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Volumn 10, Issue 1, 2012, Pages 107-115

Bioengineering of coagulation factor VIII for efficient expression through elimination of a dispensable disulfide loop

Author keywords

Bioengineering; Disulfide bonds; Factor VIII; Hemophilia A; Secretion

Indexed keywords

CYSTEINE; GLYCINE; RECOMBINANT BLOOD CLOTTING FACTOR 8; SERINE;

EID: 84855363773     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2011.04545.x     Document Type: Article
Times cited : (24)

References (37)
  • 1
    • 0032697618 scopus 로고    scopus 로고
    • Biochemistry and physiology of blood coagulation
    • Mann KG. Biochemistry and physiology of blood coagulation. Thromb Haemost 1999; 82: 165-74.
    • (1999) Thromb Haemost , vol.82 , pp. 165-174
    • Mann, K.G.1
  • 3
    • 0027237331 scopus 로고
    • Sequences in the coding region of clotting factor VIII act as dominant inhibitors of RNA accumulation and protein production
    • Lynch CM, Israel DI, Kaufman RJ, Miller AD. Sequences in the coding region of clotting factor VIII act as dominant inhibitors of RNA accumulation and protein production. Hum Gene Ther 1993; 4: 259-72.
    • (1993) Hum Gene Ther , vol.4 , pp. 259-272
    • Lynch, C.M.1    Israel, D.I.2    Kaufman, R.J.3    Miller, A.D.4
  • 4
    • 0141832940 scopus 로고    scopus 로고
    • Hemophilia: treatment options in the twenty-first century
    • Mannucci PM. Hemophilia: treatment options in the twenty-first century. J Thromb Haemost 2003; 1: 1349-55.
    • (2003) J Thromb Haemost , vol.1 , pp. 1349-1355
    • Mannucci, P.M.1
  • 5
    • 0024597022 scopus 로고
    • Effect of von Willebrand factor coexpression on the synthesis and secretion of factor VIII in Chinese hamster ovary cells
    • Kaufman RJ, Wasley LC, Davies MV, Wise RJ, Israel DI, Dorner AJ. Effect of von Willebrand factor coexpression on the synthesis and secretion of factor VIII in Chinese hamster ovary cells. Mol Cell Biol 1989; 9: 1233-42.
    • (1989) Mol Cell Biol , vol.9 , pp. 1233-1242
    • Kaufman, R.J.1    Wasley, L.C.2    Davies, M.V.3    Wise, R.J.4    Israel, D.I.5    Dorner, A.J.6
  • 7
    • 0023597393 scopus 로고
    • The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins
    • Dorner AJ, Bole DG, Kaufman RJ. The relationship of N-linked glycosylation and heavy chain-binding protein association with the secretion of glycoproteins. J Cell Biol 1987; 105: 2665-74.
    • (1987) J Cell Biol , vol.105 , pp. 2665-2674
    • Dorner, A.J.1    Bole, D.G.2    Kaufman, R.J.3
  • 8
    • 0029840409 scopus 로고    scopus 로고
    • Factor VIII C2 domain missense mutations exhibit defective trafficking of biologically functional proteins
    • Pipe SW, Kaufman RJ. Factor VIII C2 domain missense mutations exhibit defective trafficking of biologically functional proteins. J Biol Chem 1996; 271: 25671-6.
    • (1996) J Biol Chem , vol.271 , pp. 25671-25676
    • Pipe, S.W.1    Kaufman, R.J.2
  • 9
    • 0024404910 scopus 로고
    • Increased synthesis of secreted proteins induces expression of glucose-regulated proteins in butyrate-treated Chinese hamster ovary cells
    • Dorner AJ, Wasley LC, Kaufman RJ. Increased synthesis of secreted proteins induces expression of glucose-regulated proteins in butyrate-treated Chinese hamster ovary cells. J Biol Chem 1989; 264: 20602-7.
    • (1989) J Biol Chem , vol.264 , pp. 20602-20607
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 10
    • 0026511824 scopus 로고
    • Overexpression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells
    • 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: 1563-71.
    • (1992) EMBO J , vol.11 , pp. 1563-1571
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 11
    • 0025119643 scopus 로고
    • Protein dissociation from GRP78 and secretion are blocked by depletion of cellular ATP levels
    • Dorner AJ, Wasley LC, Kaufman RJ. Protein dissociation from GRP78 and secretion are blocked by depletion of cellular ATP levels. Proc Natl Acad Sci U S A 1990; 87: 7429-32.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 7429-7432
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 12
    • 0034728357 scopus 로고    scopus 로고
    • ATP-dependent dissociation of non-disulfide-linked aggregates of coagulation factor VIII is a rate-limiting step for secretion
    • Tagliavacca L, Wang Q, Kaufman RJ. ATP-dependent dissociation of non-disulfide-linked aggregates of coagulation factor VIII is a rate-limiting step for secretion. Biochemistry 2000; 39: 1973-81.
    • (2000) Biochemistry , vol.39 , pp. 1973-1981
    • Tagliavacca, L.1    Wang, Q.2    Kaufman, R.J.3
  • 15
    • 21844438479 scopus 로고    scopus 로고
    • LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway
    • Zhang B, Kaufman RJ, Ginsburg D. LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway. J Biol Chem 2005; 280: 25881-6.
    • (2005) J Biol Chem , vol.280 , pp. 25881-25886
    • Zhang, B.1    Kaufman, R.J.2    Ginsburg, D.3
  • 17
    • 34547171662 scopus 로고    scopus 로고
    • Receptor-mediated protein transport in the early secretory pathway
    • Baines AC, Zhang B. Receptor-mediated protein transport in the early secretory pathway. Trends Biochem Sci 2007; 32: 381-8.
    • (2007) Trends Biochem Sci , vol.32 , pp. 381-388
    • Baines, A.C.1    Zhang, B.2
  • 18
    • 0023918719 scopus 로고
    • Synthesis, processing, and secretion of recombinant human factor VIII expressed in mammalian cells
    • Kaufman RJ, Wasley LC, Dorner AJ. Synthesis, processing, and secretion of recombinant human factor VIII expressed in mammalian cells. J Biol Chem 1988; 263: 6352-62.
    • (1988) J Biol Chem , vol.263 , pp. 6352-6362
    • Kaufman, R.J.1    Wasley, L.C.2    Dorner, A.J.3
  • 19
    • 0022760260 scopus 로고
    • A large region (approximately equal to 95kDa) of human factor VIII is dispensable for in vitro procoagulant activity
    • Toole JJ, Pittman DD, Orr EC, Murtha P, Wasley LC, Kaufman RJ. A large region (approximately equal to 95kDa) of human factor VIII is dispensable for in vitro procoagulant activity. Proc Natl Acad Sci U S A 1986; 83: 5939-42.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 5939-5942
    • Toole, J.J.1    Pittman, D.D.2    Orr, E.C.3    Murtha, P.4    Wasley, L.C.5    Kaufman, R.J.6
  • 20
    • 0027319588 scopus 로고
    • Biochemical, immunological, and in vivo functional characterization of B-domain-deleted factor VIII
    • Pittman DD, Alderman EM, Tomkinson KN, Wang JH, Giles AR, Kaufman RJ. Biochemical, immunological, and in vivo functional characterization of B-domain-deleted factor VIII. Blood 1993; 81: 2925-35.
    • (1993) Blood , vol.81 , pp. 2925-2935
    • Pittman, D.D.1    Alderman, E.M.2    Tomkinson, K.N.3    Wang, J.H.4    Giles, A.R.5    Kaufman, R.J.6
  • 21
    • 0030821993 scopus 로고    scopus 로고
    • Mutagenesis of a potential immunoglobulin-binding protein-binding site enhances secretion of coagulation factor VIII
    • Swaroop M, Moussalli M, Pipe SW, Kaufman RJ. Mutagenesis of a potential immunoglobulin-binding protein-binding site enhances secretion of coagulation factor VIII. J Biol Chem 1997; 272: 24121-4.
    • (1997) J Biol Chem , vol.272 , pp. 24121-24124
    • Swaroop, M.1    Moussalli, M.2    Pipe, S.W.3    Kaufman, R.J.4
  • 22
    • 0032704952 scopus 로고    scopus 로고
    • Mannose-dependent endoplasmic reticulum (ER)-Golgi intermediate compartment-53-mediated ER to Golgi trafficking of coagulation factors V and VIII
    • Moussalli M, Pipe SW, Hauri HP, Nichols WC, Ginsburg D, Kaufman RJ. Mannose-dependent endoplasmic reticulum (ER)-Golgi intermediate compartment-53-mediated ER to Golgi trafficking of coagulation factors V and VIII. J Biol Chem 1999; 274: 32539-42.
    • (1999) J Biol Chem , vol.274 , pp. 32539-32542
    • Moussalli, M.1    Pipe, S.W.2    Hauri, H.P.3    Nichols, W.C.4    Ginsburg, D.5    Kaufman, R.J.6
  • 24
    • 0036186384 scopus 로고    scopus 로고
    • Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum
    • Fassio A, Sitia R. Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum. Histochem Cell Biol 2002; 117: 151-7.
    • (2002) Histochem Cell Biol , vol.117 , pp. 151-157
    • Fassio, A.1    Sitia, R.2
  • 25
    • 23744457478 scopus 로고    scopus 로고
    • Versatility of the endoplasmic reticulum protein folding factory
    • van Anken E, Braakman I. Versatility of the endoplasmic reticulum protein folding factory. Crit Rev Biochem Mol Biol 2005; 40: 191-228.
    • (2005) Crit Rev Biochem Mol Biol , vol.40 , pp. 191-228
    • van Anken, E.1    Braakman, I.2
  • 26
    • 0023896186 scopus 로고
    • Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae
    • Taniyama Y, Yamamoto Y, Nakao M, Kikuchi M, Ikehara M. Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae. Biochem Biophys Res Commun 1988; 152: 962-7.
    • (1988) Biochem Biophys Res Commun , vol.152 , pp. 962-967
    • Taniyama, Y.1    Yamamoto, Y.2    Nakao, M.3    Kikuchi, M.4    Ikehara, M.5
  • 27
    • 0025862426 scopus 로고
    • Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae
    • Inaka K, Taniyama Y, Kikuchi M, Morikawa K, Matsushima M. Role of disulfide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae. J Biol Chem 1991; 266: 12599-603.
    • (1991) J Biol Chem , vol.266 , pp. 12599-12603
    • Inaka, K.1    Taniyama, Y.2    Kikuchi, M.3    Morikawa, K.4    Matsushima, M.5
  • 28
    • 0024813415 scopus 로고
    • Elimination of disulfide bonds affects assembly and secretion of the human chorionic gonadotropin beta subunit
    • Suganuma N, Matzuk MM, Boime I. Elimination of disulfide bonds affects assembly and secretion of the human chorionic gonadotropin beta subunit. J Biol Chem 1989; 264: 19302-7.
    • (1989) J Biol Chem , vol.264 , pp. 19302-19307
    • Suganuma, N.1    Matzuk, M.M.2    Boime, I.3
  • 29
    • 0028116115 scopus 로고
    • Mutagenesis of cysteine residues in the human gonadotropin alpha subunit. Roles of individual disulfide bonds in secretion, assembly, and biologic activity
    • Furuhashi M, Ando H, Bielinska M, Pixley MR, Shikone T, Hsueh AJ, Boime I. Mutagenesis of cysteine residues in the human gonadotropin alpha subunit. Roles of individual disulfide bonds in secretion, assembly, and biologic activity. J Biol Chem 1994; 269: 25543-8.
    • (1994) J Biol Chem , vol.269 , pp. 25543-25548
    • Furuhashi, M.1    Ando, H.2    Bielinska, M.3    Pixley, M.R.4    Shikone, T.5    Hsueh, A.J.6    Boime, I.7
  • 30
    • 0028939696 scopus 로고
    • Locations of disulfide bonds and free cysteines in the heavy and light chains of recombinant human factor VIII (antihemophilic factor A)
    • McMullen BA, Fujikawa K, Davie EA, Hedner U, Ezban M. Locations of disulfide bonds and free cysteines in the heavy and light chains of recombinant human factor VIII (antihemophilic factor A). Protein Sci 1995; 4: 740-6.
    • (1995) Protein Sci , vol.4 , pp. 740-746
    • McMullen, B.A.1    Fujikawa, K.2    Davie, E.A.3    Hedner, U.4    Ezban, M.5
  • 31
    • 0027527981 scopus 로고
    • Site-directed mutagenesis and expression of coagulation factors VIII and V in mammalian cells
    • Pittman DD, Kaufman RJ. Site-directed mutagenesis and expression of coagulation factors VIII and V in mammalian cells. Methods Enzymol 1993; 222: 236-60.
    • (1993) Methods Enzymol , vol.222 , pp. 236-260
    • Pittman, D.D.1    Kaufman, R.J.2
  • 32
    • 2942709860 scopus 로고    scopus 로고
    • High-level expression of proteins in mammalian cells using transcription regulatory sequences from the Chinese hamster EF-1α gene
    • Running Deer J, Allison DS. High-level expression of proteins in mammalian cells using transcription regulatory sequences from the Chinese hamster EF-1α gene. Biotechnol Prog 2004; 20: 880-9.
    • (2004) Biotechnol Prog , vol.20 , pp. 880-889
    • Running Deer, J.1    Allison, D.S.2
  • 33
    • 0032805251 scopus 로고    scopus 로고
    • Hydrodynamics-based transfection in animals by systemic administration of plasmid DNA
    • Liu F, Song Y, Liu D. Hydrodynamics-based transfection in animals by systemic administration of plasmid DNA. Gene Ther 1999; 6: 1258-66.
    • (1999) Gene Ther , vol.6 , pp. 1258-1266
    • Liu, F.1    Song, Y.2    Liu, D.3
  • 34
    • 0033166561 scopus 로고    scopus 로고
    • High levels of foreign gene expression in hepatocytes after tail vein injections of naked plasmid DNA
    • Zhang G, Budker V, Wolff JA. High levels of foreign gene expression in hepatocytes after tail vein injections of naked plasmid DNA. Hum Gene Ther 1999; 10: 1735-7.
    • (1999) Hum Gene Ther , vol.10 , pp. 1735-1737
    • Zhang, G.1    Budker, V.2    Wolff, J.A.3
  • 35
    • 0025267375 scopus 로고
    • Evidence for difference in the roles of two cysteine residues involved in disulfide bond formation in the folding of human lysozyme
    • Taniyama Y, Yamamoto Y, Kuroki R, Kikuchi M. Evidence for difference in the roles of two cysteine residues involved in disulfide bond formation in the folding of human lysozyme. J Biol Chem 1990; 265: 7570-5.
    • (1990) J Biol Chem , vol.265 , pp. 7570-7575
    • Taniyama, Y.1    Yamamoto, Y.2    Kuroki, R.3    Kikuchi, M.4
  • 36
    • 0028241866 scopus 로고
    • Post-translational requirements for functional factor V and factor VIII secretion in mammalian cells
    • Pittman DD, Tomkinson KN, Kaufman RJ. Post-translational requirements for functional factor V and factor VIII secretion in mammalian cells. J Biol Chem 1994; 269: 17329-37.
    • (1994) J Biol Chem , vol.269 , pp. 17329-17337
    • Pittman, D.D.1    Tomkinson, K.N.2    Kaufman, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.