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Volumn 648, Issue , 2010, Pages 139-159

Production of cells with targeted integration of gene variants of human ABC transporter for stable and regulated expression using the Flp recombinase system

Author keywords

Aggresome; ATP binding cassette (ABC) transporter; Endoplasmic reticulum associated degradation (ERAD); Flp recombinase; Genetic polymorphisms; N linked glycosylation; Proteasome

Indexed keywords

BREAST CANCER RESISTANCE PROTEIN; COMPLEMENTARY DNA; GENOMIC DNA; RECOMBINASE; ABC TRANSPORTER; ABCG2 PROTEIN, HUMAN; DNA POLYMERASE; TUMOR PROTEIN;

EID: 79952016115     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-60761-756-3_9     Document Type: Chapter
Times cited : (10)

References (48)
  • 1
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgaard L, Molinari M, Helenius A (1999) Setting the standards: quality control in the secretory pathway. Science 286:1882–1888
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181:223–230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • Tu BP, Weissman JS (2004) Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164:341–346
    • (2004) J Cell Biol , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 4
    • 0037053397 scopus 로고    scopus 로고
    • Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobu-lin folding complex
    • Sargsyan E, Baryshev M, Szekely L, Sharipo A, Mkrtchian S (2002) Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobu-lin folding complex. J Biol Chem 277: 17009–17015
    • (2002) J Biol Chem , vol.277 , pp. 17009-17015
    • Sargsyan, E.1    Baryshev, M.2    Szekely, L.3    Sharipo, A.4    Mkrtchian, S.5
  • 6
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A, Aebi M (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73:1019–1049
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 7
    • 0034716887 scopus 로고    scopus 로고
    • Tripartite management of unfolded proteins in the endoplasmic reticulum
    • Mori K (2000) Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell 101:451–454
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 8
    • 0035424237 scopus 로고    scopus 로고
    • ER quality control: Towards an understanding at the molecular level
    • Ellgaard L, Helenius A (2001) ER quality control: towards an understanding at the molecular level. Curr Opin Cell Biol 13: 431–437
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 431-437
    • Ellgaard, L.1    Helenius, A.2
  • 9
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton RY (2002) ER-associated degradation in protein quality control and cellular regulation. Curr Opin Cell Biol 14:476–482
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 10
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen B, Braakman I (2004) Protein folding and quality control in the endoplasmic reticulum. Curr Opin Cell Biol 16:343–349
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 11
    • 37649025515 scopus 로고    scopus 로고
    • Dissecting the ER-associated degradation of a misfolded polytopic membrane protein
    • Nakatsukasa K, Huyer G, Michaelis S, Brodsky JL (2008) Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 132:101–112
    • (2008) Cell , vol.132 , pp. 101-112
    • Nakatsukasa, K.1    Huyer, G.2    Michaelis, S.3    Brodsky, J.L.4
  • 14
    • 59049084011 scopus 로고    scopus 로고
    • Physiological and pharmacological roles of ABCG2 (BCRP): Recent findings in Abcg2 knockout mice
    • Vlaming ML, Lagas JS, Schinkel AH (2009) Physiological and pharmacological roles of ABCG2 (BCRP): recent findings in Abcg2 knockout mice. Adv Drug Deliv Rev 61: 14–25
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 14-25
    • Vlaming, M.L.1    Lagas, J.S.2    Schinkel, A.H.3
  • 15
    • 0037050736 scopus 로고    scopus 로고
    • Dominant-negative inhibition of breast cancer resistance protein as drug efflux pump through the inhibition of S-S dependent homodimerization
    • Kage K, Tsukahara S, Sugiyama T, Asada S, Ishikawa E, Tsuruo T, Sugimoto Y (2002) Dominant-negative inhibition of breast cancer resistance protein as drug efflux pump through the inhibition of S-S dependent homodimerization. Int J Cancer 97: 626–630
    • (2002) Int J Cancer , vol.97 , pp. 626-630
    • Kage, K.1    Tsukahara, S.2    Sugiyama, T.3    Asada, S.4    Ishikawa, E.5    Tsuruo, T.6    Sugimoto, Y.7
  • 16
    • 0042068263 scopus 로고    scopus 로고
    • A functional study on polymorphism of the ATP-binding cassette transporter ABCG2: Critical role of arginine-482 in methotrexate transport
    • Mitomo H, Kato R, Ito A, Kasamatsu S, Ikegami Y, Kii I, Kudo A, Kobatake E, Sumino Y, Ishikawa T (2003) A functional study on polymorphism of the ATP-binding cassette transporter ABCG2: critical role of arginine-482 in methotrexate transport. Biochem J 373: 767–774
    • (2003) Biochem J , vol.373 , pp. 767-774
    • Mitomo, H.1    Kato, R.2    Ito, A.3    Kasamatsu, S.4    Ikegami, Y.5    Kii, I.6    Kudo, A.7    Kobatake, E.8    Sumino, Y.9    Ishikawa, T.10
  • 17
    • 30344485123 scopus 로고    scopus 로고
    • Role of Cys-603 in dimer/oligomer formation of the breast cancer resistance protein BCRP/ ABCG2
    • Kage K, Fujita T, Sugimoto Y (2005) Role of Cys-603 in dimer/oligomer formation of the breast cancer resistance protein BCRP/ ABCG2. Cancer Sci 96:866–872
    • (2005) Cancer Sci , vol.96 , pp. 866-872
    • Kage, K.1    Fujita, T.2    Sugimoto, Y.3
  • 18
    • 27744459366 scopus 로고    scopus 로고
    • Identification of intra-and intermo-lecular disulfide bridges in the multidrug resistance transporter ABCG2
    • Henriksen U, Fog JU, Litman T, Gether U (2005) Identification of intra-and intermo-lecular disulfide bridges in the multidrug resistance transporter ABCG2. J Biol Chem 280:36926–36934
    • (2005) J Biol Chem , vol.280 , pp. 36926-36934
    • Henriksen, U.1    Fog, J.U.2    Litman, T.3    Gether, U.4
  • 19
    • 33646703561 scopus 로고    scopus 로고
    • Identification of cysteine residues critically involved in homodimer formation and protein expression of human ATP-binding cassette transporter ABCG2: A new approach using the flp recombinase system
    • Wakabayashi K, Nakagawa H, Adachi T, Kii I, Kobatake E, Kudo A, Ishikawa T (2006) Identification of cysteine residues critically involved in homodimer formation and protein expression of human ATP-binding cassette transporter ABCG2: a new approach using the flp recombinase system. J Exp Ther Oncol 5:205–222
    • (2006) J Exp Ther Oncol , vol.5 , pp. 205-222
    • Wakabayashi, K.1    Nakagawa, H.2    Adachi, T.3    Kii, I.4    Kobatake, E.5    Kudo, A.6    Ishikawa, T.7
  • 20
    • 34948910289 scopus 로고    scopus 로고
    • Intramolecular disulfide bond is a critical check point determining degradative fates of ATP-binding cassette (ABC) transporter ABCG2 protein
    • Wakabayashi K, Nakagawa H, Tamura A, Koshiba S, Hoshijima K, Komada M, Ishikawa T (2007) Intramolecular disulfide bond is a critical check point determining degradative fates of ATP-binding cassette (ABC) transporter ABCG2 protein. J Biol Chem 282:27841–27846
    • (2007) J Biol Chem , vol.282 , pp. 27841-27846
    • Wakabayashi, K.1    Nakagawa, H.2    Tamura, A.3    Koshiba, S.4    Hoshijima, K.5    Komada, M.6    Ishikawa, T.7
  • 21
    • 71949113235 scopus 로고    scopus 로고
    • Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of human ATP-binding cassette transporter ABCG2
    • Nakagawa H, Wakabayashi-Nakao K, Tamura A, Toyoda Y, Koshiba S, Ishikawa T (2009) Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of human ATP-binding cassette transporter ABCG2. FEBS J. 276:7237–7252
    • (2009) FEBS J , vol.276 , pp. 7237-7252
    • Nakagawa, H.1    Wakabayashi-Nakao, K.2    Tamura, A.3    Toyoda, Y.4    Koshiba, S.5    Ishikawa, T.6
  • 22
    • 33846063389 scopus 로고    scopus 로고
    • Genetic polymorphisms of human ABC transporter ABCG2: Development of the standard method for functional validation of SNPs by using the Flp recombinase system
    • Tamura A, Wakabayashi K, Onishi Y, Nakagawa H, Tsuji M, Matsuda Y, Ishikawa T (2006) Genetic polymorphisms of human ABC transporter ABCG2: development of the standard method for functional validation of SNPs by using the Flp recombinase system. J Exp Ther Oncol 6:1–11
    • (2006) J Exp Ther Oncol , vol.6 , pp. 1-11
    • Tamura, A.1    Wakabayashi, K.2    Onishi, Y.3    Nakagawa, H.4    Tsuji, M.5    Matsuda, Y.6    Ishikawa, T.7
  • 23
    • 33845655480 scopus 로고    scopus 로고
    • Re-evaluation and functional classification of non-synonymous single nucleotide polymorphisms of the human ATP-binding cassette transporter ABCG2
    • Tamura A, Wakabayashi K, Onishi Y, Takeda M, Ikegami Y, Sawada S, Tsuji M, Matsuda Y, Ishikawa T (2007) Re-evaluation and functional classification of non-synonymous single nucleotide polymorphisms of the human ATP-binding cassette transporter ABCG2. Cancer Sci 98:231–239
    • (2007) Cancer Sci , vol.98 , pp. 231-239
    • Tamura, A.1    Wakabayashi, K.2    Onishi, Y.3    Takeda, M.4    Ikegami, Y.5    Sawada, S.6    Tsuji, M.7    Matsuda, Y.8    Ishikawa, T.9
  • 25
    • 58549097067 scopus 로고    scopus 로고
    • Major SNP (Q141K) variant of human ABC transporter ABCG2 undergoes lysosomal and proteasomal degradations
    • Furukawa T, Wakabayashi K, Tamura A, Nakagawa H, Morishima Y, Osawa Y, Ishikawa T (2009) Major SNP (Q141K) variant of human ABC transporter ABCG2 undergoes lysosomal and proteasomal degradations. Pharm Res 26:469–479
    • (2009) Pharm Res , vol.26 , pp. 469-479
    • Furukawa, T.1    Wakabayashi, K.2    Tamura, A.3    Nakagawa, H.4    Morishima, Y.5    Osawa, Y.6    Ishikawa, T.7
  • 26
  • 27
    • 59049087689 scopus 로고    scopus 로고
    • Quality control of human ABCG2 protein in the endoplasmic reticulum: Ubiquitination and proteasomal degradation
    • Wakabayashi-Nakao K, Tamura A, Furukawa T, Nakagawa H, Ishikawa T (2009) Quality control of human ABCG2 protein in the endoplasmic reticulum: ubiquitination and proteasomal degradation. Adv Drug Deliv Rev 61:66–72
    • (2009) Adv Drug Deliv Rev , vol.61 , pp. 66-72
    • Wakabayashi-Nakao, K.1    Tamura, A.2    Furukawa, T.3    Nakagawa, H.4    Ishikawa, T.5
  • 28
    • 0025847620 scopus 로고
    • Recombinase-mediated gene activation and site-specific integration in mammalian cells
    • O’Gorman S, Fox DT, Wahl GM (1991) Recombinase-mediated gene activation and site-specific integration in mammalian cells. Science 251:1351–1355
    • (1991) Science , vol.251 , pp. 1351-1355
    • O’Gorman, S.1    Fox, D.T.2    Wahl, G.M.3
  • 29
    • 0028148244 scopus 로고
    • Site-specific recombination: Developments and applications
    • Sauer B (1994) Site-specific recombination: developments and applications. Curr Opin Biotechnol 5:521–527
    • (1994) Curr Opin Biotechnol , vol.5 , pp. 521-527
    • Sauer, B.1
  • 30
    • 0031053576 scopus 로고    scopus 로고
    • Positive selection of FLP- mediated unequal sister chromatid exchange products in mammalian cells
    • Aladjem MI, Brody LL, O’Gorman S, Wahl GM (1997) Positive selection of FLP- mediated unequal sister chromatid exchange products in mammalian cells. Mol Cell Biol 17:857–861
    • (1997) Mol Cell Biol , vol.17 , pp. 857-861
    • Aladjem, M.I.1    Brody, L.L.2    O’Gorman, S.3    Wahl, G.M.4
  • 31
    • 0032903245 scopus 로고    scopus 로고
    • Sequential gene disruption in Candida albicans by FLP-mediated site-specific recombination
    • Morschhauser J, Michel S, Staib P (1999) Sequential gene disruption in Candida albicans by FLP-mediated site-specific recombination. Mol Microbiol 32:547–556
    • (1999) Mol Microbiol , vol.32 , pp. 547-556
    • Morschhauser, J.1    Michel, S.2    Staib, P.3
  • 33
    • 0037423742 scopus 로고    scopus 로고
    • Stepwise manipulation of DNA specificity in Flp recombinase: Progressively adapting Flp to individual and combinatorial mutations in its target site
    • Voziyanov Y, Konieczka JH, Stewart AF, Jayaram M (2003) Stepwise manipulation of DNA specificity in Flp recombinase: progressively adapting Flp to individual and combinatorial mutations in its target site. J Mol Biol 326:65–76
    • (2003) J Mol Biol , vol.326 , pp. 65-76
    • Voziyanov, Y.1    Konieczka, J.H.2    Stewart, A.F.3    Jayaram, M.4
  • 34
    • 4644332204 scopus 로고    scopus 로고
    • Flp-mediated integration of expression cassettes into FRT-tagged chromosomal loci in mammalian cells
    • Wirth D, Hauser H (2004) Flp-mediated integration of expression cassettes into FRT-tagged chromosomal loci in mammalian cells. Methods Mol Biol 267:467–476
    • (2004) Methods Mol Biol , vol.267 , pp. 467-476
    • Wirth, D.1    Hauser, H.2
  • 35
    • 0022388399 scopus 로고
    • Determination of DNA sequences essential for FLP-mediated recombination by a novel method
    • Gronostajski RM, Sadowski PD (1985) Determination of DNA sequences essential for FLP-mediated recombination by a novel method. J Biol Chem 260:12320–12327
    • (1985) J Biol Chem , vol.260 , pp. 12320-12327
    • Gronostajski, R.M.1    Sadowski, P.D.2
  • 36
    • 0022399815 scopus 로고
    • Two-micrometer circle site-specific recombination: The minimal substrate and the possible role of flanking sequences
    • Jayaram M (1985) Two-micrometer circle site-specific recombination: the minimal substrate and the possible role of flanking sequences. Proc Natl Acad Sci U S A 82:5875–5879
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 5875-5879
    • Jayaram, M.1
  • 37
    • 0022378550 scopus 로고
    • The FLP recombinase of the yeast 2-micron plasmid: Characterization of its recombination site
    • Senecoff JF, Bruckner RC, Cox MM (1985) The FLP recombinase of the yeast 2-micron plasmid: characterization of its recombination site. Proc Natl Acad Sci U S A 82: 7270–7274
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 7270-7274
    • Senecoff, J.F.1    Bruckner, R.C.2    Cox, M.M.3
  • 38
    • 0021972533 scopus 로고
    • The FLP recombinase of the 2 micron circle DNA of yeast: Interaction with its target sequences
    • Andrews BJ, Proteau GA, Beatty LG, Sadowski PD (1985) The FLP recombinase of the 2 micron circle DNA of yeast: interaction with its target sequences. Cell 40:795–803
    • (1985) Cell , vol.40 , pp. 795-803
    • Andrews, B.J.1    Proteau, G.A.2    Beatty, L.G.3    Sadowski, P.D.4
  • 39
    • 0022371467 scopus 로고
    • A very strong enhancer is located upstream of an immediate early gene of human cytomegalovirus
    • Boshart M, Weber F, Jahn G, Dorsch-Hasler K, Fleckenstein B, Schaffner W (1985) A very strong enhancer is located upstream of an immediate early gene of human cytomegalovirus. Cell 41:521–530
    • (1985) Cell , vol.41 , pp. 521-530
    • Boshart, M.1    Weber, F.2    Jahn, G.3    Dorsch-Hasler, K.4    Fleckenstein, B.5    Schaffner, W.6
  • 40
    • 0023444881 scopus 로고
    • Negative and positive regulation by a short segment in the 5’-flanking region of the human cytomegalovirus major immediate-early gene
    • Nelson JA, Reynolds-Kohler C, Smith BA (1987) Negative and positive regulation by a short segment in the 5’-flanking region of the human cytomegalovirus major immediate-early gene. Mol Cell Biol 7:4125–4129
    • (1987) Mol Cell Biol , vol.7 , pp. 4125-4129
    • Nelson, J.A.1    Reynolds-Kohler, C.2    Smith, B.A.3
  • 41
    • 0024394549 scopus 로고
    • Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
    • Andersson S, Davis DL, Dahlback H, Jornvall H, Russell DW (1989) Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J Biol Chem 264:8222–8229
    • (1989) J Biol Chem , vol.264 , pp. 8222-8229
    • Andersson, S.1    Davis, D.L.2    Dahlback, H.3    Jornvall, H.4    Russell, D.W.5
  • 42
    • 0021078994 scopus 로고
    • Plasmid-encoded hygromycin B resistance: The sequence of hygromycin B phosphotransferase gene and its expression in Escherichia coli and Saccharomyces cerevisiae
    • Gritz L, Davies J (1983) Plasmid-encoded hygromycin B resistance: the sequence of hygromycin B phosphotransferase gene and its expression in Escherichia coli and Saccharomyces cerevisiae. Gene 25: 179–188
    • (1983) Gene , vol.25 , pp. 179-188
    • Gritz, L.1    Davies, J.2
  • 43
    • 0018955095 scopus 로고
    • Replication and recombination functions associated with the yeast plasmid, 2 mu circle
    • Broach JR, Hicks JB (1980) Replication and recombination functions associated with the yeast plasmid, 2 mu circle. Cell 21:501–508
    • (1980) Cell , vol.21 , pp. 501-508
    • Broach, J.R.1    Hicks, J.B.2
  • 44
    • 0020132004 scopus 로고
    • Recombination within the yeast plasmid 2mu circle is site-specific
    • Broach JR, Guarascio VR, Jayaram M (1982) Recombination within the yeast plasmid 2mu circle is site-specific. Cell 29:227–234
    • (1982) Cell , vol.29 , pp. 227-234
    • Broach, J.R.1    Guarascio, V.R.2    Jayaram, M.3
  • 46
    • 0024236673 scopus 로고
    • The mechanism of conservative site-specific recombination
    • Craig NL (1988) The mechanism of conservative site-specific recombination. Annu Rev Genet 22: 77–105
    • (1988) Annu Rev Genet , vol.22 , pp. 77-105
    • Craig, N.L.1
  • 47
    • 0029860719 scopus 로고    scopus 로고
    • Different thermostabili-ties of FLP and Cre recombinases: Implications for applied site-specific recombination
    • Buchholz F, Ringrose L, Angrand PO, Rossi F, Stewart AF (1996) Different thermostabili-ties of FLP and Cre recombinases: implications for applied site-specific recombination. Nucleic Acids Res 24:4256–4262
    • (1996) Nucleic Acids Res , vol.24 , pp. 4256-4262
    • Buchholz, F.1    Ringrose, L.2    Angrand, P.O.3    Rossi, F.4    Stewart, A.F.5
  • 48
    • 1242319383 scopus 로고    scopus 로고
    • Single nucleotide polymorphisms results in impaired membrane localization and reduced ATPase activity in multidrug transporter ABCG2
    • Mizuarai S, Aozasa N, Kotani H (2004) Single nucleotide polymorphisms results in impaired membrane localization and reduced ATPase activity in multidrug transporter ABCG2. Int J Cancer 109:238–246
    • (2004) Int J Cancer , vol.109 , pp. 238-246
    • Mizuarai, S.1    Aozasa, N.2    Kotani, H.3


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