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Volumn 59, Issue 2, 2008, Pages 289-296

Recombinant human fibrinogen expressed in the yeast Pichia pastoris was assembled and biologically active

Author keywords

Assembly; Biologically active; Recombinant human fibrinogen; Yeast Pichia pastoris

Indexed keywords

FIBRINOGEN; RECOMBINANT PROTEIN;

EID: 42749089626     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.02.010     Document Type: Article
Times cited : (17)

References (51)
  • 1
    • 0021109431 scopus 로고
    • Characterization of a complementary deoxynucleic acid coding for the α chain of human fibrinogen
    • Rixon M.W., Chan W.Y., Davie E.W., and Chang D.W. Characterization of a complementary deoxynucleic acid coding for the α chain of human fibrinogen. Biochemistry 22 (1983) 3237-3244
    • (1983) Biochemistry , vol.22 , pp. 3237-3244
    • Rixon, M.W.1    Chan, W.Y.2    Davie, E.W.3    Chang, D.W.4
  • 2
    • 0021109413 scopus 로고
    • Characterization of a complementary deoxynucleic acid and genomic deoxyribonucleic acid for the β chain of human fibrinogen
    • Chang D.W., Que B.G., Rixon M.W., Mace Jr. M., and Davie E.W. Characterization of a complementary deoxynucleic acid and genomic deoxyribonucleic acid for the β chain of human fibrinogen. Biochemistry 22 (1983) 3244-3250
    • (1983) Biochemistry , vol.22 , pp. 3244-3250
    • Chang, D.W.1    Que, B.G.2    Rixon, M.W.3    Mace Jr., M.4    Davie, E.W.5
  • 3
    • 0021109426 scopus 로고
    • Characterization of a complementary deoxyribonucleic acid coding for the γ chain of human fibrinogen
    • Chang D.W., Chan W.Y., and Davie E.W. Characterization of a complementary deoxyribonucleic acid coding for the γ chain of human fibrinogen. Biochemistry 22 (1983) 3250-3256
    • (1983) Biochemistry , vol.22 , pp. 3250-3256
    • Chang, D.W.1    Chan, W.Y.2    Davie, E.W.3
  • 4
    • 0025876240 scopus 로고
    • Nucleotide sequence of the three genes coding for human fibrinogen
    • Chang D.W., Harris J.E., and Davie E.W. Nucleotide sequence of the three genes coding for human fibrinogen. Adv. Exp. Med. Biol. 281 (1991) 39-48
    • (1991) Adv. Exp. Med. Biol. , vol.281 , pp. 39-48
    • Chang, D.W.1    Harris, J.E.2    Davie, E.W.3
  • 10
    • 0037700516 scopus 로고    scopus 로고
    • Fibrin sealants in clinical practice
    • Albara D.M. Fibrin sealants in clinical practice. Cardiovasc. Surg. 1 (2003) 5-11
    • (2003) Cardiovasc. Surg. , vol.1 , pp. 5-11
    • Albara, D.M.1
  • 11
  • 12
    • 33845295089 scopus 로고    scopus 로고
    • Use of fibrin sealants for the localized, controlled release of cefazolin
    • Tredwell S., Jackson J.K., Hamilton D., Lee V., and Burt H.M. Use of fibrin sealants for the localized, controlled release of cefazolin. Can. J. Surg. 49 (2006) 347-352
    • (2006) Can. J. Surg. , vol.49 , pp. 347-352
    • Tredwell, S.1    Jackson, J.K.2    Hamilton, D.3    Lee, V.4    Burt, H.M.5
  • 15
    • 0029661284 scopus 로고    scopus 로고
    • The role of βγ and αγ complexes in the assembly of human fibrinogen
    • Huang S., Cao Z., Chung D.W., and Davie E.W. The role of βγ and αγ complexes in the assembly of human fibrinogen. J. Biol. Chem. 271 (1996) 27942-27947
    • (1996) J. Biol. Chem. , vol.271 , pp. 27942-27947
    • Huang, S.1    Cao, Z.2    Chung, D.W.3    Davie, E.W.4
  • 16
    • 0029864510 scopus 로고    scopus 로고
    • The assembly of human fibrinogen
    • Xu W.F., Chung D.W., and Davie E.W. The assembly of human fibrinogen. J. Biol. Chem. 271 (1996) 27948-27953
    • (1996) J. Biol. Chem. , vol.271 , pp. 27948-27953
    • Xu, W.F.1    Chung, D.W.2    Davie, E.W.3
  • 17
    • 0027505548 scopus 로고
    • Characterization of purified recombinant fibrinogen: partial phosphorylation of fibrinopeptide A
    • Binnie C.G., Hettasch J.M., Strickland E., and Lord S.T. Characterization of purified recombinant fibrinogen: partial phosphorylation of fibrinopeptide A. Biochemistry 32 (1993) 107-113
    • (1993) Biochemistry , vol.32 , pp. 107-113
    • Binnie, C.G.1    Hettasch, J.M.2    Strickland, E.3    Lord, S.T.4
  • 19
    • 0030998485 scopus 로고    scopus 로고
    • The conversion of fibrinogen to fibrin: recombinant fibrinogen typifies plasma fibrinogen
    • Gorkun O.V., Veklich Y.I., Weisel J.W., and Lord S.T. The conversion of fibrinogen to fibrin: recombinant fibrinogen typifies plasma fibrinogen. Blood 89 (1997) 4407-4414
    • (1997) Blood , vol.89 , pp. 4407-4414
    • Gorkun, O.V.1    Veklich, Y.I.2    Weisel, J.W.3    Lord, S.T.4
  • 21
    • 0030813942 scopus 로고    scopus 로고
    • Current progress in production of recombinant human fibrinogen in the milk of transgenic animals
    • Butler S.P., Cott K.V., Subrumanian A., Gwazduaskas F.C., and Velander W.H. Current progress in production of recombinant human fibrinogen in the milk of transgenic animals. Thromb. Haemost. 78 (1997) 537-542
    • (1997) Thromb. Haemost. , vol.78 , pp. 537-542
    • Butler, S.P.1    Cott, K.V.2    Subrumanian, A.3    Gwazduaskas, F.C.4    Velander, W.H.5
  • 22
    • 0032238451 scopus 로고    scopus 로고
    • Transgenic animal bioreactors in biotechnology and production of blood proteins
    • Lubon H. Transgenic animal bioreactors in biotechnology and production of blood proteins. Biotechnol. Annu. Rev. 4 (1998) 1-54
    • (1998) Biotechnol. Annu. Rev. , vol.4 , pp. 1-54
    • Lubon, H.1
  • 24
    • 0023912859 scopus 로고
    • High-level expression of a functional human fibrinogen gamma chain in Escherichia coli
    • Bolyard M.G., and Load S.T. High-level expression of a functional human fibrinogen gamma chain in Escherichia coli. Gene 66 (1988) 183-192
    • (1988) Gene , vol.66 , pp. 183-192
    • Bolyard, M.G.1    Load, S.T.2
  • 25
    • 0024515270 scopus 로고
    • Expression in Escherichia coli of the human fibrinogen Bβ chain and its cleavage by thrombin
    • Bolyard M.G., and Load S.T. Expression in Escherichia coli of the human fibrinogen Bβ chain and its cleavage by thrombin. Blood 73 (1989) 1202-1206
    • (1989) Blood , vol.73 , pp. 1202-1206
    • Bolyard, M.G.1    Load, S.T.2
  • 26
    • 0024497457 scopus 로고
    • Expression of a fibrinogen fusion peptide in Escherichia coli: a model thrombin substrate for structure/function analysis
    • Load S.T., and Fowlkes D.M. Expression of a fibrinogen fusion peptide in Escherichia coli: a model thrombin substrate for structure/function analysis. Blood 73 (1989) 166-171
    • (1989) Blood , vol.73 , pp. 166-171
    • Load, S.T.1    Fowlkes, D.M.2
  • 28
  • 29
    • 33645451010 scopus 로고    scopus 로고
    • Mutant fibrinogen cleared from the endoplasmic reticulum via endoplasmic reticulum-associated protein degradation and autophagy
    • Kruse K.B., Dear A., Kaltenbrun E.R., Crum B.E., George P.M., Brennan S.O., and McCracken A.A. Mutant fibrinogen cleared from the endoplasmic reticulum via endoplasmic reticulum-associated protein degradation and autophagy. Am. J. Pathol. 168 (2006) 1299-1308
    • (2006) Am. J. Pathol. , vol.168 , pp. 1299-1308
    • Kruse, K.B.1    Dear, A.2    Kaltenbrun, E.R.3    Crum, B.E.4    George, P.M.5    Brennan, S.O.6    McCracken, A.A.7
  • 30
    • 0027246187 scopus 로고
    • Processing of the carboxyl 15-amino acid extension in the α-chain of fibrinogen
    • Farrell D.H., Huang S., and Davie E.W. Processing of the carboxyl 15-amino acid extension in the α-chain of fibrinogen. J. Biol. Chem. 268 (1993) 10351-10355
    • (1993) J. Biol. Chem. , vol.268 , pp. 10351-10355
    • Farrell, D.H.1    Huang, S.2    Davie, E.W.3
  • 31
    • 0021324744 scopus 로고
    • Potential basis for regulation of the coordinately expressed fibrinogen genes: homology in the 5′ flanking regions
    • Fowlkes D.M., Mullis N.T., Comeau C.M., and Crabtree G.R. Potential basis for regulation of the coordinately expressed fibrinogen genes: homology in the 5′ flanking regions. Proc. Natl. Acad. Sci. USA 81 (1984) 2313-2316
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2313-2316
    • Fowlkes, D.M.1    Mullis, N.T.2    Comeau, C.M.3    Crabtree, G.R.4
  • 33
    • 0028292207 scopus 로고
    • The positive and negative cis-acting elements for methanol regulation in the Pichia pastoris AOX2 gene
    • Ohi H., Miura M., Hiramatsu R., and Ohmura T. The positive and negative cis-acting elements for methanol regulation in the Pichia pastoris AOX2 gene. Mol. Gen. Genet. 243 (1994) 489-499
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 489-499
    • Ohi, H.1    Miura, M.2    Hiramatsu, R.3    Ohmura, T.4
  • 34
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H., Fukuda Y., Murata K., and Kimura A. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153 (1983) 163-168
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 35
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase
    • Tarentino A.L., Gomez C.M., and Plummer Jr. T.H. Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase. Biochemistry 24 (1985) 4665
    • (1985) Biochemistry , vol.24 , pp. 4665
    • Tarentino, A.L.1    Gomez, C.M.2    Plummer Jr., T.H.3
  • 36
    • 0029443619 scopus 로고
    • Expression of a synthetic gene encoding the anticoagulant-antimetastatic protein ghilanten by the methylotrophic yeast Pichia pastoris
    • Brankamp R.G., Sreekrishna K., Smith P.L., Blankenship D.T., and Cardin A.D. Expression of a synthetic gene encoding the anticoagulant-antimetastatic protein ghilanten by the methylotrophic yeast Pichia pastoris. J. Protein Expr. Purif. 6 (1995) 813-820
    • (1995) J. Protein Expr. Purif. , vol.6 , pp. 813-820
    • Brankamp, R.G.1    Sreekrishna, K.2    Smith, P.L.3    Blankenship, D.T.4    Cardin, A.D.5
  • 37
    • 0014817348 scopus 로고
    • Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin
    • McKee P.A., Mattock P., and Hill R.L. Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin. Proc. Natl. Acad. Sci. USA 66 3 (1970) 738-744
    • (1970) Proc. Natl. Acad. Sci. USA , vol.66 , Issue.3 , pp. 738-744
    • McKee, P.A.1    Mattock, P.2    Hill, R.L.3
  • 38
    • 0015498720 scopus 로고
    • Fibrinoligase: the fibrin-stabilizing factor system of blood plasma
    • Lorand L. Fibrinoligase: the fibrin-stabilizing factor system of blood plasma. Ann. NY Acad. Sci. 202 (1972) 6-30
    • (1972) Ann. NY Acad. Sci. , vol.202 , pp. 6-30
    • Lorand, L.1
  • 39
    • 0016759666 scopus 로고
    • Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor (factor XIIIa)
    • Kanaide H., and Shainoff J.R. Cross-linking of fibrinogen and fibrin by fibrin-stabilizing factor (factor XIIIa). J. Lab. Clin. Med. 85 (1975) 574-597
    • (1975) J. Lab. Clin. Med. , vol.85 , pp. 574-597
    • Kanaide, H.1    Shainoff, J.R.2
  • 40
    • 0028809739 scopus 로고
    • The covalent structure of factor XIIIa crosslinked fibrinogen fibrils
    • Mosesson M.W., and Siebenlist K.R. The covalent structure of factor XIIIa crosslinked fibrinogen fibrils. J. Struct. Biol. 115 (1995) 88-101
    • (1995) J. Struct. Biol. , vol.115 , pp. 88-101
    • Mosesson, M.W.1    Siebenlist, K.R.2
  • 41
    • 28444478753 scopus 로고    scopus 로고
    • The αC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis
    • Collet J.P., Moen J.L., Veklich Y.I., Gorkun O.V., Lord S.T., Montalescot G., and Weisel J.W. The αC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis. Blood 106 (2005) 3824-3830
    • (2005) Blood , vol.106 , pp. 3824-3830
    • Collet, J.P.1    Moen, J.L.2    Veklich, Y.I.3    Gorkun, O.V.4    Lord, S.T.5    Montalescot, G.6    Weisel, J.W.7
  • 42
    • 0029661284 scopus 로고    scopus 로고
    • The role of βγ and αγ complexes in the assembly of human fibrinogen
    • Huang S., Cao Z., Chang D.W., and Davie E.W. The role of βγ and αγ complexes in the assembly of human fibrinogen. J. Biol. Chem. 271 (1996) 27942-27947
    • (1996) J. Biol. Chem. , vol.271 , pp. 27942-27947
    • Huang, S.1    Cao, Z.2    Chang, D.W.3    Davie, E.W.4
  • 43
    • 0029861007 scopus 로고    scopus 로고
    • Fibrinogen assembly and secretion
    • Zhang J.Z., and Redman C. Fibrinogen assembly and secretion. J. Biol. Chem. 271 (1996) 30083-30088
    • (1996) J. Biol. Chem. , vol.271 , pp. 30083-30088
    • Zhang, J.Z.1    Redman, C.2
  • 44
    • 33846995713 scopus 로고    scopus 로고
    • A review of the expression, assembly, secretion and intracellular degradation of fibrinogen
    • Redman C.M., and Xia H. A review of the expression, assembly, secretion and intracellular degradation of fibrinogen. Fibrinolysis 14 (2000) 198-205
    • (2000) Fibrinolysis , vol.14 , pp. 198-205
    • Redman, C.M.1    Xia, H.2
  • 45
    • 0034964312 scopus 로고    scopus 로고
    • Fibrinogen biosynthesis, assembly, intracellular degradation, and association with lipid synthesis and secretion
    • Redman C.M., and Xia H. Fibrinogen biosynthesis, assembly, intracellular degradation, and association with lipid synthesis and secretion. Ann. NY Acad. Sci. 936 (2001) 480-495
    • (2001) Ann. NY Acad. Sci. , vol.936 , pp. 480-495
    • Redman, C.M.1    Xia, H.2
  • 47
    • 0029560973 scopus 로고
    • Expression of functional mouse 5-HT5A serotonin receptor in the methylotrophic yeast Pichia pastoris: pharmacological characterization and localization
    • Weiss H.M., Haase W., Michel H., and Reilander H. Expression of functional mouse 5-HT5A serotonin receptor in the methylotrophic yeast Pichia pastoris: pharmacological characterization and localization. FEBS Lett. 377 (1995) 451-456
    • (1995) FEBS Lett. , vol.377 , pp. 451-456
    • Weiss, H.M.1    Haase, W.2    Michel, H.3    Reilander, H.4
  • 49
    • 0029990729 scopus 로고    scopus 로고
    • Secretion of a variant of human single-chain urokinase-type plasminogen activator without an N-glycosylation site in the methylotrophic yeast, Pichia pastoris and characterization of secretion product
    • Tsujikawa M., Okabayashi K., Morita M., and Tanabe T. Secretion of a variant of human single-chain urokinase-type plasminogen activator without an N-glycosylation site in the methylotrophic yeast, Pichia pastoris and characterization of secretion product. Yeast 12 (1996) 541-553
    • (1996) Yeast , vol.12 , pp. 541-553
    • Tsujikawa, M.1    Okabayashi, K.2    Morita, M.3    Tanabe, T.4
  • 50
    • 0019849737 scopus 로고
    • The release of carbohydrate moieties from human fibrinogen by almond glycopeptidase without alteration in fibrinogen clottability
    • Nishibe H., and Takahashi N. The release of carbohydrate moieties from human fibrinogen by almond glycopeptidase without alteration in fibrinogen clottability. Biochim. Biophys. Acta 661 (1981) 274-279
    • (1981) Biochim. Biophys. Acta , vol.661 , pp. 274-279
    • Nishibe, H.1    Takahashi, N.2
  • 51
    • 0018096066 scopus 로고
    • Disfibrinogenemia associated with hepatoma: increased carbohydrate content of the fibrinogen molecule
    • Gralnick H.R., Givelber H., and Abrams E. Disfibrinogenemia associated with hepatoma: increased carbohydrate content of the fibrinogen molecule. N. Engl. J. Med. 299 (1978) 221-226
    • (1978) N. Engl. J. Med. , vol.299 , pp. 221-226
    • Gralnick, H.R.1    Givelber, H.2    Abrams, E.3


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