Method for recombinant production of a desired polypeptide using a mammalian cell co-expressing a taurine transporter polypeptide

التفاصيل البيبلوغرافية
العنوان: Method for recombinant production of a desired polypeptide using a mammalian cell co-expressing a taurine transporter polypeptide
Patent Number: 9,238,687
تاريخ النشر: January 19, 2016
Appl. No: 12/226195
Application Filed: April 12, 2007
مستخلص: The present invention provides a method capable of producing a natural or recombinant protein at low cost. The present invention relates to a method of producing a polypeptide, comprising culturing a cell which strongly expresses a taurine transporter and has a transferred DNA encoding a desired polypeptide and thereby allowing the cell to produce the polypeptide. Hamster taurine transporter, a DNA encoding the same, a recombinant vector and a transformed cell are also provided.
Inventors: Tabuchi, Hisahiro (Tokyo, JP); Sugiyama, Tomoya (Tokyo, JP); Tanaka, Saeko (Tokyo, JP); Tainaka, Satoshi (Tokyo, JP)
Assignees: Chugai Seiyaku Kabushiki Kaisha (Tokyo, JP)
Claim: 1. A method of producing a desired secreted polypeptide comprising culturing an isolated mammalian cell transfected with a DNA encoding a taurine transporter and further transfected with a DNA encoding a desired secreted polypeptide, thereby allowing the mammalian cell to produce said desired secreted polypeptide, wherein the DNA encoding the taurine transporter is any one of the following (a) or (b): (a) a DNA encoding a polypeptide having the amino acid sequence of SEQ ID NO: 2; or (b) a DNA encoding a polypeptide having 98% or more amino acid sequence homology with the amino acid sequence of SEQ ID NO: 2, and wherein the taurine transporter has taurine transporter activity.
Claim: 2. The method of claim 1 , wherein the isolated mammalian cell is a Chinese hamster ovary cell.
Claim: 3. The method of claim 1 , comprising culturing the isolated mammalian cell in a medium with a taurine concentration of 0 to 100 g/L.
Claim: 4. A method of preparing a pharmaceutical comprising a desired secreted polypeptide, comprising preparing the desired secreted polypeptide by the method of any one of claim 1 , 2 or 3 and preparing the pharmaceutical comprising the desired secreted polypeptide.
Claim: 5. An isolated DNA comprising a DNA encoding a taurine transporter and a heterologous promoter, wherein the DNA encoding the taurine transporter is any one of the following (a) or (b): (a) a DNA encoding a polypeptide having the amino acid sequence of SEQ ID NO: 2; or (b) a DNA encoding a polypeptide having 98% or more amino acid sequence homology with the amino acid sequence of SEQ ID NO: 2, and wherein the taurine transporter has taurine transporter activity.
Claim: 6. A recombinant vector comprising the isolated DNA of claim 5 .
Claim: 7. An isolated cell transformed or transfected with the isolated DNA of claim 5 .
Claim: 8. The method of claim 1 , wherein the desired secreted polypeptide is an antibody.
Patent References Cited: 5658786 August 1997 Smith et al.
6184007 February 2001 Dusch et al.
6225115 May 2001 Smith et al.
6251613 June 2001 Kishimoto et al.
6316238 November 2001 Nakamura et al.
6812339 November 2004 Venter et al.
7413536 August 2008 Dower et al.
7919086 April 2011 Nakano et al.
8697397 April 2014 Tabuchi et al.
2003/0064510 April 2003 Reff et al.
2003/0165495 September 2003 Carulli et al.
2005/0221466 October 2005 Liao et al.
2005/0265983 December 2005 Melamed et al.
2006/0014937 January 2006 Kang et al.
2007/0162995 July 2007 Good et al.
2007/0166362 July 2007 Sakuma et al.
2007/0190599 August 2007 Nakano et al.
2009/0221442 September 2009 Dower et al.
2010/0167346 July 2010 Tabuchi et al.
2010/0233759 September 2010 Tabuchi et al.
2010/0248359 September 2010 Nakano et al.
2011/0003334 January 2011 Tabuchi et al.
2011/0014654 January 2011 Tabuchi et al.
2012/0045795 February 2012 Tabuchi et al.
1612689 May 2005
1838969 September 2006
1 212 619 May 2007
2 213 746 August 2010
08-191693 July 1996
10-075787 March 1998
10-191984 July 1998
2000-228990 August 2000
2005-525100 August 2005
2006-506086 February 2006
WO-92/04381 March 1992
WO-97/27485 July 1997
WO-01/20331 March 2001
WO-02/092768 November 2002
WO-03/039485 May 2003
WO 2005/076015 August 2005
WO-2006/006693 January 2006
WO-2006/119115 November 2006
WO-2007/056507 May 2007
WO-2007/119774 October 2007
WO-2008/114673 September 2008
WO-2009/020144 February 2009
WO-2009/051109 April 2009
WO-2009/054433 April 2009



























































































Other References: Tinland et al., PNAS 91:8000-8004, 1994. cited by examiner
Ramamoorthy et al., Biochem. J. 300:893-900, 1994. cited by examiner
Kim et al., J. Biotechnol. 95:237-248, 2002. cited by examiner
Ito et al., Biochem. J. 382:177-182, 2004. cited by examiner
Han et al., “Mechanisms of Regulation of Taurine Transporter Activity”, Taurine 6, Edited by Oja and Saransaari, Springer, New York 2006, pp. 79-90. cited by examiner
Liu et al., “Cloning and expression of a cDNA encoding the transporter of taurine and β-alanine in mouse brain,” Proc. Natl. Acad. Sci. USA, Dec. 1992, 89(24):12145-12149. cited by applicant
Smith et al., “Cloning and Expression of a High Affinity Taurine Transporter from Rat Brain,” Mol. Pharmacol., 1992, 42(4):563-569. cited by applicant
Supplementary European Search Report and European Search Opinion dated Oct. 9, 2009, in corresponding EP 07741485.2, 12 pages. cited by applicant
Ganapathy et al., “Expression and Regulation of the Taurine Transporter in Cultured Cell Lines of Human Origin,” Advances in Experimental Medicine and Biology, 1994, 359:51-57, XP009123192. cited by applicant
Jhiang et al., “Cloning of the human taurine transporter and characterization of taurine uptake in thyroid cells,” FEBS Letters, Mar. 1, 1993, 318(2):139-144. cited by applicant
Uchida et al., “Molecular cloning of the cDNA for an MDCK cell Na+- and Cl−-dependent taurine transporter that is regulated by hypertonicity,” Proc. Natl. Acad. Sci. USA, Sep. 1992, 89:8230-8234. cited by applicant
Voss et al., “Regulation of the expression and subcellular localization of the taurine transporter TauT in mouse NIH3T3 fibroblasts,” Eur. J. Biochem., 2004, 271:4646-4658. cited by applicant
European Search Report dated Aug. 5, 2010 in corresponding EP 10157011.7, 11 pages. cited by applicant
Database UniProt [Online] Jul. 1, 1993, XP002493028, retrieved from EBI accession No. UNIPROT:Q00589, 2 pages. cited by applicant
Database EMBL [Online] Jul. 23, 1992, XP002593029, retrieved from EBI accession No. EMBL:M95495, 3 pages. cited by applicant
Database Uniprot [Online] Oct. 1, 2000, XP002593031, retrieved from EBI accession No. UNIPROT:Q9MZ34, 2 pages. cited by applicant
Database Uniprot [Online] Mar. 15, 2005, XP002593030, retrieved from EBI accession No. UNIPROT:Q5F431, 1 page. cited by applicant
Database Uniprot [Online] Jan. 10, 2006, XP002593032, retrieved from EBI accession No. UNIPROT:Q2VRP7, 1 page. cited by applicant
Jhiang et al., “Cloning of the human taurine transporter and characterization of taurine uptake in thyroid cells,” FEBS Letters, Mar. 1993, 318(2):139-144. cited by applicant
Liu et al., “Cloning and expression of a cDNA encoding the transporter of taurine and β-alanine in mouse brain,” PNAS, Dec. 1992, 89(24):12145-12149. cited by applicant
Miyasaka et al., “Characterization of Human Taurine Transporter Expressed in Insect Cells Using a Recombinant Baculovirus,” Protein Expression and Purification, 2001, 23(3):389-397. cited by applicant
Smith et al., “Cloning and Expression of a High Affinity Taurine Transporter from Rat Brain,” Molecular Pharmacology, 1992, 42(4):563-569. cited by applicant
Uchida et al., “Molecular cloning of the cDNA for an MDCK cell Na+- and CL−-dependent taurine transporter that is regulated by hypertonicity,” PNAS, Sep. 1992, 89(17):8230-8234. cited by applicant
Voss et al., “Regulation of the expression and subcellular localization of the taurine transporter TauT in mouse NIH3T3 fibroblasts,” Eur. J. Biochem., Dec. 2004, 271(23-24):4646-4658. cited by applicant
Office Action dated Jul. 8, 2010, in corresponding EP 07 741 485.2, 4 pages. cited by applicant
Butler, Michael, “Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals,” Appl. Microbiol. Biotechnol., 2005, 68:283-291. cited by applicant
Trill et al., “Production of monoclonal antibodies in COS and CHO cells,” Current Opinion in Biotechnology, 1995, 6:553-560. cited by applicant
Beckmann et al., “Coexpression of band 3 mutants and Rh polypeptides: differential effects of band 3 on the expression of the Rh complex containing D polypeptide and the Rh complex containing CcEe polypeptide,” Blood, Apr. 15, 2001, 97(8):2496-2505. cited by applicant
Han et al., “Regulation of TauT by cisplatin in LLC-PK1 renal cells,” Pediatr. Nephrol., 2005, 20:1067-1072. cited by applicant
Ishiguro et al., “CO2 permeability and bicarbonate transport in microperfused interlobular ducts isolated from guinea-pig pancreas,” Journal of Physiology, 2000, 528.2:305-315. cited by applicant
Mount et al., “The SLC26 gene family of multifunctional anion exchangers,” Pflugers Arch.—Eur. J. Physiol., 2004, 447:710-721. cited by applicant
Pushkin et al., “SLC4 base (HCO-3, CO-23) transporters: classification, function, structure, genetic diseases, and knockout models,” Am. J. Physiol. Renal Physiol., 2006, 290:F580-F599. cited by applicant
Final Office Action dated Mar. 2, 2012 in U.S. Appl. No. 12/734,283. cited by applicant
Final Office Action dated Aug. 23, 2011 in U.S. Appl. No. 12/733,815. cited by applicant
Notice of Allowance dated Dec. 20, 2012 in U.S. Appl. No. 12/733,052. cited by applicant
Office Action dated Jan. 6, 2011 in U.S. Appl. No. 12/733,815. cited by applicant
Office Action dated Aug. 3, 2011 in U.S. Appl. No. 12/734,283. cited by applicant
Office Action dated Sep. 21, 2012 in U.S. Appl. No. 13/368,945. cited by applicant
Shibayama et al., “Effect of Methotrexate Treatment on Expression Levels of Organic Anion Transporter Polypeptide 2,P-Glycoprotein and Bile Salt Export Pump in Rats,” Biol. Pharm. Bull., Mar. 2009, 32(3):493-496. cited by applicant
Office Action dated Feb. 27, 2013 in U.S. Appl. No. 13/138,909. cited by applicant
Final Office Action dated May 24, 2013 in U.S. Appl. No. 13/368,945. cited by applicant
Tanner et al., “The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence,” Biochem. J., 1988, 256:703-712. cited by applicant
U.S. Appl. No. 13/368,945, filed Feb. 8, 2012, Tabuchi et al. cited by applicant
Alper, Seth L., “Molecular physiology of SLC4 anion exchangers,” Exp. Physiol., 2006, 91:153-161. cited by applicant
Arden et al., “Life and death in mammalian cell culture: strategies for apoptosis inhibition,” Trends in Biotechnology, Apr. 2004, 22(4):174-180. cited by applicant
Bell et al., “Genetic Engineering of Hybridoma Glutamine Metabolism,” Enzyme and Microbial Technology, 1995, 17(2):98-106. cited by applicant
Butler, Michael, “Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals,” Appl. Microbiol. Biotechnol., Aug. 2005, 68(3):283-291. cited by applicant
Chambard et al., “Sugar transport by mammalian members of the SLC26 superfamily of anion-bicarbonate exchangers,” J. Physiol., 2003, 550:667-677. cited by applicant
Christensen et al., “High expression of the taurine transporter TauT in primary cilia of NIH3T3 fibroblasts,” Cell Biology International, 2005, 29:347-351. cited by applicant
Christie et al., “The Adaptation of BHK Cells to a Non-Ammoniagenic Glutamate-Based Culture Medium,” Biotechnology and Bioengineering, Aug. 5, 1999, 64(3):298-309. cited by applicant
Database DDBJ/EMBL/GenBank [online], Accession No. NM—000342, uploaded Sep. 25, 2007, Keskanokwong et al., Definition: Homo sapiens solute carrier family 4, anion exchanger, member 1 (erythrocyte membrane protein band 3, Diego blood group) (SLC4A1), mRNA, retrieved Nov. 11, 2008, 12 pages. cited by applicant
Database UniProt [Online] Jun. 1, 2001, “RecName: Full=Cysteine sulfinic acid decarboxylase; EC=4.1.1.29; AltName: Full=Cysteine-sulfinate decarboxylase; AltName: Full=Sulfinoalanine decarboxylase;” XP002597738 retrieved from EBI accession No. UNIPROT:Q9DBE0 Database accession No. Q9DBE0, 2 pages. cited by applicant
de la Cruz Edmonds et al., “Development of Transfection and High-Producer Screening Protocols for the CHOK1SV Cell System,” Molecular Biology, Oct. 1, 2006, 34(2):179-190. cited by applicant
de la Rosa et al., “Evidence for a Rate-Limiting Role of Cysteinesulfinate Decarboxylase Activity in Taurine Biosynthesis In Vivo,” Comp. Biochem. Physiol., 1985, 81B(3):565-571. cited by applicant
Dusch et al., “Expression of the Corynebacterium glutamicum panD Gene Encoding L-Aspartate-alpha-Decarboxylase Leads to Pantothenate Overproduction in Escherichia coli,” Applied and Environmental Microbiology, Apr. 1999, 65(4):1530-1539. cited by applicant
Final Office Action dated Mar. 1, 2012 in U.S. Appl. No. 12/733,052. cited by applicant
Fu et al., “Direct interaction and cooperative role of tumor suppressor p16 with band 3 (AE1),” FEBS Letters, 2005, 579(10):2105-2110. cited by applicant
GenBank Accession No. AEQ38544, Oct. 2011, 2 pages. cited by applicant
GenBank Accession No. EGW01898, Aug. 2011, 2 pages. cited by applicant
Good et al., “Engineering nitrogen use efficiency with alanine aminotransferase,” Canadian Journal of Botany, Mar. 1, 2007, 85(3):252-262. cited by applicant
Griffith, Owen W., “Crysteinesulfinate Metabolism, Altered Partitioning Between Transamination and Decarboxylation Following Administration of β-Methyleneaspartate,” J. Biol. Chem., Feb. 10, 1983, 258(3):1591-1598. cited by applicant
Hammer et al., “β-Alanine but not taurine can function as an organic osmolyte in preimplantation mouse embryos cultured from fertilized eggs,” Molecular Reproduction and Development, Oct. 2003, 66(2):153-161. cited by applicant
Han et al., “Is TauT an Anti-Apoptotic Gene?” Taurine 6, Oja et al. Eds., 2006, 59-67. cited by applicant
Hwang et al., “Expression and purification of recombinant human angiopoietin-2 produced in Chinese hamster ovary cells,” Protein Expression and Purification, 2005, 39:175-183. cited by applicant
Ifandi et al., “Regulation of Cell Proliferation and Apoptosis in CHO-K1 Cells by the Coexpression of c-Myc and Bcl-2,” Biotechnol. Prog., 2005, 21:671-677. cited by applicant
Jhiang et al., “Cloning of the human taurine transporter and characterization of taurine uptake in thyroid cells,” FEBS, 318(2):139-144, 1993. cited by applicant
Kalwy et al., “Toward More Efficient Protein Expression,” Molecular Biotechnology, Oct. 2006, 34(2):151-156. cited by applicant
Kennel et al,. “Principles and Practices of Nucleic Acid Hybridization,” Prog. Nucleic Acid Res. Mol. Biol., 1971, 11:259-270. cited by applicant
Kim et al., “Characterization of Chimeric Antibody Producing CHO Cells in the Course of Dihydrofolate Reductase-Mediated Gene Amplification and Their Stability in the Absence of Selective Pressure,” Biotechnology and Bioengineering, Apr. 5, 1998, 58(1):73-84. cited by applicant
Kondo et al., “Modulation of apoptosis by endogenous Bcl-xL expression in MKN-45 human gastric cancer cells,” Oncogene, 1998, 17:2585-2591. cited by applicant
Lee et al., “Development of Apoptosis-Resistant Dihydrofolate Reductase-Deficient Chinese Hamster Ovary Cell Line,” Biotechnol. Bioengineer., 2003, 82:872-876. cited by applicant
Liu et al., “Cloning and expression of a cDNA encoding the transporter taurine and β-alanine in mouse brain,” Proc. Natl. Acad. Sci. USA, Dec. 1992, 89:12145-12149. cited by applicant
Lux et al., “Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1),” Proc. Natl. Acad. Sci. USA, Dec. 1989, 86:9089-9093. cited by applicant
Miyasaka et al., “Characterization of Human Taurine Transporter Expressed in Insect Cells Using a Recombinant Baculovirus,” Protein Expression and Purification, 2001, 23:389-397. cited by applicant
Morgan et al., “Interactions of transmembrane carbonic anhydrase, CAIX, with bicarbonate transporters,” Am. J. Physiol. Cell Physiol., Aug. 2007, 293(2):C738-C748. cited by applicant
Ngo et al., “Computational Complexity, Protein Structure Prediction, and the Levinthal Paradox,” The Protein Folding Problem and Tertiary Structure Prediction, Merz et al. (Eds.), 1994, 433 and 492-495. cited by applicant
Office Action dated May 12, 2011 in U.S. Appl. No. 12/733,052. cited by applicant
Office Action dated Aug. 9, 2011 in U.S. Appl. No. 12/450,161. cited by applicant
Porter et al., “Non-steady-state kinetics of brain glutamate decarboxylase resulting from interconversion of the apo- and holoenzyme,” Biochimica et Biophysica Acta, 1988, 874:235-244. cited by applicant
Reymond et al., “Molecular cloning and sequence analysis of the cDNA encoding rat liver cysteine sulfinate decarboxylase (CSD),” Biochimica et Biophysica Acta, 1996, 1307:152-156. cited by applicant
Rudinger, J., “Characteristics of the amino acids as components of a peptide hormone sequence,” Peptide Hormones, Parsons (Ed.), 1976, 1-7. cited by applicant
Shen et al., “Expression of Anion Exchanger 1 Sequestrates p16 in the Cytoplasm in Gastric and Colonic Adenocarcinoma,” Neoplasia, Oct. 2007, 9(10):812-819. cited by applicant
Smith et al., “Cloning and Expression of a High Affinity Taurine Transporter from Rat Brain,” Molecular Pharmacology, 1992, 42:563-569. cited by applicant
Tabuchi et al., “Overexpression of Taurine Transporter in Chinese Hamster Ovary cells Can Enhance Cell Viability and Product Yield, While Promoting Glutamine Consumption,” Biotechnology and Bioengineering, 2010, 107(6):998-1003. cited by applicant
Tang et al., “Protein Phosphorylation and Taurine Biosynthesis In Vivo and In Vitro,” Journal of Neuroscience, Sep. 15, 1997, 17(18):6947-6951. cited by applicant
Tappaz et al., “Characterization of the cDNA Coding for Rat Brain Cysteine Sulfinate Decarboxylase: Brain and Liver Enzymes are Identical Proteins Encoded by Two Distince mRNAs,” J. Neurochem., 1999, 73(3):903-912. cited by applicant
Wirth et al., “Isolation of overproducing recombinant mammalian cell lines by a fast and simple selection procedure,” Gene, 1988, 73:419-426. cited by applicant
Wu et al., “Overexpression of Anion Exchanger 2 in Human Hepatocellular Carcinoma,” Chinese Journal of Physiology, 2006, 49(4):192-198. cited by applicant
Yang et al., “Human Hepatitis B Viral e Antigen Interacts with Cellular Interleukin-1 Receptor Accessory Protein and Triggers Interleukin-1 Response,” Journal of Biological Chemistry, Nov. 10, 2006, 281(45):34525-34536. cited by applicant
Yang et al., “cDNA Cloning, Genomic Structure, Chromosomal Mapping, and Functional Expression of a Novel Human Alanine Aminotransferase,” Genomics, Mar. 1, 2002, 79(3):445-450. cited by applicant
Zhang et al., “Metabolic characteristics of recombinant Chinese hamster ovary cells expressing glutamine synthetase in presence and absence of glutamine,” Cytotechnology, 2006, 51(1):21-28. cited by applicant
Herman et al., “Low dose methotrexate induces apoptosis with reactive oxygen species involvement in T lymphocytic cell lines to a greater extent than in monocytic lines,” Inflammation Research, 2005, 54:273-280. cited by applicant
Primary Examiner: Steadman, David J
Attorney, Agent or Firm: Foley & Lardner LLP
رقم الانضمام: edspgr.09238687
قاعدة البيانات: USPTO Patent Grants