메뉴 건너뛰기




Volumn 12, Issue 2, 1998, Pages 201-207

Expression of recombinant human soluble type ii transforming growth factor-β receptor in Pichia pastoris and Escherichia coli: Two powerful systems to express a potent inhibitor of transforming growth factor-β

Author keywords

[No Author keywords available]

Indexed keywords

AGAROSE; CELL DIFFERENTIATION; CELL METABOLISM; CELL PROLIFERATION; GENE EXPRESSION SYSTEM; GLYCOSYLATION; GROWTH FACTOR RECEPTOR; NEUTRALIZATION; PROTEIN FOLDING; PURIFICATION; SOLUBILIZATION; TISSUE REPAIR; TRANSFORMING GROWTH FACTOR;

EID: 0032029757     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1997.0819     Document Type: Article
Times cited : (20)

References (30)
  • 1
    • 0029742706 scopus 로고    scopus 로고
    • Transforming growth factor-beta: A general review
    • Lawrence D. A. Transforming growth factor-beta: A general review. Eur. Cytokine. Netw. 7:1996;363-374.
    • (1996) Eur. Cytokine. Netw. , vol.7 , pp. 363-374
    • Lawrence, D.A.1
  • 2
    • 0027136263 scopus 로고
    • A major advance in the use of growth factors to enhance wound healing
    • Sporn M. B., Roberts A. B. A major advance in the use of growth factors to enhance wound healing. J. Clin. Invest. 92:1993;2565-2566.
    • (1993) J. Clin. Invest. , vol.92 , pp. 2565-2566
    • Sporn, M.B.1    Roberts, A.B.2
  • 3
    • 0028205108 scopus 로고
    • Local injection of TGF-beta increases the strength of tibial fractures in the rat
    • Nielsen H. M., Andreassen T. T., Ledet T., Oxlund H. Local injection of TGF-beta increases the strength of tibial fractures in the rat. Acta Orthop. Scand. 65:1994;37-41.
    • (1994) Acta Orthop. Scand. , vol.65 , pp. 37-41
    • Nielsen, H.M.1    Andreassen, T.T.2    Ledet, T.3    Oxlund, H.4
  • 4
    • 0028128443 scopus 로고
    • In vivo protection against interleukin-1-induced articular cartilage damage by transforming growth factor-beta 1: Age-related differences
    • van Beuningen H. M., van der Kraan P. M., Arntz O. J., van den Berg W. B. In vivo protection against interleukin-1-induced articular cartilage damage by transforming growth factor-beta 1: Age-related differences. Ann. Rheum. Dis. 53:1994;593-600.
    • (1994) Ann. Rheum. Dis. , vol.53 , pp. 593-600
    • Van Beuningen, H.M.1    Van Der Kraan, P.M.2    Arntz, O.J.3    Van Den Berg, W.B.4
  • 5
    • 0028230233 scopus 로고
    • Antibodies against transforming growth factor-beta 1 suppress intimal hyperplasia in a rat model
    • Wolf Y. G., Rasmussen L. M., Ruoslahti E. Antibodies against transforming growth factor-beta 1 suppress intimal hyperplasia in a rat model. J. Clin. Invest. 93:1994;1172-1178.
    • (1994) J. Clin. Invest. , vol.93 , pp. 1172-1178
    • Wolf, Y.G.1    Rasmussen, L.M.2    Ruoslahti, E.3
  • 6
    • 0026676859 scopus 로고
    • Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease
    • Border W. A., Noble N. A., Yamamoto T., Harper J. R., Yamaguchi Y., Pierschbacher M. D., Ruoslahti E. Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease. Nature. 360:1992;361-364.
    • (1992) Nature , vol.360 , pp. 361-364
    • Border, W.A.1    Noble, N.A.2    Yamamoto, T.3    Harper, J.R.4    Yamaguchi, Y.5    Pierschbacher, M.D.6    Ruoslahti, E.7
  • 8
    • 0026505458 scopus 로고
    • Control of scarring in adult wounds by neutralising antibody to transforming growth factor beta
    • Shah M., Foreman D. M., Ferguson M. W. Control of scarring in adult wounds by neutralising antibody to transforming growth factor beta. Lancet. 339:1992;213-214.
    • (1992) Lancet , vol.339 , pp. 213-214
    • Shah, M.1    Foreman, D.M.2    Ferguson, M.W.3
  • 9
    • 0028169834 scopus 로고
    • Transforming growth factor-beta 1 stimulates articular chondrocyte proteoglycan synthesis and induces osteophyte formation in the murine knee joint
    • van Beuningen H. M., van der Kraan P. M., Arntz O. J., van den Berg W. B. Transforming growth factor-beta 1 stimulates articular chondrocyte proteoglycan synthesis and induces osteophyte formation in the murine knee joint. Lab. Invest. 71:1994;279-290.
    • (1994) Lab. Invest. , vol.71 , pp. 279-290
    • Van Beuningen, H.M.1    Van Der Kraan, P.M.2    Arntz, O.J.3    Van Den Berg, W.B.4
  • 10
    • 0026559398 scopus 로고
    • Transforming growth factor beta (TGF-beta) in inflammation: A cause and a cure
    • Wahl S. M. Transforming growth factor beta (TGF-beta) in inflammation: A cause and a cure. J. Clin. Immunol. 12:1992;61-74.
    • (1992) J. Clin. Immunol. , vol.12 , pp. 61-74
    • Wahl, S.M.1
  • 12
    • 0026537831 scopus 로고
    • Expression cloning of the TGF-beta type II receptor, a functional transmembrane serine/threonine kinase
    • Lin H. Y., Wang X. F., Ng Eaton E., Weinberg R. A., Lodish H. F. Expression cloning of the TGF-beta type II receptor, a functional transmembrane serine/threonine kinase. Cell. 68:1992;775-785.
    • (1992) Cell , vol.68 , pp. 775-785
    • Lin, H.Y.1    Wang, X.F.2    Ng Eaton, E.3    Weinberg, R.A.4    Lodish, H.F.5
  • 13
    • 0023253612 scopus 로고
    • A simple sensitive bioassay for interleukin-1 which is unresponsive to 10(3) U/ml of interleukin-2
    • Gearing A. J., Bird C. R., Bristow A., Poole S., Thorpe R. A simple sensitive bioassay for interleukin-1 which is unresponsive to 10(3) U/ml of interleukin-2. J. Immunol. Methods. 99:1987;7-11.
    • (1987) J. Immunol. Methods , vol.99 , pp. 7-11
    • Gearing, A.J.1    Bird, C.R.2    Bristow, A.3    Poole, S.4    Thorpe, R.5
  • 15
    • 0028878041 scopus 로고
    • The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor: A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands
    • Lin H. Y., Moustakas A., Knaus P., Wells R. G., Henis Y. I., Lodish H. F. The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor: A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands. J. Biol. Chem. 270:1995;2747-2754.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2747-2754
    • Lin, H.Y.1    Moustakas, A.2    Knaus, P.3    Wells, R.G.4    Henis, Y.I.5    Lodish, H.F.6
  • 16
    • 0000823705 scopus 로고
    • High level secretion of glycosylated invertase in the methylotrophic yeast Pichia pastoris
    • Tschopp J. F., Sverlow G., Kosson R., Craig W., Grinna L. High level secretion of glycosylated invertase in the methylotrophic yeast Pichia pastoris. Biotechnology. 5:1987;1305-1308.
    • (1987) Biotechnology , vol.5 , pp. 1305-1308
    • Tschopp, J.F.1    Sverlow, G.2    Kosson, R.3    Craig, W.4    Grinna, L.5
  • 17
    • 0024637162 scopus 로고
    • Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris
    • Grinna L. S., Tschopp J. F. Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris. Yeast. 5:1989;107-115.
    • (1989) Yeast. , vol.5 , pp. 107-115
    • Grinna, L.S.1    Tschopp, J.F.2
  • 18
    • 0028361018 scopus 로고
    • Refolding recombinant proteins: Process strategies and novel approaches
    • Chaudhuri J. B. Refolding recombinant proteins: process strategies and novel approaches. Ann. N.Y. Acad. Sci. 721:1994;374-385.
    • (1994) Ann. N.Y. Acad. Sci. , vol.721 , pp. 374-385
    • Chaudhuri, J.B.1
  • 19
    • 0029876942 scopus 로고    scopus 로고
    • Characterization of folded, intermediate, and unfolded states of recombinant human interstitial collagenase
    • Zhang Y., Gray R. D. Characterization of folded, intermediate, and unfolded states of recombinant human interstitial collagenase. J. Biol. Chem. 271:1996;8015-8021.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8015-8021
    • Zhang, Y.1    Gray, R.D.2
  • 20
    • 0028850277 scopus 로고
    • Recombinant human pancreatic ribonuclease produced in E. coli: Importance of the amino-terminal sequence
    • Futami J., Seno M., Kosaka M., Tada H., Seno S., Yamada H. Recombinant human pancreatic ribonuclease produced in E. coli: Importance of the amino-terminal sequence. Biochem. Biophys. Res. Commun. 216:1995;406-413.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 406-413
    • Futami, J.1    Seno, M.2    Kosaka, M.3    Tada, H.4    Seno, S.5    Yamada, H.6
  • 21
    • 0026679842 scopus 로고
    • Isolation and renaturation of bio-active proteins expressed in Escherichia coli as inclusion bodies
    • Fischer B., Sumner I., Goodenough P. Isolation and renaturation of bio-active proteins expressed in Escherichia coli as inclusion bodies. Arzneimittelforschung. 42:1992;1512-1515.
    • (1992) Arzneimittelforschung , vol.42 , pp. 1512-1515
    • Fischer, B.1    Sumner, I.2    Goodenough, P.3
  • 22
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner J., Rudolph R. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Biotechnol. N.Y. 9:1991;157-162.
    • (1991) Biotechnol. N.Y. , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 23
    • 0027941840 scopus 로고
    • Cloning of an isoform of mouse TGF-beta type II receptor gene
    • Suzuki A., Shioda N., Maeda T., Tada M., Ueno N. Cloning of an isoform of mouse TGF-beta type II receptor gene. FEBS Lett. 355:1994;19-22.
    • (1994) FEBS Lett. , vol.355 , pp. 19-22
    • Suzuki, A.1    Shioda, N.2    Maeda, T.3    Tada, M.4    Ueno, N.5
  • 24
    • 0029858733 scopus 로고    scopus 로고
    • The unglycosylated extracellular domain of type-II receptor for transforming growth factor-beta - A novel assay for characterizing ligand affinity and specificity
    • Goetschy J. F., Letourneur O., Cerletti N., Horisberger M. A. The unglycosylated extracellular domain of type-II receptor for transforming growth factor-beta - A novel assay for characterizing ligand affinity and specificity. Eur. J. Biochem. 241:1996;355-362.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 355-362
    • Goetschy, J.F.1    Letourneur, O.2    Cerletti, N.3    Horisberger, M.A.4
  • 25
    • 0027976511 scopus 로고
    • Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: Mapping of ligand binding and GAG attachment sites
    • Lopez Casillas F., Payne H. M., Andres J. L., Massague J. Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: Mapping of ligand binding and GAG attachment sites. J. Cell Biol. 124:1994;557-568.
    • (1994) J. Cell Biol. , vol.124 , pp. 557-568
    • Lopez Casillas, F.1    Payne, H.M.2    Andres, J.L.3    Massague, J.4
  • 26
    • 0027490673 scopus 로고
    • The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand
    • Moustakas A., Lin H. Y., Henis Y. I., Plamondon J., O'Connor McCourt M. D., Lodish H. F. The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand. J. Biol. Chem. 268:1993;22215-22218.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22215-22218
    • Moustakas, A.1    Lin, H.Y.2    Henis, Y.I.3    Plamondon, J.4    O'Connor McCourt, M.D.5    Lodish, H.F.6
  • 27
    • 0029556633 scopus 로고
    • Analysis of the interaction between two TGF-beta-binding proteins and three TGF-beta isoforms using surface plasmon resonance
    • O'Connor McCourt M. D., Segarubu O., Grothe S., Tsang M., Weatherbee J. A. Analysis of the interaction between two TGF-beta-binding proteins and three TGF-beta isoforms using surface plasmon resonance. Ann. N.Y. Acad. Sci. 766:1995;300-302.
    • (1995) Ann. N.Y. Acad. Sci. , vol.766 , pp. 300-302
    • O'Connor McCourt, M.D.1    Segarubu, O.2    Grothe, S.3    Tsang, M.4    Weatherbee, J.A.5
  • 30
    • 0000346267 scopus 로고    scopus 로고
    • Binding affinity of transforming growth factor-beta for its type II receptor is determined by the C-terminal region of the molecule
    • Qian S. W., Burmester J. K., Tsang M. L. S., Weatherbee J. A., Hinck A. P., Ohlsen D. J., Sporn M. B., Roberts A. B. Binding affinity of transforming growth factor-beta for its type II receptor is determined by the C-terminal region of the molecule. J. Biol. Chem. 271:1996;30656-30662.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30656-30662
    • Qian, S.W.1    Burmester, J.K.2    Tsang, M.L.S.3    Weatherbee, J.A.4    Hinck, A.P.5    Ohlsen, D.J.6    Sporn, M.B.7    Roberts, A.B.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.