메뉴 건너뛰기




Volumn 14, Issue 1, 2009, Pages 49-60

Calnexin overexpression sensitizes recombinant CHO cells to apoptosis induced by sodium butyrate treatment

Author keywords

Apoptosis; Calnexin; Chinese hamster ovary (CHO) cells

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; BUTYRIC ACID; CALCIUM; CALNEXIN; CYTOCHROME C; TUMOR NECROSIS FACTOR RECEPTOR; DOXORUBICIN; TETRACYCLINE;

EID: 67649232964     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-008-0054-0     Document Type: Article
Times cited : (11)

References (64)
  • 1
    • 0037195869 scopus 로고    scopus 로고
    • Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria
    • Arnaudeau S, Frieden M, Nakamura K, Castelbou C, Michalak M, Demaurex N (2002) Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria. J Biol Chem 277:46696-46705
    • (2002) J Biol Chem , vol.277 , pp. 46696-46705
    • Arnaudeau, S.1    Frieden, M.2    Nakamura, K.3    Castelbou, C.4    Michalak, M.5    Demaurex, N.6
  • 2
    • 0032482220 scopus 로고    scopus 로고
    • Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization
    • Bass J, Chiu G, Argon Y, Steiner DF (1998) Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization. J Cell Biol 141:637-646
    • (1998) J Cell Biol , vol.141 , pp. 637-646
    • Bass, J.1    Chiu, G.2    Argon, Y.3    Steiner, D.F.4
  • 3
    • 0033039544 scopus 로고    scopus 로고
    • N-Acetylcysteine increases the biosynthesis of recombinant EPO in apoptotic Chinese hamster ovary cells
    • Chang KH, Kim KS, Kim JH (1999) N-Acetylcysteine increases the biosynthesis of recombinant EPO in apoptotic Chinese hamster ovary cells. Free Radic Res 30:85-91
    • (1999) Free Radic Res , vol.30 , pp. 85-91
    • Chang, K.H.1    Kim, K.S.2    Kim, J.H.3
  • 4
    • 0028725582 scopus 로고
    • Role of environmental conditions on the expression levels, glycoform pattern and levels of sialyltransferase for hFSH produced by recombinant CHO cells
    • Chotigeat W, Watanapokasin Y, Mahler S, Gray PP (1994) Role of environmental conditions on the expression levels, glycoform pattern and levels of sialyltransferase for hFSH produced by recombinant CHO cells. Cytotechnology 15:217-221
    • (1994) Cytotechnology , vol.15 , pp. 217-221
    • Chotigeat, W.1    Watanapokasin, Y.2    Mahler, S.3    Gray, P.P.4
  • 6
    • 1442352043 scopus 로고    scopus 로고
    • Effect of doxycycline-regulated calnexin and calreticulin expression on specific thrombopoietin productivity of recombinant Chinese hamster ovary cells
    • Chung JY, Lim SW, Hong YJ, Hwang SO, Lee GM (2004) Effect of doxycycline-regulated calnexin and calreticulin expression on specific thrombopoietin productivity of recombinant Chinese hamster ovary cells. Biotechnol Bioeng 85:539-546
    • (2004) Biotechnol Bioeng , vol.85 , pp. 539-546
    • Chung, J.Y.1    Lim, S.W.2    Hong, Y.J.3    Hwang, S.O.4    Lee, G.M.5
  • 7
    • 11944265249 scopus 로고
    • High level expression of tissue inhibitor of metalloproteinases in Chinese hamster ovary cells using glutamine synthetase gene amplification
    • Cockett MI, Bebbington CR, Yarranton GT (1990) High level expression of tissue inhibitor of metalloproteinases in Chinese hamster ovary cells using glutamine synthetase gene amplification. Biotechnology 8:662-667
    • (1990) Biotechnology , vol.8 , pp. 662-667
    • Cockett, M.I.1    Bebbington, C.R.2    Yarranton, G.T.3
  • 8
    • 0027156495 scopus 로고
    • Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin)
    • David V, Hochstenbach F, Rajagopalan S, Brenner MB (1993) Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). J Biol Chem 268: 9585-9592
    • (1993) J Biol Chem , vol.268 , pp. 9585-9592
    • David, V.1    Hochstenbach, F.2    Rajagopalan, S.3    Brenner, M.B.4
  • 9
    • 33847042606 scopus 로고    scopus 로고
    • Calnexin-dependent regulation of tunicamycin-induced apoptosis in breast carcinoma MCF-7 cells
    • Delom F, Emadali A, Cocolakis E, Lebrun JJ, Nantel A, Chevet E (2006) Calnexin-dependent regulation of tunicamycin-induced apoptosis in breast carcinoma MCF-7 cells. Cell Death Differ 3:586-596
    • (2006) Cell Death Differ , vol.3 , pp. 586-596
    • Delom, F.1    Emadali, A.2    Cocolakis, E.3    Lebrun, J.J.4    Nantel, A.5    Chevet, E.6
  • 10
    • 33846530584 scopus 로고    scopus 로고
    • Regulation of calnexin sub-cellular localization modulates endoplasmic reticulum stress-induced apoptosis in MCF-7 cells
    • Delom F, Fessart D, Chevet E (2007) Regulation of calnexin sub-cellular localization modulates endoplasmic reticulum stress-induced apoptosis in MCF-7 cells. Apoptosis 12:293-305
    • (2007) Apoptosis , vol.12 , pp. 293-305
    • Delom, F.1    Fessart, D.2    Chevet, E.3
  • 11
    • 0034463216 scopus 로고    scopus 로고
    • Calnexin and calreticulin binding to human thyroperoxidase is required for its first folding step(s) but is not sufficient to promote efficient cell surface expression
    • Fayadat L, Siffroi-Fernandez S, Lanet J, Franc JL (2000) Calnexin and calreticulin binding to human thyroperoxidase is required for its first folding step(s) but is not sufficient to promote efficient cell surface expression. Endocrinology 141:959-966
    • (2000) Endocrinology , vol.141 , pp. 959-966
    • Fayadat, L.1    Siffroi-Fernandez, S.2    Lanet, J.3    Franc, J.L.4
  • 13
    • 0021101284 scopus 로고
    • Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate
    • Gorman CM, Howard BH, Reeves R (1983) Expression of recombinant plasmids in mammalian cells is enhanced by sodium butyrate. Nucleic Acids Res 11:7631-7648
    • (1983) Nucleic Acids Res , vol.11 , pp. 7631-7648
    • Gorman, C.M.1    Howard, B.H.2    Reeves, R.3
  • 14
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen M, Bujard H (1992) Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc Natl Acad Sci 89:5547-5551
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 16
    • 0029053768 scopus 로고
    • Removal of sialic acid from a glycoprotein in CHO cell culture supernatant by action of an extracellular CHO cell sialidase
    • Gramer MJ, Goochee CF, Chock VY, Brousseau DT, Sliwkowski MB (1995) Removal of sialic acid from a glycoprotein in CHO cell culture supernatant by action of an extracellular CHO cell sialidase. Bio/Technology 13:692-698
    • (1995) Bio/Technology , vol.13 , pp. 692-698
    • Gramer, M.J.1    Goochee, C.F.2    Chock, V.Y.3    Brousseau, D.T.4    Sliwkowski, M.B.5
  • 18
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BiP and calnexin
    • Hammond C, Helenius A (1994) Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266: 456-458
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 19
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C, Braakman I, Helenius A (1994) Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci U S A 91:913-917
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 20
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert DN, Foellmer B, Helenius A (1996) Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J 5: 2961-2968
    • (1996) EMBO J , vol.5 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 21
    • 18244367173 scopus 로고    scopus 로고
    • Increased productivity of recombinant tissular plasminogen activator (t-PA) by butyrate and shift of temperature: A cell cycle phases analysis
    • Hendrick V, Winnepenninckx P, Abdelkafi C, Vandeputte O, Cherlet M, Marique T, Renemann G, Loa A et al (2001) Increased productivity of recombinant tissular plasminogen activator (t-PA) by butyrate and shift of temperature: a cell cycle phases analysis. Cytotechnology 36:71-83
    • (2001) Cytotechnology , vol.36 , pp. 71-83
    • Hendrick, V.1    Winnepenninckx, P.2    Abdelkafi, C.3    Vandeputte, O.4    Cherlet, M.5    Marique, T.6    Renemann, G.7    Loa, A.8
  • 22
    • 38449096145 scopus 로고    scopus 로고
    • Nutrient deprivation induces autophagy as well as apoptosis in Chinese hamster ovary cell culture
    • Hwang SO, Lee GM (2008) Nutrient deprivation induces autophagy as well as apoptosis in Chinese hamster ovary cell culture. Biotechnol Bioeng 99:678-685
    • (2008) Biotechnol Bioeng , vol.99 , pp. 678-685
    • Hwang, S.O.1    Lee, G.M.2
  • 23
    • 0037274196 scopus 로고    scopus 로고
    • Effect of doxycycline-regulated ERp57 expression on specific thrombopoietin productivity of recombinant CHO cells
    • Hwang SO, Chung JY, Lee GM (2003) Effect of doxycycline-regulated ERp57 expression on specific thrombopoietin productivity of recombinant CHO cells. Biotechnol Prog 19:179-184
    • (2003) Biotechnol Prog , vol.19 , pp. 179-184
    • Hwang, S.O.1    Chung, J.Y.2    Lee, G.M.3
  • 24
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, Calnexin (p88, IP90)
    • Jackson MR, Cohen-Doyle MF, Peterson PA, Williams DB (1994) Regulation of MHC class I transport by the molecular chaperone, Calnexin (p88, IP90). Science 263:384-386
    • (1994) Science , vol.263 , pp. 384-386
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Williams, D.B.4
  • 25
    • 0027993624 scopus 로고
    • Persistence of glucose residues on core oligosaccharides prevents association of TCRa and TCRb with calnexin and results specifically in accelerated degradation of nascent TCRa proteins within the endoplasmic reticulum
    • Kearse KP, Williams DB, Singer A (1994) Persistence of glucose residues on core oligosaccharides prevents association of TCRa and TCRb with calnexin and results specifically in accelerated degradation of nascent TCRa proteins within the endoplasmic reticulum. EMBO J 13:3678-3686
    • (1994) EMBO J , vol.13 , pp. 3678-3686
    • Kearse, K.P.1    Williams, D.B.2    Singer, A.3
  • 26
    • 0001162423 scopus 로고    scopus 로고
    • Overexpression of bcl-2 inhibits sodium butyrate-induced apoptosis in Chinese hamster ovary cells resulting in enhanced humanized antibody production
    • Kim NS, Lee GM (2001) Overexpression of bcl-2 inhibits sodium butyrate-induced apoptosis in Chinese hamster ovary cells resulting in enhanced humanized antibody production. Biotechnol Bioeng 71:184-193
    • (2001) Biotechnol Bioeng , vol.71 , pp. 184-193
    • Kim, N.S.1    Lee, G.M.2
  • 27
    • 0037140412 scopus 로고    scopus 로고
    • Inhibition of sodium butyrate-induced apoptosis in recombinant Chinese hamster ovary cells by constitutively expressing antisense RNA of caspase-3
    • Kim NS, Lee GM (2002) Inhibition of sodium butyrate-induced apoptosis in recombinant Chinese hamster ovary cells by constitutively expressing antisense RNA of caspase-3. Biotechnol Bioeng 78:217-228
    • (2002) Biotechnol Bioeng , vol.78 , pp. 217-228
    • Kim, N.S.1    Lee, G.M.2
  • 28
    • 0032006868 scopus 로고    scopus 로고
    • Calcium and reactive oxygen species mediate staurosporine-induced mitochondrial dysfunction and apoptosis in PC12 cells
    • Kruman I, Guo Q, Mattson MP (1998) Calcium and reactive oxygen species mediate staurosporine-induced mitochondrial dysfunction and apoptosis in PC12 cells. J Neurosci Res 51:293-308
    • (1998) J Neurosci Res , vol.51 , pp. 293-308
    • Kruman, I.1    Guo, Q.2    Mattson, M.P.3
  • 29
    • 0030058801 scopus 로고    scopus 로고
    • High-level expression of human inducible nitric oxide synthase in Chinese hamster ovary cells and characterization of the purified enzyme
    • Laubach VE, Garvey EP, Sherman PA (1996) High-level expression of human inducible nitric oxide synthase in Chinese hamster ovary cells and characterization of the purified enzyme. Biochem Biophys Res Commun 218:802-807
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 802-807
    • Laubach, V.E.1    Garvey, E.P.2    Sherman, P.A.3
  • 30
    • 0028341304 scopus 로고
    • Association between calnexin and a secretion-incompetent variant of human a1-antitrypsin
    • Le A, Steiner JL, Ferrell GA, Shaker JC, Sifers RN (1994) Association between calnexin and a secretion-incompetent variant of human a1-antitrypsin. J Biol Chem 269:7514-7519
    • (1994) J Biol Chem , vol.269 , pp. 7514-7519
    • Le, A.1    Steiner, J.L.2    Ferrell, G.A.3    Shaker, J.C.4    Sifers, R.N.5
  • 31
    • 0028127183 scopus 로고
    • Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis
    • Loo TW, Clarke DM (1994) Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis. J Biol Chem 269:28683-28689
    • (1994) J Biol Chem , vol.269 , pp. 28683-28689
    • Loo, T.W.1    Clarke, D.M.2
  • 32
    • 0033711955 scopus 로고    scopus 로고
    • Basic fibroblast growth factor inhibits apoptosis of spontaneously immortalized granulosa cells by regulating intracellular free calcium levels through a protein kinase Cdelta-dependent pathway
    • Lynch K, Fernandez G, Pappalardo A, Peluso JJ (2000) Basic fibroblast growth factor inhibits apoptosis of spontaneously immortalized granulosa cells by regulating intracellular free calcium levels through a protein kinase Cdelta-dependent pathway. Endocrinology 141:4209-4217
    • (2000) Endocrinology , vol.141 , pp. 4209-4217
    • Lynch, K.1    Fernandez, G.2    Pappalardo, A.3    Peluso, J.J.4
  • 33
    • 2942738879 scopus 로고    scopus 로고
    • Cell viability and secretion of active proteins in Schizosaccharomyces pombe do not require the chaperone function of calnexin
    • Maréchal A, Tanguay PL, Callejo M, Guérin R, Boileau G, Rokeach LA (2004) Cell viability and secretion of active proteins in Schizosaccharomyces pombe do not require the chaperone function of calnexin. Biochem J 380(Pt 2):441-448
    • (2004) Biochem J , vol.380 , Issue.PART 2 , pp. 441-448
    • Maréchal, A.1    Tanguay, P.L.2    Callejo, M.3    Guérin, R.4    Boileau, G.5    Rokeach, L.A.6
  • 34
    • 0026005818 scopus 로고
    • Programmed death of nonproliferating androgen-independent prostatic cancer cells
    • Martikainen P, Kyprianou N, Tucker RW, Isaacs JT (1991) Programmed death of nonproliferating androgen-independent prostatic cancer cells. Cancer Res 51:4693-4700
    • (1991) Cancer Res , vol.51 , pp. 4693-4700
    • Martikainen, P.1    Kyprianou, N.2    Tucker, R.W.3    Isaacs, J.T.4
  • 35
    • 0031594742 scopus 로고    scopus 로고
    • The endoplasmic reticulum Ca2+ store: A view from the lumen
    • Meldolesi J, Pozzan T (1998) The endoplasmic reticulum Ca2+ store: a view from the lumen. Trends Biochem Sci 23:10-14
    • (1998) Trends Biochem Sci , vol.23 , pp. 10-14
    • Meldolesi, J.1    Pozzan, T.2
  • 37
    • 0036877146 scopus 로고    scopus 로고
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • 2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 32:269-278
    • (2002) Cell Calcium , vol.32 , pp. 269-278
    • Michalak, M.1    Robert Parker, J.M.2    Opas, M.3
  • 38
    • 0035164036 scopus 로고    scopus 로고
    • Butyrate increases production of human chimeric IgG in CHO-K1 cells whilst maintaining function and glycoform profile
    • Mimura Y, Lund J, Church S, Dong S, Li J, Goodall M, Jefferis R (2001) Butyrate increases production of human chimeric IgG in CHO-K1 cells whilst maintaining function and glycoform profile. J Immunol Methods 247:205-216
    • (2001) J Immunol Methods , vol.247 , pp. 205-216
    • Mimura, Y.1    Lund, J.2    Church, S.3    Dong, S.4    Li, J.5    Goodall, M.6    Jefferis, R.7
  • 39
    • 35048827454 scopus 로고    scopus 로고
    • Effect of doxycycline-regulated protein disulfide isomerase expression on the specific productivity of recombinant CHO cells: Thrombopoietin and antibody
    • Mohan C, Park SH, Chung JY, Lee GM (2007) Effect of doxycycline-regulated protein disulfide isomerase expression on the specific productivity of recombinant CHO cells: Thrombopoietin and antibody. Biotechnol Bioeng 983:611-615
    • (2007) Biotechnol Bioeng , vol.983 , pp. 611-615
    • Mohan, C.1    Park, S.H.2    Chung, J.Y.3    Lee, G.M.4
  • 42
    • 0034680917 scopus 로고    scopus 로고
    • Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum
    • Okazaki Y, Ohno H, Takase K, Ochiai T, Saito T (2000) Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum. J Biol Chem 275:35751-35758
    • (2000) J Biol Chem , vol.275 , pp. 35751-35758
    • Okazaki, Y.1    Ohno, H.2    Takase, K.3    Ochiai, T.4    Saito, T.5
  • 43
    • 0027263908 scopus 로고
    • Induction of recombinant human gamma-glutamyl transferase by sodium butyrate in transfected V79 and CHO Chinese hamster cells
    • Oster T, Thioudellet C, Chevalot I, Masson C, Wellman M, Marc A, Siest G (1993) Induction of recombinant human gamma-glutamyl transferase by sodium butyrate in transfected V79 and CHO Chinese hamster cells. Biochem Biophys Res Commun 193:406-412
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 406-412
    • Oster, T.1    Thioudellet, C.2    Chevalot, I.3    Masson, C.4    Wellman, M.5    Marc, A.6    Siest, G.7
  • 44
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou W-J, Cameron PH, Thomas DY, Bergeron JJM (1993) Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364:771-776
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.-J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 45
    • 0025860171 scopus 로고
    • Production of analytical quantities of recombinant proteins in Chinese hamster ovary cells using sodium butyrate to elevate gene expression
    • Palermo DP, DeGraaf ME, Marotti KR, Rehberg E, Post LE (1991) Production of analytical quantities of recombinant proteins in Chinese hamster ovary cells using sodium butyrate to elevate gene expression. J Biotechnol 19:35-48
    • (1991) J Biotechnol , vol.19 , pp. 35-48
    • Palermo, D.P.1    DeGraaf, M.E.2    Marotti, K.R.3    Rehberg, E.4    Post, L.E.5
  • 46
    • 0026235117 scopus 로고
    • Mammalian cell gene expression: Protein glyco-sylation
    • Parekh RB (1991) Mammalian cell gene expression: protein glyco-sylation. Curr Opin Biotechnol 2:730-734
    • (1991) Curr Opin Biotechnol , vol.2 , pp. 730-734
    • Parekh, R.B.1
  • 47
    • 0028232167 scopus 로고
    • Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator
    • Pind S, Riordan JR, Williams DB (1994) Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 269:12784-12788
    • (1994) J Biol Chem , vol.269 , pp. 12784-12788
    • Pind, S.1    Riordan, J.R.2    Williams, D.B.3
  • 48
    • 0034610995 scopus 로고    scopus 로고
    • Reduced loading of intracellular Ca (2+) stores and downregulation of capacitative Ca (2+) influx in Bcl-2-overexpressing cells
    • Pinton P, Ferrari D, Magalhães P, Schulze-Osthoff K, Di Virgilio F, Pozzan T, Rizzuto R (2000) Reduced loading of intracellular Ca (2+) stores and downregulation of capacitative Ca (2+) influx in Bcl-2-overexpressing cells. J Cell Biol 148:857-862
    • (2000) J Cell Biol , vol.148 , pp. 857-862
    • Pinton, P.1    Ferrari, D.2    Magalhães, P.3    Schulze-Osthoff, K.4    Di Virgilio, F.5    Pozzan, T.6    Rizzuto, R.7
  • 50
    • 0034640960 scopus 로고    scopus 로고
    • Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b
    • Roderick HL, Lechleiter JD, Camacho P (2000) Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b. J Cell Biol 149:1235-1248
    • (2000) J Cell Biol , vol.149 , pp. 1235-1248
    • Roderick, H.L.1    Lechleiter, J.D.2    Camacho, P.3
  • 51
    • 0036413254 scopus 로고    scopus 로고
    • Association of the thyrotropin receptor with calnexin, calreticulin and BiPEffects on the maturation of the receptor
    • Siffroi-Fernandez S, Giraud A, Lanet J, Franc JL (2002) Association of the thyrotropin receptor with calnexin, calreticulin and BiPEffects on the maturation of the receptor. Eur J Biochem 269:4930-4937
    • (2002) Eur J Biochem , vol.269 , pp. 4930-4937
    • Siffroi-Fernandez, S.1    Giraud, A.2    Lanet, J.3    Franc, J.L.4
  • 53
    • 13544271821 scopus 로고    scopus 로고
    • Enhanced human thrombopoietin production by sodium butyrate addition to serum-free suspension culture of bcl-2-overexpressing CHO cells
    • Sung YH, Lee GM (2005) Enhanced human thrombopoietin production by sodium butyrate addition to serum-free suspension culture of bcl-2-overexpressing CHO cells. Biotechnol Prog 21:50-57
    • (2005) Biotechnol Prog , vol.21 , pp. 50-57
    • Sung, Y.H.1    Lee, G.M.2
  • 54
    • 4143145162 scopus 로고    scopus 로고
    • Effect of sodium butyrate on the production, heterogeneity and biological activity of human thrombopoietin by recombinant Chinese hamster ovary cells
    • Sung YH, Song YJ, Lim SW, Chung JY, Lee GM (2004) Effect of sodium butyrate on the production, heterogeneity and biological activity of human thrombopoietin by recombinant Chinese hamster ovary cells. J Biotechnol 112:323-335
    • (2004) J Biotechnol , vol.112 , pp. 323-335
    • Sung, Y.H.1    Song, Y.J.2    Lim, S.W.3    Chung, J.Y.4    Lee, G.M.5
  • 55
    • 0029100978 scopus 로고
    • Calnexin influences folding of human class I histocompatibility proteins but not their assembly with B2-microglobulin
    • Tector M, Salter RD (1995) Calnexin influences folding of human class I histocompatibility proteins but not their assembly with B2-microglobulin. J Biol Chem 270:19638-19642
    • (1995) J Biol Chem , vol.270 , pp. 19638-19642
    • Tector, M.1    Salter, R.D.2
  • 58
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • Vassilakos A, Cohen-Doyle MF, Peterson PA, Jackson MR, Williams DB (1996) The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J 15:1495-1506
    • (1996) EMBO J , vol.15 , pp. 1495-1506
    • Vassilakos, A.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Jackson, M.R.4    Williams, D.B.5
  • 59
    • 0025937289 scopus 로고
    • SSRa and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane
    • Wada I, Rindress D, Cameron PH, Ou W, Doherty JJ, Louvard D, Bell AW, Dignard D et al (1991) SSRa and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J Biol Chem 226:19599-19610
    • (1991) J Biol Chem , vol.226 , pp. 19599-19610
    • Wada, I.1    Rindress, D.2    Cameron, P.H.3    Ou, W.4    Doherty, J.J.5    Louvard, D.6    Bell, A.W.7    Dignard, D.8
  • 60
    • 26444593029 scopus 로고    scopus 로고
    • Mitochondria and endoplasmic reticulum: The lethal interorganelle cross-talk
    • Walter L, Hajnóczky G (2005) Mitochondria and endoplasmic reticulum: the lethal interorganelle cross-talk. J Bioenerg Biomembr 37:191-206
    • (2005) J Bioenerg Biomembr , vol.37 , pp. 191-206
    • Walter, L.1    Hajnóczky, G.2
  • 61
    • 0002723192 scopus 로고    scopus 로고
    • Manufacture of proteins based on recombinant Chinese hamster ovary cells: Assessment of genetic issues and assurance of consistency and quality
    • Schmidt ER, Hankeln T eds, Springer, Berlin, p
    • Wurm FM, Petropoulos CJ, O'Connor JV (1996) Manufacture of proteins based on recombinant Chinese hamster ovary cells: assessment of genetic issues and assurance of consistency and quality. In: Schmidt ER, Hankeln T (eds) Transgenic organisms and biosafety. Springer, Berlin, p 546
    • (1996) Transgenic organisms and biosafety , pp. 546
    • Wurm, F.M.1    Petropoulos, C.J.2    O'Connor, J.V.3
  • 62
    • 4043105472 scopus 로고    scopus 로고
    • Effect of simultaneous application of stressful culture conditions on specific productivity and heterogeneity of erythropoietin in Chinese hamster ovary cells
    • Yoon SK, Hong JK, Lee GM (2004) Effect of simultaneous application of stressful culture conditions on specific productivity and heterogeneity of erythropoietin in Chinese hamster ovary cells. Biotechnol Prog 20:1293-1296
    • (2004) Biotechnol Prog , vol.20 , pp. 1293-1296
    • Yoon, S.K.1    Hong, J.K.2    Lee, G.M.3
  • 63
    • 0031841549 scopus 로고    scopus 로고
    • 2+]i in avian cochlear nucleus neurons: Roles of protein kinases A and C and relation to cell death
    • 2+]i in avian cochlear nucleus neurons: roles of protein kinases A and C and relation to cell death. J Neurophysiol 79:2288-2302
    • (1998) J Neurophysiol , vol.79 , pp. 2288-2302
    • Zirpel, L.1    Lippe, W.R.2    Rubel, E.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.