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Volumn 1814, Issue 2, 2011, Pages 375-387

Conformational and thermal stability of mature dimeric human myeloperoxidase and a recombinant monomeric form from CHO cells

Author keywords

Conformational stability; Innate immune system; Myeloperoxidase; proMPO; Proteolytic processing; Thermal unfolding

Indexed keywords

DIMER; DISULFIDE; DITHIOTHREITOL; ELEMENT; HEME; MONOMER; MYELOPEROXIDASE; PROTEIN; RECOMBINANT ENZYME;

EID: 79251594822     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.09.015     Document Type: Article
Times cited : (28)

References (37)
  • 1
    • 46449130668 scopus 로고    scopus 로고
    • The peroxidase-cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system
    • M. Zamocky, C. Jakopitsch, P.G. Furtmüller, C. Dunand, and C. Obinger The peroxidase-cyclooxygenase superfamily: reconstructed evolution of critical enzymes of the innate immune system Proteins 71 2008 589 605
    • (2008) Proteins , vol.71 , pp. 589-605
    • Zamocky, M.1    Jakopitsch, C.2    Furtmüller, P.G.3    Dunand, C.4    Obinger, C.5
  • 2
    • 0034697020 scopus 로고    scopus 로고
    • X-ray structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution
    • T.J. Fiedler, C.A. Davey, and R.E. Fenna X-ray structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution J. Biol. Chem. 275 2000 11964 11971
    • (2000) J. Biol. Chem. , vol.275 , pp. 11964-11971
    • Fiedler, T.J.1    Davey, C.A.2    Fenna, R.E.3
  • 4
    • 0033546296 scopus 로고    scopus 로고
    • Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo
    • C. Oxvig, A.R. Thomsen, M.T. Overgaard, E.S. Sorensen, P. Hojrup, M.J. Bjerrum, G.J. Gleich, and C. Oxvig Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo J. Biol. Chem. 274 1999 16953 16958
    • (1999) J. Biol. Chem. , vol.274 , pp. 16953-16958
    • Oxvig, C.1    Thomsen, A.R.2    Overgaard, M.T.3    Sorensen, E.S.4    Hojrup, P.5    Bjerrum, M.J.6    Gleich, G.J.7    Oxvig, C.8
  • 7
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • S.J. Klebanoff Myeloperoxidase: friend and foe J. Leukoc. Biol. 77 2005 598 625
    • (2005) J. Leukoc. Biol. , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 9
    • 30544452175 scopus 로고    scopus 로고
    • Biosynthesis, processing, and sorting of human myeloperoxidase
    • M. Hansson, I. Olsson, and W.M. Nauseef Biosynthesis, processing, and sorting of human myeloperoxidase Arch. Biochem. Biophys. 445 2006 214 224
    • (2006) Arch. Biochem. Biophys. , vol.445 , pp. 214-224
    • Hansson, M.1    Olsson, I.2    Nauseef, W.M.3
  • 10
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic molymorphonuclear leukocyte
    • N. Borregaard, and J.B. Cowland Granules of the human neutrophilic molymorphonuclear leukocyte Blood 89 1997 3501 3521
    • (1997) Blood , vol.89 , pp. 3501-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 11
    • 0031665631 scopus 로고    scopus 로고
    • Insights into myeloperoxidase biosynthesis from its inherited deficiency
    • W.M. Nauseef Insights into myeloperoxidase biosynthesis from its inherited deficiency J. Mol. Med. 76 1998 661 668
    • (1998) J. Mol. Med. , vol.76 , pp. 661-668
    • Nauseef, W.M.1
  • 12
    • 0026474687 scopus 로고
    • Roles of heme insertion and the mannose-6-phosphate receptor in processing of the human myeloid lysosomal enzyme, myeloperoxidase
    • W.M. Nauseef, S. McCormick, and H. Yi Roles of heme insertion and the mannose-6-phosphate receptor in processing of the human myeloid lysosomal enzyme, myeloperoxidase Blood 80 1992 2622 2633
    • (1992) Blood , vol.80 , pp. 2622-2633
    • Nauseef, W.M.1    McCormick, S.2    Yi, H.3
  • 13
    • 0025157291 scopus 로고
    • Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures
    • M. Yamada, S.J. Hur, and H. Toda Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures Biochem. Biophys. Res. Commun. 166 1990 852 859
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 852-859
    • Yamada, M.1    Hur, S.J.2    Toda, H.3
  • 14
    • 0025891959 scopus 로고
    • Structural and biological properties of human recombinant myeloperoxidase produced by Chinese hamster ovary cell lines
    • N. Moguilevsky, L. Garcia-Quintana, A. Jacquet, C. Tournay, L. Fabry, L. Pierard, and A. Bollen Structural and biological properties of human recombinant myeloperoxidase produced by Chinese hamster ovary cell lines Eur. J. Biochem. 197 1991 605 614
    • (1991) Eur. J. Biochem. , vol.197 , pp. 605-614
    • Moguilevsky, N.1    Garcia-Quintana, L.2    Jacquet, A.3    Tournay, C.4    Fabry, L.5    Pierard, L.6    Bollen, A.7
  • 16
    • 0032558979 scopus 로고    scopus 로고
    • Reaction of myeloperoxidase compound i with chloride, bromide, iodide, and thiocyanate
    • P.G. Furtmüller, U. Burner, and C. Obinger Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate Biochemistry 37 1998 17923 17930
    • (1998) Biochemistry , vol.37 , pp. 17923-17930
    • Furtmüller, P.G.1    Burner, U.2    Obinger, C.3
  • 17
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least square procedure
    • A. Savitzky, and M.J.E. Golay Smoothing and differentiation of data by simplified least square procedure Anal. Chem. 36 1964 1627 1639
    • (1964) Anal. Chem. , vol.36 , pp. 1627-1639
    • Savitzky, A.1    Golay, M.J.E.2
  • 18
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Meth. Enzymol. 131 1986 266 280
    • (1986) Meth. Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 19
  • 20
    • 0344541766 scopus 로고    scopus 로고
    • Conformational states in denaturants of cytochrome c and horseradish peroxidases examined by fluorescence and circular dichroism
    • G. Tsaprailis, D. Wing Sze Chan, and A.M. English Conformational states in denaturants of cytochrome c and horseradish peroxidases examined by fluorescence and circular dichroism Biochemistry 37 1998 2004 2016
    • (1998) Biochemistry , vol.37 , pp. 2004-2016
    • Tsaprailis, G.1    Wing Sze Chan, D.2    English, A.M.3
  • 22
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor. Evidence for a two-state transition
    • S.E. Jakson, and A. Fersht Folding of chymotrypsin inhibitor. Evidence for a two-state transition Biochemistry 30 1991 10428 10435
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jakson, S.E.1    Fersht, A.2
  • 24
    • 33646721360 scopus 로고    scopus 로고
    • Detection of albumin unfolding preceding proteolysis using Fourier transform infrared spectroscopy and chemometric data analysis
    • A. Domínguez-Vidal, M.P. Saenz-Navajas, M.J. Ayora-Cañada, and B. Lendl Detection of albumin unfolding preceding proteolysis using Fourier transform infrared spectroscopy and chemometric data analysis Anal. Chem. 78 2006 3257 3264
    • (2006) Anal. Chem. , vol.78 , pp. 3257-3264
    • Domínguez-Vidal, A.1    Saenz-Navajas, M.P.2    Ayora-Cañada, M.J.3    Lendl, B.4
  • 25
    • 0035997270 scopus 로고    scopus 로고
    • Automatic amide i frequency selection for rapid quantification of protein secondary structure from Fourier transform infrared spectra of proteins
    • J.A. Hering, P.R. Innocent, and P.I. Haris Automatic amide I frequency selection for rapid quantification of protein secondary structure from Fourier transform infrared spectra of proteins Proteomics 2 2002 839 849
    • (2002) Proteomics , vol.2 , pp. 839-849
    • Hering, J.A.1    Innocent, P.R.2    Haris, P.I.3
  • 26
    • 0032831759 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in analysis of protein deposits
    • S. Seshadri, R. Khurana, and A.L. Fink Fourier transform infrared spectroscopy in analysis of protein deposits Meth. Enzymol. 309 1999 559 576
    • (1999) Meth. Enzymol. , vol.309 , pp. 559-576
    • Seshadri, S.1    Khurana, R.2    Fink, A.L.3
  • 27
    • 0026625050 scopus 로고
    • X-ray crystal structure of canine myeloperoxidase at 3 Å resolution
    • J. Zeng, and R.E. Fenna X-ray crystal structure of canine myeloperoxidase at 3 Å resolution J. Mol. Biol. 226 1992 185 207
    • (1992) J. Mol. Biol. , vol.226 , pp. 185-207
    • Zeng, J.1    Fenna, R.E.2
  • 28
    • 0035923432 scopus 로고    scopus 로고
    • Human myeloperoxidase: Structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 Å resolution
    • M. Blair-Johnson, T. Fiedler, and R.E. Fenna Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 Å resolution Biochemistry 40 2001 13990 13997
    • (2001) Biochemistry , vol.40 , pp. 13990-13997
    • Blair-Johnson, M.1    Fiedler, T.2    Fenna, R.E.3
  • 30
    • 33750346770 scopus 로고    scopus 로고
    • Redox thermodynamics of the Fe(III)/Fe(II) couple of human myeloperoxidase in its high-spin and low-spin forms
    • G. Battistuzzi, M. Bellei, M. Zederbauer, P.G. Furtmüller, M. Sola, and C. Obinger Redox thermodynamics of the Fe(III)/Fe(II) couple of human myeloperoxidase in its high-spin and low-spin forms Biochemistry 45 2006 12750 12755
    • (2006) Biochemistry , vol.45 , pp. 12750-12755
    • Battistuzzi, G.1    Bellei, M.2    Zederbauer, M.3    Furtmüller, P.G.4    Sola, M.5    Obinger, C.6
  • 32
    • 34548311972 scopus 로고    scopus 로고
    • Lactoperoxidase folding and catalysis relies on the stabilization of the α-helix rich core domain: A thermal unfolding study
    • B. Boscolo, S.S. Leal, E.M. Ghibaudi, and C.M. Gomes Lactoperoxidase folding and catalysis relies on the stabilization of the α-helix rich core domain: a thermal unfolding study Biochim. Biophys. Acta 1774 2007 1164 1172
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 1164-1172
    • Boscolo, B.1    Leal, S.S.2    Ghibaudi, E.M.3    Gomes, C.M.4
  • 33
    • 67349089554 scopus 로고    scopus 로고
    • The prominent conformational plasticity of lactoperoxidase: A chemical and pH stability analysis
    • B. Boscolo, S.S. Leal, C. Salgueiro, E.M. Ghibaudi, and C.M. Gomes The prominent conformational plasticity of lactoperoxidase: a chemical and pH stability analysis Biochim. Biophys. Acta 1794 2009 1041 1048
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1041-1048
    • Boscolo, B.1    Leal, S.S.2    Salgueiro, C.3    Ghibaudi, E.M.4    Gomes, C.M.5
  • 34
    • 77952323466 scopus 로고    scopus 로고
    • Differential scanning calorimetry and fluorescence study of lactoperoxidase as a function of guanidinium-HCl, urea, and pH
    • B. Zelent, K.A. Sharp, and J.M. Vanderkooi Differential scanning calorimetry and fluorescence study of lactoperoxidase as a function of guanidinium-HCl, urea, and pH Biochim. Biophys. Acta 1804 2010 1508 1515
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1508-1515
    • Zelent, B.1    Sharp, K.A.2    Vanderkooi, J.M.3
  • 35
    • 33845997473 scopus 로고    scopus 로고
    • Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome
    • C.C. Winterbourn, M.B. Hampton, J.H. Livesey, and A.J. Kettle Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome J. Biol. Chem. 281 2006 39860 39869
    • (2006) J. Biol. Chem. , vol.281 , pp. 39860-39869
    • Winterbourn, C.C.1    Hampton, M.B.2    Livesey, J.H.3    Kettle, A.J.4
  • 36
    • 0019480640 scopus 로고
    • The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH
    • A.W. Segal, M. Geisow, R. Garcia, A. Harper, and R. Miller The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH Nature 290 1981 406 409
    • (1981) Nature , vol.290 , pp. 406-409
    • Segal, A.W.1    Geisow, M.2    Garcia, R.3    Harper, A.4    Miller, R.5
  • 37
    • 30544453606 scopus 로고    scopus 로고
    • Role of eosinophil peroxidase in host defense and disease pathology
    • J. Wang, and A. Slungaard Role of eosinophil peroxidase in host defense and disease pathology Arch. Biochem. Biophys. 445 2006 256 260
    • (2006) Arch. Biochem. Biophys. , vol.445 , pp. 256-260
    • Wang, J.1    Slungaard, A.2


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