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Volumn 72, Issue 2, 2010, Pages 179-183

Expression and purification of secreted recombinant hsp60 from eukaryotic cells

Author keywords

Eukaryotic cells; Leader peptide; Recombinant hsp60; Secretion

Indexed keywords

CHAPERONIN; RECOMBINANT PROTEIN;

EID: 77955432426     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.03.021     Document Type: Article
Times cited : (9)

References (22)
  • 1
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • M.J. Gething, and J. Sambrook Protein folding in the cell Nature 355 1992 33 45
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 2
    • 0026520064 scopus 로고
    • Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space
    • H. Koll, B. Guiard, J. Rassow, J. Ostermann, A.L. Horwich, W. Neupert, and F.U. Hartl Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space Cell 68 1992 1163 1175
    • (1992) Cell , vol.68 , pp. 1163-1175
    • Koll, H.1    Guiard, B.2    Rassow, J.3    Ostermann, J.4    Horwich, A.L.5    Neupert, W.6    Hartl, F.U.7
  • 3
    • 0031147756 scopus 로고    scopus 로고
    • Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells
    • B.J. Soltys, and R.S. Gupta Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells Cell Biol. Int. 21 1997 315 320
    • (1997) Cell Biol. Int. , vol.21 , pp. 315-320
    • Soltys, B.J.1    Gupta, R.S.2
  • 6
    • 34248389725 scopus 로고    scopus 로고
    • Chlamydial Hsp60-2 is iron responsive in Chlamydia trachomatis serovar E-infected human endometrial epithelial cells in vitro
    • R.W. LaRue, B.D. Dill, D.K. Giles, J.D. Whittimore, and J.E. Raulston Chlamydial Hsp60-2 is iron responsive in Chlamydia trachomatis serovar E-infected human endometrial epithelial cells in vitro Infect. Immun. 75 2007 2374 2380
    • (2007) Infect. Immun. , vol.75 , pp. 2374-2380
    • Larue, R.W.1    Dill, B.D.2    Giles, D.K.3    Whittimore, J.D.4    Raulston, J.E.5
  • 7
    • 0033559496 scopus 로고    scopus 로고
    • Human 60-kDa heat-shock protein: A danger signal to the innate immune system
    • W. Chen, U. Syldath, K. Bellmann, V. Burkart, and H. Kolb Human 60-kDa heat-shock protein: a danger signal to the innate immune system J. Immunol. 162 1999 3212 3219
    • (1999) J. Immunol. , vol.162 , pp. 3212-3219
    • Chen, W.1    Syldath, U.2    Bellmann, K.3    Burkart, V.4    Kolb, H.5
  • 8
    • 0037080218 scopus 로고    scopus 로고
    • The receptor for heat shock protein 60 on macrophages is saturable, specific, and distinct from receptors for other heat shock proteins
    • C. Habich, K. Baumgart, H. Kolb, and V. Burkart The receptor for heat shock protein 60 on macrophages is saturable, specific, and distinct from receptors for other heat shock proteins J. Immunol. 168 2002 569 576
    • (2002) J. Immunol. , vol.168 , pp. 569-576
    • Habich, C.1    Baumgart, K.2    Kolb, H.3    Burkart, V.4
  • 9
    • 0035903158 scopus 로고    scopus 로고
    • Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells
    • R.M. Vabulas, P. Ahmad-Nejad, C. da Costa, T. Miethke, C.J. Kirschning, H. Hacker, and H. Wagner Endocytosed HSP60s use toll-like receptor 2 (TLR2) and TLR4 to activate the toll/interleukin-1 receptor signaling pathway in innate immune cells J. Biol. Chem. 276 2001 31332 31339
    • (2001) J. Biol. Chem. , vol.276 , pp. 31332-31339
    • Vabulas, R.M.1    Ahmad-Nejad, P.2    Da Costa, C.3    Miethke, T.4    Kirschning, C.J.5    Hacker, H.6    Wagner, H.7
  • 11
    • 0037928705 scopus 로고    scopus 로고
    • Recombinant human heat shock protein 60 does not induce the release of tumor necrosis factor alpha from murine macrophages
    • B. Gao, and M.F. Tsan Recombinant human heat shock protein 60 does not induce the release of tumor necrosis factor alpha from murine macrophages J. Biol. Chem. 278 2003 22523 22529
    • (2003) J. Biol. Chem. , vol.278 , pp. 22523-22529
    • Gao, B.1    Tsan, M.F.2
  • 13
    • 33947510303 scopus 로고    scopus 로고
    • Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide
    • A. Osterloh, U. Kalinke, S. Weiss, B. Fleischer, and M. Breloer Synergistic and differential modulation of immune responses by Hsp60 and lipopolysaccharide J. Biol. Chem. 282 2007 4669 4680
    • (2007) J. Biol. Chem. , vol.282 , pp. 4669-4680
    • Osterloh, A.1    Kalinke, U.2    Weiss, S.3    Fleischer, B.4    Breloer, M.5
  • 16
    • 0020570088 scopus 로고
    • Western blot analysis of the antigens of Toxoplasma gondii recognized by human IgM and IgG antibodies
    • S.D. Sharma, J. Mullenax, F.G. Araujo, H.A. Erlich, and J.S. Remington Western blot analysis of the antigens of Toxoplasma gondii recognized by human IgM and IgG antibodies J. Immunol. 131 1983 977 983
    • (1983) J. Immunol. , vol.131 , pp. 977-983
    • Sharma, S.D.1    Mullenax, J.2    Araujo, F.G.3    Erlich, H.A.4    Remington, J.S.5
  • 17
    • 2942529252 scopus 로고    scopus 로고
    • Identification of the heat shock protein 60 epitope involved in receptor binding on macrophages
    • C. Habich, K. Kempe, V. Burkart, R. Van Der Zee, M. Lillicrap, H. Gaston, and H. Kolb Identification of the heat shock protein 60 epitope involved in receptor binding on macrophages FEBS Lett. 568 2004 65 69
    • (2004) FEBS Lett. , vol.568 , pp. 65-69
    • Habich, C.1    Kempe, K.2    Burkart, V.3    Van Der Zee, R.4    Lillicrap, M.5    Gaston, H.6    Kolb, H.7
  • 18
    • 34147122525 scopus 로고    scopus 로고
    • High level expression and purification of recombinant PEX protein in cultured skeletal muscle cell expression system
    • L. Song, Y. Ke, and Z.Q. Zhang High level expression and purification of recombinant PEX protein in cultured skeletal muscle cell expression system Biochem. Biophys. Res. Commun. 357 2007 258 263
    • (2007) Biochem. Biophys. Res. Commun. , vol.357 , pp. 258-263
    • Song, L.1    Ke, Y.2    Zhang, Z.Q.3
  • 20
    • 62649084049 scopus 로고    scopus 로고
    • Enhancing activity of N-glycosylation for constitutive proteins secretions in non-polarized cells
    • N. Akiyama, Y. Ohno, T. Fukuda, Y. Manome, and S. Saito Enhancing activity of N-glycosylation for constitutive proteins secretions in non-polarized cells Biochem. Biophys. Res. Commun. 381 2009 612 618
    • (2009) Biochem. Biophys. Res. Commun. , vol.381 , pp. 612-618
    • Akiyama, N.1    Ohno, Y.2    Fukuda, T.3    Manome, Y.4    Saito, S.5
  • 21
    • 30044444506 scopus 로고    scopus 로고
    • Decorin core protein secretion is regulated by N-linked oligosaccharide and glycosaminoglycan additions
    • N.S. Seo, A.M. Hocking, M. Hook, and D.J. McQuillan Decorin core protein secretion is regulated by N-linked oligosaccharide and glycosaminoglycan additions J. Biol. Chem. 280 2005 42774 42784
    • (2005) J. Biol. Chem. , vol.280 , pp. 42774-42784
    • Seo, N.S.1    Hocking, A.M.2    Hook, M.3    McQuillan, D.J.4
  • 22
    • 0031042618 scopus 로고    scopus 로고
    • Apical sorting of hepatitis B surface antigen (HBsAg) is independent of N-glycosylation and glucosylphosphatidylinositol-anchored protein segregation
    • M.P. Marzolo, P. Bull, and A. Gonzalez Apical sorting of hepatitis B surface antigen (HBsAg) is independent of N-glycosylation and glucosylphosphatidylinositol-anchored protein segregation Proc. Natl. Acad. Sci. USA 94 1997 1834 1839
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1834-1839
    • Marzolo, M.P.1    Bull, P.2    Gonzalez, A.3


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