • 11144356043 scopus 로고    scopus 로고
    • Immunochemical approach to detection of adulteration in honey: Physiologically active royal jelly protein stimulating TNF-R release is a regular component of honey
    • Simuth, J.; Bilikova, K.; Kovacova, E.; Kuzmova, Z.; Schroder, W. Immunochemical approach to detection of adulteration in honey: physiologically active royal jelly protein stimulating TNF-R release is a regular component of honey. J. Agric. Food Chem. 2004, 52, 2154-2158.
    • (2004) . J. Agric. Food Chem , vol.52 , pp. 2154-2158
    • Simuth, J.1    Bilikova, K.2    Kovacova, E.3    Kuzmova, Z.4    Schroder, W.5
  • 22
    • 17744408947 scopus 로고    scopus 로고
    • Preparation of recombinant most abundant protein MRJP1 of royal jelly
    • Judova, J.; Klaudiny, J.; Simuth, J. Preparation of recombinant most abundant protein MRJP1 of royal jelly. Biologia 1998, 53, 7778-7784.
    • (1998) Biologia , vol.53 , pp. 7778-7784
    • Judova, J.1    Klaudiny, J.2    Simuth, J.3
  • 23
    • 0942268089 scopus 로고    scopus 로고
    • And characterization of major royal jelly cDNAs and proteins of honey bee (Apis cerana)
    • Srisuparbh, D.; Klinbunga, S.; Wangsiri, S.; Sittipraneed, S. Isolation and characterization of major royal jelly cDNAs and proteins of honey bee (Apis cerana). J. Biochem. Mol. Biol. 2003, 6, 572-579.
    • (2003) J. Biochem. Mol. Biol , vol.6 , pp. 572-579
    • Srisuparbh, D.1    Klinbunga, S.2    Wangsiri, S.3    Isolation, S.S.4
  • 24
    • 21244500225 scopus 로고    scopus 로고
    • Expression and genomic organization of genes encoding major royal jelly protein 1 and 2 of the honey bee (Apis cerana)
    • Imjongjirak, C.; Klinbunga, S.; Sittipraneed, S. Cloning, expression and genomic organization of genes encoding major royal jelly protein 1 and 2 of the honey bee (Apis cerana). J. Biochem. Mol. Biol. 2005, 38, 49-57.
    • (2005) J. Biochem. Mol. Biol , vol.38 , pp. 49-57
    • Imjongjirak, C.1    Klinbunga S.Cloning2
  • 25
    • 56649086805 scopus 로고    scopus 로고
    • The utilization and industrialization of insect resources in China
    • Zhang, C. X.; Tang, X. D.; Cheng, J. A. The utilization and industrialization of insect resources in China. Entomol. Res. 2008, 38, S38-S47.
    • (2008) .Entomol. Res , vol.38
    • Zhang, C.X.1    Tang, X.D.2    Cheng, J.A.3
  • 26
    • 55549134694 scopus 로고    scopus 로고
    • Expression of apalbumin1 of Apis cerana cerana in the larvae of silkworm Bombyx mori
    • Tao, T.; Su, S. K.; Miao, Y. G.; Yue, W. F.; Du, H. H.; Chen, S. L.; Fang Liu, F.; Zhan, Y. Expression of apalbumin1 of Apis cerana cerana in the larvae of silkworm, Bombyx mori. J. Agric. Food Chem. 2010, 56, 9464-9468.
    • J. Agric. Food Chem. , vol.2010 , Issue.56 , pp. 9464-9468
    • Tao, T.1    Su, S.K.2    Miao, Y.G.3    Yue, W.F.4    Du, H.H.5    Chen, S.L.6    Fang, LiuF.7    Zhan, Y.8
  • 27
    • 84891489166 scopus 로고    scopus 로고
    • Cloning of royal jelly AccMRJP1 gene from Apis cerana cerana and its expression in Escherichia coli
    • Zhang, L. W.; Ding, M. H.; Zhang, W. G.; Jin, F.; Shen, L. R. Cloning of royal jelly AccMRJP1 gene from Apis cerana cerana and its expression in Escherichia coli. J. Zhejiang Univ. (Agric. Life Sci.) 2010, 36 (2), 119-124.
    • (2010) J. Zhejiang Univ. (Agric. Life Sci.) , vol.36 , Issue.2 , pp. 119-124
    • Zhang, L.W.1    Ding, M.H.2    Zhang, W.G.3    Jin, F.4    Shen, L.R.5
  • 29
    • 24944551249 scopus 로고    scopus 로고
    • Molecular cloning and analysis of four cDNAs from the heads of Apis cerana cerana nurse honeybees coding for major royal jelly proteins
    • Su, S. K.; Albert, S.; Chen, S. L.; Zhong, B. X. Molecular cloning and analysis of four cDNAs from the heads of Apis cerana cerana nurse honeybees coding for major royal jelly proteins. Apidologie 2005, 36, 389-401.
    • (2005) Apidologie , vol.36 , pp. 389-401
    • Su, S.K.1    Albert, S.2    Chen, S.L.3    Zhong, B.X.4
  • 30
    • 0028002024 scopus 로고
    • Molecular cloning of two cDNAs from the head of the nurse honey bee (Apis mellifera L.) for coding related proteins of royal jelly
    • Klaudiny, J.; Hanes, J.; Kulifajova, J.; Albert, S.; Simuth, J. Molecular cloning of two cDNAs from the head of the nurse honey bee (Apis mellifera L.) for coding related proteins of royal jelly. J. Apic. Res. 1994, 33, 105-111.
    • (1994) J. Apic. Res , vol.33 , pp. 105-111
    • Klaudiny, J.1    Hanes, J.2    Kulifajova, J.3    Albert, S.4    Simuth, J.5
  • 31
    • 0035257551 scopus 로고    scopus 로고
    • Storage-dependant degradation of 57-kDa protein in royal jelly: A possible marker for freshness
    • Kamakura, M.; Fukuda, T.; Fukushima, M.; Yonekura, M. Storage-dependant degradation of 57-kDa protein in royal jelly: a possible marker for freshness. Biosci., Biotechnol., Biochem. 2001, 65, 277-284.
    • (2001) Biosci., Biotechnol., Biochem. , vol.65 , pp. 277-284
    • Kamakura, M.1    Fukuda, T.2    Fukushima, M.3    Yonekura, M.4
  • 32
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino, J. L.; Cregg, J. M. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 2000, 24, 45-66.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 33
    • 4644348208 scopus 로고    scopus 로고
    • Recombinant expression systems in the pharmaceutical industry
    • Schmidt, F. R. Recombinant expression systems in the pharmaceutical industry. Appl. Microbiol. Biotechnol. 2004, 65, 363-372.
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , pp. 363-372
    • Schmidt, F.R.1
  • 34
    • 77249147339 scopus 로고    scopus 로고
    • Engineering of protein secretion in yeast: Strategies and impact on protein production
    • Idiris, A.; Tohda, H.; Kumagai, H.; Takegaw, K. Engineering of protein secretion in yeast: strategies and impact on protein production. Appl. Microbiol. Biotechnol. 2010, 86, 403-417.
    • Appl. Microbiol. Biotechnol. , vol.2010 , Issue.86 , pp. 403-417
    • Idiris, A.1    Tohda, H.2    Kumagai, H.3    Takegaw, K.4
  • 36
    • 76749106494 scopus 로고    scopus 로고
    • Identification of the N-glycosylation sites on recombinant bovine CD38 expressed in Pichia pastoris: Their impact on enzyme stability and catalytic activity
    • Muller-Steffnera, H.; Kuhn, I.; Argentini, M.; Schuber, F. Identification of the N-glycosylation sites on recombinant bovine CD38 expressed in Pichia pastoris: their impact on enzyme stability and catalytic activity. Protein Express. Purif. 2010, 70, 151-157.
    • Protein Express. Purif , vol.2010 , Issue.70 , pp. 151-157
    • Muller-Steffnera, H.1    Kuhn, I.2    Argentini, M.3    Schuber, F.4
  • 37
    • 0001094662 scopus 로고    scopus 로고
    • Glycobiology: Toward understanding the function of sugars
    • Dwek, R. A. Glycobiology: toward understanding the function of sugars. Chem. Rev. 1996, 96, 683-720.
    • (1996) Chem. Rev , vol.96 , pp. 683-720
    • Dwek, R.A.1
  • 41
    • 2842588207 scopus 로고    scopus 로고
    • 350-kDa royal jelly glycoprotein (apisin), which stimulates proliferation of human monocytes, bears the β1-3 galactosylated N-glycan: Analysis of the N-glycosylation site
    • Kimura, M.; Kimura, Y.; Tsumura, K.; Okihara, K.; Sugimoto, H.; Yamad, H.; Yonekura, M. 350-kDa royal jelly glycoprotein (apisin), which stimulates proliferation of human monocytes, bears the β1-3 galactosylated N-glycan: analysis of the N-glycosylation site. Biosci., Biotechnol., Biochem. 2003, 67, 2055-2058.
    • (2003) Biosci., Biotechnol., Biochem , vol.67 , pp. 2055-2058
    • Kimura, M.1    Kimura, Y.2    Tsumura, K.3    Okihara, K.4    Sugimoto, H.5    Yamad, H.6    Yonekura, M.7
  • 43


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