Ver registro no DEDALUS
Exportar registro bibliográfico

Metrics


Metrics:

Quantitative correlation between transcriptional levels of ER chaperone, peroximal protein and FVIII productivity in human Hek-293 cell line (2013)

  • Authors:
  • USP affiliated authors: FONTES, APARECIDA MARIA - FMRP ; COVAS, DIMAS TADEU - FMRP ; ANDRADE, LUIZ ALBERTO MARTINS DE - FMRP
  • USP Schools: FMRP; FMRP; FMRP
  • DOI: 10.1186/2193-1801-2-328
  • Subjects: PROTEÍNAS RECOMBINANTES; FATOR VIII; EXPRESSÃO GÊNICA; HEMOFILIA
  • Language: Inglês
  • Imprenta:
  • Source:
  • Acesso online ao documento

    Online accessDOI or search this record in
    Informações sobre o DOI: 10.1186/2193-1801-2-328 (Fonte: oaDOI API)
    • Este periódico é de assinatura
    • Este artigo é de acesso aberto
    • URL de acesso aberto
    • Cor do Acesso Aberto: hybrid
    • Licença: cc-by
    Informações sobre o Citescore
  • Título: SpringerPlus

    ISSN: 2193-1801

    Citescore - 2017: 1.23

    SJR - 2017: 0.389

    SNIP - 2017: 0.896


  • Exemplares físicos disponíveis nas Bibliotecas da USP
    BibliotecaCód. de barrasNúm. de chamada
    FMRP2483017pcd 2483017 Estantes Deslizantes
    How to cite
    A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas

    • ABNT

      RODRIGUES, Evandra Strazza; PICANÇO-CASTRO, Virgínia; ESPANHOL, Marta Regina; et al. Quantitative correlation between transcriptional levels of ER chaperone, peroximal protein and FVIII productivity in human Hek-293 cell line. Springer Plus, Heidelberg, v. 2, 2013. Disponível em: < http://dx.doi.org/10.1186/2193-1801-2-328 > DOI: 10.1186/2193-1801-2-328.
    • APA

      Rodrigues, E. S., Picanço-Castro, V., Espanhol, M. R., Andrade, L. A. M. de, Palma, P. V. B., Kashima, S., et al. (2013). Quantitative correlation between transcriptional levels of ER chaperone, peroximal protein and FVIII productivity in human Hek-293 cell line. Springer Plus, 2. doi:10.1186/2193-1801-2-328
    • NLM

      Rodrigues ES, Picanço-Castro V, Espanhol MR, Andrade LAM de, Palma PVB, Kashima S, Fontes AM, Covas DT. Quantitative correlation between transcriptional levels of ER chaperone, peroximal protein and FVIII productivity in human Hek-293 cell line [Internet]. Springer Plus. 2013 ; 2Available from: http://dx.doi.org/10.1186/2193-1801-2-328
    • Vancouver

      Rodrigues ES, Picanço-Castro V, Espanhol MR, Andrade LAM de, Palma PVB, Kashima S, Fontes AM, Covas DT. Quantitative correlation between transcriptional levels of ER chaperone, peroximal protein and FVIII productivity in human Hek-293 cell line [Internet]. Springer Plus. 2013 ; 2Available from: http://dx.doi.org/10.1186/2193-1801-2-328

    Referências citadas na obra
    Albesiano E, Messmer BT, Damle RN, Allen SL, Rai KR, Chiorazzi N: Activation-induced cytidine deaminase in chronic lymphocytic leukemia B cells: expression as multiple forms in a dynamic, variably sized fraction of the clone. Blood 2003, 102: 3333-3339. 10.1182/blood-2003-05-1585
    Antunes SV, Vicari P, Cavalheiro S, Bordin JO: Intracranial haemorrhage among a population of haemophilic patients in Brazil. Haemophilia 2003, 9(5):573-577. 10.1046/j.1365-2516.2003.00789.x
    Baxter: Advate® Prescribing Information. Baxter, Deerfield; 2010.
    Becker S, Simpson JC, Pepperkok R, Heinz S, Herder C, Grez M, Seifried E, Tonn T: Confocal microscopy analysis of native full length and B-domain deleted coagulation factor VIII trafficking in mammalian cells. Thromb Haemost 2004, 1: 23-35.
    Brown HC, Gangadharan B, Doering CB: Enhanced biosynthesis of coagulation factor VIII through diminished engagement of the unfolded protein response. J Biol Chem 2011, 286(27):24451-7. 10.1074/jbc.M111.238758
    Burton M, Nakai H, Colosi P, Cunningham J, Mitchell R, Couto L: Coexpression of factor VIII heavy and light chain adeno-associated viral vectors produces biologically active protein. Proc Natl Acad Sci USA 1999, 96(22):12725-12730. 10.1073/pnas.96.22.12725
    Chen C, Wang Q, Fang X, Xu Q, Chi C, Gu J: Roles of Phytanoyl-CoA -Hydroxylase in Mediating the Expression of Human Coagulation Factor VIII. J Biol Chem 2001, 276(49):46340-46346. 10.1074/jbc.M106124200
    Dorner AJ, Kaufman RJ: The levels of endoplasmic reticulum proteins and ATP affect folding and secretion of selective proteins. Biologicals 1994, 22(2):103-12. 10.1006/biol.1994.1016
    Dorner AJ, Wasley LC, Kaufman RJ: Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J 1992, 11(4):1563-71.
    Durocher Y, Butler M: Expression systems for therapeutic glycoprotein production. Curr Opin Biotechnol 2009, 20(6):700-7. 10.1016/j.copbio.2009.10.008
    Durocher Y, Perret S, Kamen A: High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res 2002, 15: 30-32.
    Ghosh K: Management of haemophilia and its complications in developing countries. Clin Lab Haematol 2004, 26(4):243-251. 10.1111/j.1365-2257.2004.00590.x
    HealthCare B: Kogenate® Prescribing Information. Bayer HealthCare, Leverkusen; 2009.
    Herlitschka SE, Schlokat U, Falkner FG, Dorner F: High expression of a B-domain deleted factor VIII gene in a human hepatic cell line. J Biotechnol 1998, 61(3):165-173. 10.1016/S0168-1656(98)00035-2
    Invitrogen Corporation: User Manual Free Style TM 293-F Cells (R790-07). 2007. http://www.graphpad.com/support/instat-3-updates/
    Jiang R, Monroe T, McRogers R, Larson PJ: Manufacturing challenges in the commercial production of recombinant coagulation factor VIII. Haemophilia 2002, 8(2):1-5.
    Kannicht C, Ramström M, Kohla G, Tiemeyer M, Casademunt E, Walter O, Sandberg H: Characterisation of the post-translational modifications of a novel, human cell line-derived recombinant human factor VIII. Thromb Res 2013, 131(1):78-88. 10.1016/j.thromres.2012.09.011
    Lee C: Recombinant clotting factors in the treatment of hemophilia. Thromb Haemost 1999, 2: 516-524. Review
    Lenting PJ, Christophe OD, Guéguen P: The disappearing act of factor VIII. Haemophilia 2010, 16(102):6-15.
    Lind P, Larsson K, Spira J, Sydow-Bäckman M, Almstedt A, Gray E, Sandberg H: Novel forms of B-domain-deleted recombinant factor VIII molecules. Construction and biochemical characterization. Eur J Biochem 1995, 232(1):19-27. 10.1111/j.1432-1033.1995.tb20776.x
    Marquette KA, Pittman DD, Kaufman RJ: A 110-amino acid region within the A1-domain of coagulation factor VIII inhibits secretion from mammalian cells. J Biol Chem 1995, 270(17):10297-10303. 10.1074/jbc.270.17.10297
    Meulien P, Faure T, Mischler F, Harrer H, Ulrich P, Bouderbala B, Dott K, Sainte Marie M, Mazurier C, Wiesel ML: A new recombinant procoagulant protein derived from the cDNA encoding human factor VIII. Protein Eng 1988, 2(4):301-306. 10.1093/protein/2.4.301
    Miao HZ, Sirachainan N, Palmer L, Kucab P, Cunningham MA, Kaufman RJ, Pipe SW: Bioengineering of coagulation factor VIII for improved secretion. Blood 2004, 103(9):3412-9. 10.1182/blood-2003-10-3591
    Morris JA, Dorner AJ, Edwards CA, Hendershot LM, Kaufman RJ: Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. J Biol Chem 1997, 272(7):4327-4334. 10.1074/jbc.272.7.4327
    Neidhardt E, Koval R, Burke E, Warne N: In vitro evaluation of B-domain deleted recombinant factor VIII (ReFacto) stability during simulated continuous infusion administration. Haemophilia 2005, 11(4):319-325. 10.1111/j.1365-2516.2005.01094.x
    Picanço V, Heinz S, Bott D, Behrmann M, Covas DT, Seifried E, Tonn T: Recombinant expression of coagulation factor VIII in hepatic and non-hepatic cell lines stably transduced with third generation lentiviral vectors comprising the minimal factor VIII promoter. Cytotherapy 2007, 9(Suppl 8):785-94.
    Pipe SW: Functional roles of the factor VIII B domain. Haemophilia 2009, 15(6):1187-96. 10.1111/j.1365-2516.2009.02026.x
    Shen BW, Spiegel PC, Chang CH, Huh JW, Lee JS, Kim J, Kim YH, Stoddard BL: The tertiary structure and domain organization of coagulation factor VIII. Blood 2008, 111(3):1240-1247.
    Srour MA, Grupp J, Aburubaiha Z, Albert T, Brondke H, Oldenburg J, Schwaab R: Modified expression of coagulation factor VIII by addition of a glycosylation site at the N terminus of the protein. Ann Hematol 2008, 87(2):107-12. 10.1007/s00277-007-0380-9
    Stanley SL Jr: The need for continuing vigilance addressing the threat for transmission of blood-borne infectious disease. Semin Hematol 2006, 43(2 Suppl 3):S17-22.
    Swiech K, Kamen A, Ansorge S, Durocher Y, Picanço-Castro V, Russo-Carbolante EM, Neto MS, Covas DT: Transient transfection of serum-free suspension HEK 293 cell culture for efficient production of human rFVIII. BMC Biotechnol 2011, 11: 114. 10.1186/1472-6750-11-114
    Thomas P, Smart TG: HEK293 cell line: a vehicle for the expression of recombinant proteins. J Pharmacol Toxicol Methods 2005, 51(3):187-200. 10.1016/j.vascn.2004.08.014
    Toole JJ, Pittman DD, Orr EC, Murtha P, Wasley LC, Kaufman RJ: A large region (approximately equal to 95 kDa) of human factor VIII is dispensable for in vitro procoagulant activity. Proc Natl Acad Sci USA 1986, 83(16):5939-5942. 10.1073/pnas.83.16.5939
    Wyeth Pharma (Pfizer): ReFacto® Prescribing Information. Wyeth Pharma (Pfizer), Madison; 2007.
    Zago MA, Covas DT, Ismael SJ, Bottura C: Splenic function in haemophilia. Haematologia (Budap) 20 1987, 1: 57-62.