메뉴 건너뛰기




Volumn 63, Issue 2, 2009, Pages 75-83

Overexpression of homogeneous and active ABCG2 in insect cells

Author keywords

ABCG2 breast cancer resistance protein; Baculovirus insect cells; Chemical chaperones; Heterologous protein overexpression; Membrane protein maturation; Translation and transcription inhibitors

Indexed keywords

HEXAPODA;

EID: 56349140193     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.09.021     Document Type: Article
Times cited : (5)

References (55)
  • 1
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano R.L., and Ling V. A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants. Biochim. Biophys. Acta 455 (1976) 152-162
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 3
    • 0032404092 scopus 로고    scopus 로고
    • A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome 4q22 that is involved in multidrug resistance
    • Allikmets R., Schriml L.M., Hutchinson A., Romano-Spica V., and Dean M. A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome 4q22 that is involved in multidrug resistance. Cancer Res. 58 (1998) 5337-5339
    • (1998) Cancer Res. , vol.58 , pp. 5337-5339
    • Allikmets, R.1    Schriml, L.M.2    Hutchinson, A.3    Romano-Spica, V.4    Dean, M.5
  • 6
    • 0026496549 scopus 로고
    • Reduced intracellular drug accumulation in the absence of P-glycoprotein (mdr1) overexpression in mitoxantrone-resistant human MCF-7 breast cancer cells
    • Nakagawa M., Schneider E., Dixon K.H., Horton J., Kelley K., Morrow C., and Cowan K.H. Reduced intracellular drug accumulation in the absence of P-glycoprotein (mdr1) overexpression in mitoxantrone-resistant human MCF-7 breast cancer cells. Cancer Res. 52 (1992) 6175-6181
    • (1992) Cancer Res. , vol.52 , pp. 6175-6181
    • Nakagawa, M.1    Schneider, E.2    Dixon, K.H.3    Horton, J.4    Kelley, K.5    Morrow, C.6    Cowan, K.H.7
  • 8
    • 0042354831 scopus 로고    scopus 로고
    • Transport of methotrexate, methotrexate polyglutamates, and 17beta-estradiol 17-(beta-d-glucuronide) by ABCG2: effects of acquired mutations at R482 on methotrexate transport
    • Chen Z.S., Robey R.W., Belinsky M.G., Shchaveleva I., Ren X.Q., Sugimoto Y., Ross D.D., Bates S.E., and Kruh G.D. Transport of methotrexate, methotrexate polyglutamates, and 17beta-estradiol 17-(beta-d-glucuronide) by ABCG2: effects of acquired mutations at R482 on methotrexate transport. Cancer Res. 63 (2003) 4048-4054
    • (2003) Cancer Res. , vol.63 , pp. 4048-4054
    • Chen, Z.S.1    Robey, R.W.2    Belinsky, M.G.3    Shchaveleva, I.4    Ren, X.Q.5    Sugimoto, Y.6    Ross, D.D.7    Bates, S.E.8    Kruh, G.D.9
  • 12
    • 0038757689 scopus 로고    scopus 로고
    • Sterol transport by the human breast cancer resistance protein (ABCG2) expressed in Lactococcus lactis
    • Janvilisri T., Venter H., Shahi S., Reuter G., Balakrishnan L., and van Veen H.W. Sterol transport by the human breast cancer resistance protein (ABCG2) expressed in Lactococcus lactis. J. Biol. Chem. 278 (2003) 20645-20651
    • (2003) J. Biol. Chem. , vol.278 , pp. 20645-20651
    • Janvilisri, T.1    Venter, H.2    Shahi, S.3    Reuter, G.4    Balakrishnan, L.5    van Veen, H.W.6
  • 13
    • 3042765579 scopus 로고    scopus 로고
    • Functional expression of the human breast cancer resistance protein in Pichia pastoris
    • Mao Q., Conseil G., Gupta A., Cole S.P., and Unadkat J.D. Functional expression of the human breast cancer resistance protein in Pichia pastoris. Biochem. Biophys. Res. Commun. 320 (2004) 730-737
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 730-737
    • Mao, Q.1    Conseil, G.2    Gupta, A.3    Cole, S.P.4    Unadkat, J.D.5
  • 15
    • 19644378841 scopus 로고    scopus 로고
    • Flavonoid structure-activity studies identify 6-prenylchrysin and tectochrysin as potent and specific inhibitors of breast cancer resistance protein ABCG2
    • Ahmed-Belkacem A., Pozza A., Munoz-Martinez F., Bates S.E., Castanys S., Gamarro F., Perez-Victoria J.M., and Di Pietro A. Flavonoid structure-activity studies identify 6-prenylchrysin and tectochrysin as potent and specific inhibitors of breast cancer resistance protein ABCG2. Cancer Res. 65 (2005) 4852-4860
    • (2005) Cancer Res. , vol.65 , pp. 4852-4860
    • Ahmed-Belkacem, A.1    Pozza, A.2    Munoz-Martinez, F.3    Bates, S.E.4    Castanys, S.5    Gamarro, F.6    Perez-Victoria, J.M.7    Di Pietro, A.8
  • 18
    • 0345735768 scopus 로고    scopus 로고
    • Functional characterisation of human breast cancer resistance protein (BCRP, ABCG2) expressed in the oocytes of Xenopus laevis
    • Nakanishi T., Doyle L.A., Hassel B., Wei Y., Bauer K.S., Wu S., Pumplin D.W., Fang H.D., and Ross D.D. Functional characterisation of human breast cancer resistance protein (BCRP, ABCG2) expressed in the oocytes of Xenopus laevis. Mol. Pharmacol. 64 (2003) 1452-1462
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1452-1462
    • Nakanishi, T.1    Doyle, L.A.2    Hassel, B.3    Wei, Y.4    Bauer, K.S.5    Wu, S.6    Pumplin, D.W.7    Fang, H.D.8    Ross, D.D.9
  • 23
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 95 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 24
    • 0026672405 scopus 로고
    • ATPase activity of partially purified P-glycoprotein from multidrug-resistant Chinese hamster ovary cells
    • Doige C.A., Yu X., and Sharom F.J. ATPase activity of partially purified P-glycoprotein from multidrug-resistant Chinese hamster ovary cells. Biochim. Biophys. Acta 1109 (1992) 149-160
    • (1992) Biochim. Biophys. Acta , vol.1109 , pp. 149-160
    • Doige, C.A.1    Yu, X.2    Sharom, F.J.3
  • 26
    • 33748742271 scopus 로고    scopus 로고
    • Protein N-glycosylation in the baculovirus-insect cell expression system and engineering of insect cells to produce "Mammalianized" recombinant glycoprotein
    • Harrison R.L., and Jarvis D.L. Protein N-glycosylation in the baculovirus-insect cell expression system and engineering of insect cells to produce "Mammalianized" recombinant glycoprotein. Adv. Virus Res. 68 (2006) 159-191
    • (2006) Adv. Virus Res. , vol.68 , pp. 159-191
    • Harrison, R.L.1    Jarvis, D.L.2
  • 27
    • 16844386327 scopus 로고    scopus 로고
    • N-linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane
    • Diop N.K., and Hrycyna C.A. N-linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane. Biochemistry 44 (2005) 5420-5429
    • (2005) Biochemistry , vol.44 , pp. 5420-5429
    • Diop, N.K.1    Hrycyna, C.A.2
  • 28
    • 0015731292 scopus 로고
    • A high resolution PAS stain for polyacrylamide gel electrophoresis
    • Kapitanay R.A., and Zebrowski E.J. A high resolution PAS stain for polyacrylamide gel electrophoresis. Anal. Biochem. 56 (1973) 361-369
    • (1973) Anal. Biochem. , vol.56 , pp. 361-369
    • Kapitanay, R.A.1    Zebrowski, E.J.2
  • 29
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5 (1994) 253-265
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 30
    • 0141730230 scopus 로고    scopus 로고
    • The contribution of N-linked glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis
    • Trombetta E.S. The contribution of N-linked glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis. Glycobiology 13 (2003) 77R-91R
    • (2003) Glycobiology , vol.13
    • Trombetta, E.S.1
  • 31
    • 0030154323 scopus 로고    scopus 로고
    • Influence of molecular and chemical chaperones on protein folding
    • Welch W.J., and Brown C.R. Influence of molecular and chemical chaperones on protein folding. Cell Stress Chaperon. 1 (1996) 109-115
    • (1996) Cell Stress Chaperon. , vol.1 , pp. 109-115
    • Welch, W.J.1    Brown, C.R.2
  • 32
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • Denning G.M., Anderson M.P., Amara J.F., Marshall J., Smith A.E., and Welsh M.J. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358 (1992) 761-764
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 34
    • 12444283809 scopus 로고    scopus 로고
    • Structure and dynamics of the Golgi complex at 15 °C: low temperature induces the formation of Golgi-derived tubules
    • Martinez-Alonso E., Egea G., Ballesta J., and Martinez-Menarguez J.A. Structure and dynamics of the Golgi complex at 15 °C: low temperature induces the formation of Golgi-derived tubules. Traffic 6 (2005) 32-44
    • (2005) Traffic , vol.6 , pp. 32-44
    • Martinez-Alonso, E.1    Egea, G.2    Ballesta, J.3    Martinez-Menarguez, J.A.4
  • 35
    • 0037450544 scopus 로고    scopus 로고
    • Specific lipid requirement of membrane proteins-a putative bottleneck in heterologous expression
    • Opekarova M., and Tanner W. Specific lipid requirement of membrane proteins-a putative bottleneck in heterologous expression. Biochim. Biophys. Acta 1610 (2003) 11-22
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 11-22
    • Opekarova, M.1    Tanner, W.2
  • 36
    • 0344820768 scopus 로고    scopus 로고
    • Lipid composition of Spodoptera frugiperda (Sf9) and Trichoplusia ni (Tn) insect cells used for baculovirus infection
    • Marheineke K., Gruënewald S., Christie W., and Reilaënder H. Lipid composition of Spodoptera frugiperda (Sf9) and Trichoplusia ni (Tn) insect cells used for baculovirus infection. FEBS Lett. 441 (1998) 49-52
    • (1998) FEBS Lett. , vol.441 , pp. 49-52
    • Marheineke, K.1    Gruënewald, S.2    Christie, W.3    Reilaënder, H.4
  • 37
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • Lichtenberg D., Goni F.M., and Heerklotz H. Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem. Sci. 30 (2005) 429-436
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 429-436
    • Lichtenberg, D.1    Goni, F.M.2    Heerklotz, H.3
  • 39
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger H. Tricine-SDS-PAGE. Nat. Protoc. 1 (2006) 16-23
    • (2006) Nat. Protoc. , vol.1 , pp. 16-23
    • Schägger, H.1
  • 40
    • 0024346677 scopus 로고
    • Hydrophobic organization of membrane proteins
    • Rees D.C., De Antonio L., and Eisenberg D. Hydrophobic organization of membrane proteins. Science 245 (1989) 510-513
    • (1989) Science , vol.245 , pp. 510-513
    • Rees, D.C.1    De Antonio, L.2    Eisenberg, D.3
  • 41
    • 0029019585 scopus 로고
    • On the distribution of amino acid residues in transmembrane α-helix bundles
    • Samatey F.A., Xu C., and Popot J.L. On the distribution of amino acid residues in transmembrane α-helix bundles. Proc. Natl. Acad. Sci. USA 92 (1995) 4577-4581
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4577-4581
    • Samatey, F.A.1    Xu, C.2    Popot, J.L.3
  • 42
    • 0001041988 scopus 로고    scopus 로고
    • Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: evaluation of reversible unfolding conditions
    • Chen G.Q., and Gouaux E. Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: evaluation of reversible unfolding conditions. Biochemistry 38 (1999) 15380-15387
    • (1999) Biochemistry , vol.38 , pp. 15380-15387
    • Chen, G.Q.1    Gouaux, E.2
  • 43
    • 0030272670 scopus 로고    scopus 로고
    • Time-resolved biophysical methods in the study of protein folding
    • Plaxco K.W., and Dobson C.M. Time-resolved biophysical methods in the study of protein folding. Curr. Opin. Struc. Biol. 6 (1996) 630-636
    • (1996) Curr. Opin. Struc. Biol. , vol.6 , pp. 630-636
    • Plaxco, K.W.1    Dobson, C.M.2
  • 44
    • 33846901901 scopus 로고    scopus 로고
    • Intermediates: ubiquitous species on folding energy landscapes?
    • Brockwell D.J., and Radford S.E. Intermediates: ubiquitous species on folding energy landscapes?. Curr. Opin. Struc. Biol. 17 (2007) 30-37
    • (2007) Curr. Opin. Struc. Biol. , vol.17 , pp. 30-37
    • Brockwell, D.J.1    Radford, S.E.2
  • 45
    • 43949145273 scopus 로고    scopus 로고
    • Amelioration of protein misfolding disease by rapamycin; translation or autophagy?
    • Wyttenbach A., Hands S., King M.A., Lipkow K., and Tolkovsky A.M. Amelioration of protein misfolding disease by rapamycin; translation or autophagy?. Autophagy 4 (2008) 542-545
    • (2008) Autophagy , vol.4 , pp. 542-545
    • Wyttenbach, A.1    Hands, S.2    King, M.A.3    Lipkow, K.4    Tolkovsky, A.M.5
  • 46
    • 41149159767 scopus 로고    scopus 로고
    • Rapamycin inhibits polyglutamine aggregation independently of autophagy by reducing protein synthesis
    • King M.A., Hands S., Hafiz F., Mizushima N., Tolkovsky A.M., and Wyttenbach A. Rapamycin inhibits polyglutamine aggregation independently of autophagy by reducing protein synthesis. Mol. Pharmacol. 73 (2008) 1052-1062
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1052-1062
    • King, M.A.1    Hands, S.2    Hafiz, F.3    Mizushima, N.4    Tolkovsky, A.M.5    Wyttenbach, A.6
  • 47
    • 18844456347 scopus 로고    scopus 로고
    • Protein synthesis inhibitors and the chemical chaperone TMAO reverse endoplasmic reticulum perturbation induced by overexpression of the iodide transporter pendrin
    • Shepshelovich J., Goldstein-Magal L., Globerson A., Yen P.M., Rotman-Pikielny P., and Hirschberg K. Protein synthesis inhibitors and the chemical chaperone TMAO reverse endoplasmic reticulum perturbation induced by overexpression of the iodide transporter pendrin. J. Cell Sci. 118 (2005) 1577-1586
    • (2005) J. Cell Sci. , vol.118 , pp. 1577-1586
    • Shepshelovich, J.1    Goldstein-Magal, L.2    Globerson, A.3    Yen, P.M.4    Rotman-Pikielny, P.5    Hirschberg, K.6
  • 48
    • 0027256737 scopus 로고
    • Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions
    • Schmid F.X. Prolyl isomerase: enzymatic catalysis of slow protein-folding reactions. Annu. Rev. Biophys. Biomed. 22 (1993) 123-142
    • (1993) Annu. Rev. Biophys. Biomed. , vol.22 , pp. 123-142
    • Schmid, F.X.1
  • 51
    • 0036303981 scopus 로고    scopus 로고
    • Hassles with taking out the garbage: aggravating aggresomes
    • Garcia-Mata R., Gao Y.S., and Sztul E. Hassles with taking out the garbage: aggravating aggresomes. Traffic 3 (2002) 388-396
    • (2002) Traffic , vol.3 , pp. 388-396
    • Garcia-Mata, R.1    Gao, Y.S.2    Sztul, E.3
  • 52
    • 0034278759 scopus 로고    scopus 로고
    • Aggresomes and Russell bodies. Symptoms of cellular indigestion?
    • Kopito R.R., and Sitia R. Aggresomes and Russell bodies. Symptoms of cellular indigestion?. EMBO Rep. 1 (2000) 225-231
    • (2000) EMBO Rep. , vol.1 , pp. 225-231
    • Kopito, R.R.1    Sitia, R.2
  • 53
    • 23844530574 scopus 로고    scopus 로고
    • Oligomerization of the human ABC transporter ABCG2: evaluation of the native protein and chimeric dimers
    • Bhatia A., Schäfer H.J., and Hrycyna C.A. Oligomerization of the human ABC transporter ABCG2: evaluation of the native protein and chimeric dimers. Biochemistry 44 (2005) 10893-10904
    • (2005) Biochemistry , vol.44 , pp. 10893-10904
    • Bhatia, A.1    Schäfer, H.J.2    Hrycyna, C.A.3
  • 54
    • 27744459366 scopus 로고    scopus 로고
    • Identification of intra- and intermolecular disulfide bridges in the multidrug resistance transporter ABCG2
    • Henriksen U., Fog J.U., Litman T., and Gether U. Identification of intra- and intermolecular disulfide bridges in the multidrug resistance transporter ABCG2. J. Biol. Chem. 280 (2005) 36926-36934
    • (2005) J. Biol. Chem. , vol.280 , pp. 36926-36934
    • Henriksen, U.1    Fog, J.U.2    Litman, T.3    Gether, U.4
  • 55
    • 33646000631 scopus 로고    scopus 로고
    • Complex folding kinetics of a multidomain protein
    • Batey S., Scott K.A., and Clarke J. Complex folding kinetics of a multidomain protein. Biophys. J. 90 (2006) 2120-2130
    • (2006) Biophys. J. , vol.90 , pp. 2120-2130
    • Batey, S.1    Scott, K.A.2    Clarke, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.