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Volumn 444, Issue 3, 2012, Pages 417-428

Bivalent and co-operative binding of complement Factor H to heparan sulfate and heparin

Author keywords

Analytical ultracentrifugation; Factor H; Heparan sulfate; Surface plasmon resonance; X ray scattering

Indexed keywords

COMPLEMENT FACTOR H; HEPARAN SULFATE; HEPARIN; MONOSACCHARIDE;

EID: 84862183665     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20120183     Document Type: Article
Times cited : (20)

References (57)
  • 3
    • 0023890664 scopus 로고
    • Molecular organization and function of the complement system
    • Müller-Eberhard, H. J. (1988) Molecular organization and function of the complement system. Annu. Rev. Biochem. 57, 321-347
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 321-347
    • Müller-Eberhard, H.J.1
  • 4
    • 0003727098 scopus 로고
    • (Second edition), IRL Press, Oxford
    • Law, S. K. A. and Reid, K. B. M. (1995) Complement (Second edition), IRL Press, Oxford
    • (1995) Complement
    • Law, S.K.A.1    Reid, K.B.M.2
  • 5
    • 0012042656 scopus 로고
    • Control of the amplification convertase of complement by the plasma protein β1H
    • Weiler, J. M., Daha, M. R., Austen, K. F. and Fearon, D. T. (1976) Control of the amplification convertase of complement by the plasma protein β1H. Proc. Natl. Acad. Sci. U.S.A. 73, 3268-3272
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 3268-3272
    • Weiler, J.M.1    Daha, M.R.2    Austen, K.F.3    Fearon, D.T.4
  • 6
    • 0017704496 scopus 로고
    • Human complement C3b inactivator: isolation, characterization, and demonstration of an absolute requirement for the serum protein β1H for cleavage of C3b and C4b in solution
    • Pangburn, M. K., Schreiber, R. D. and Müller-Eberhard, H. J. (1977) Human complement C3b inactivator: isolation, characterization, and demonstration of an absolute requirement for the serum protein β1H for cleavage of C3b and C4b in solution. J. Exp. Med. 146, 257-270 (Pubitemid 8139507)
    • (1977) Journal of Experimental Medicine , vol.146 , Issue.1 , pp. 257-270
    • Pangburn, M.K.1    Schreiber, R.D.2    Muller, E.H.J.3
  • 7
    • 0017088173 scopus 로고
    • Modulation of C3b hemolytic activity by a plasma protein distinct from C3b inactivator
    • Whaley, K. and Ruddy, S. (1976) Modulation of C3b hemolytic activity by a plasma protein distinct from C3b inactivator. Science 193, 1011-1013
    • (1976) Science , vol.193 , pp. 1011-1013
    • Whaley, K.1    Ruddy, S.2
  • 8
    • 29744434976 scopus 로고    scopus 로고
    • Complement control protein modules in the regulators of complement activators
    • Morikis, D. and Lambris, J. D., eds Taylor and Francis, Boca Raton
    • Soares, D. and Barlow, P. N. (2005) Complement control protein modules in the regulators of complement activators. In Structural Biology of the Complement System (Morikis, D. and Lambris, J. D., eds), pp. 19-62, Taylor and Francis, Boca Raton
    • (2005) Structural Biology of the Complement System , pp. 19-62
    • Soares, D.1    Barlow, P.N.2
  • 9
    • 0029763437 scopus 로고    scopus 로고
    • Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis
    • DOI 10.1073/pnas.93.20.10996
    • Sharma, A. K. and Pangburn, M. K. (1996) Identification of three physically and functionally distinct binding sites for C3b in human complement factor H by deletion mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 93, 10996-11001 (Pubitemid 26333106)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.20 , pp. 10996-11001
    • Sharma, A.K.1    Pangburn, M.K.2
  • 10
    • 0034623118 scopus 로고    scopus 로고
    • Each of the three binding sites of factor H interacts with a distinct site on C3b
    • Jokiranta, T. S., Hellwage, J., Koistinen, V., Zipfel, P. F. and Meri, S. (2000) Each of the three binding sites of factor H interacts with a distinct site on C3b. J. Biol. Chem. 275, 27657-27662
    • (2000) J. Biol. Chem. , vol.275 , pp. 27657-27662
    • Jokiranta, T.S.1    Hellwage, J.2    Koistinen, V.3    Zipfel, P.F.4    Meri, S.5
  • 11
    • 0018317786 scopus 로고
    • Human alternative complement pathway: Membrane-associated sialic acid regulates the competition between B and β1H for cell-bound C3b
    • Kazatchkine, M. D., Fearon, D. T. and Austen, K. F. (1979) Human alternative complement pathway: membrane-associated sialic acid regulates the competition between B and β1H for cell-bound C3b. J. Immunol. 122, 75-81 (Pubitemid 9078522)
    • (1979) Journal of Immunology , vol.122 , Issue.1 , pp. 75-81
    • Kazatchkine, M.D.1    Fearon, D.T.2    Austen, K.F.3
  • 12
    • 0024827512 scopus 로고
    • Regulation of the human alternative complement pathway: Formation of a ternary complex between factor H, surface-bound C3b and chemical groups on nonactivating surfaces
    • DOI 10.1002/eji.1830191126
    • Carreno, M. P., Labarre, D., Maillet, F., Jozefowicz, M. and Kazatchkine, M. D. (1989) Regulation of the human alternative complement pathway: formation of a ternary complex between factor H, surface-bound C3b and chemical groups on nonactivating surfaces. Eur. J. Immunol. 19, 2145-2150 (Pubitemid 20017724)
    • (1989) European Journal of Immunology , vol.19 , Issue.11 , pp. 2145-2150
    • Carreno, M.P.1    Labarre, D.2    Maillet, F.3    Jozefowicz, M.4    Kazatchkine, M.D.5
  • 13
    • 84930482695 scopus 로고    scopus 로고
    • The molecular architecture of heparin and heparan sulfate: Recent developments in solution structural studies
    • Mulloy, B., Khan, S. and Perkins, S. J. (2012) The molecular architecture of heparin and heparan sulfate: recent developments in solution structural studies. Pure Appl. Chem. 84, 65-76
    • (2012) Pure Appl. Chem. , vol.84 , pp. 65-76
    • Mulloy, B.1    Khan, S.2    Perkins, S.J.3
  • 14
    • 0030589294 scopus 로고    scopus 로고
    • Identification of a Heparin Binding Domain in the Seventh Short Consensus Repeat of Complement Factor H
    • Blackmore, T. K., Sadlon, T. A., Ward, H. M., Lublin, D. M. and Gordon, D. L. (1996) Identification of a heparin binding domain in the seventh short consensus repeat of complement factor H. J. Immunol. 157, 5422-5427 (Pubitemid 126448961)
    • (1996) Journal of Immunology , vol.157 , Issue.12 , pp. 5422-5427
    • Blackmore, T.K.1    Sadlon, T.A.2    Ward, H.M.3    Lublin, D.M.4    Gordon, D.L.5
  • 18
    • 0028934221 scopus 로고
    • An international classification and grading system for age related maculopathy and age-related macular degeneration
    • The International ARM Epidemiological Study Group
    • The International ARM Epidemiological Study Group (1995) An international classification and grading system for age related maculopathy and age-related macular degeneration. Surv. Ophthalmol. 39, 367-374
    • (1995) Surv. Ophthalmol. , vol.39 , pp. 367-374
  • 19
    • 0034832029 scopus 로고    scopus 로고
    • An integrated hypothesis that considers drusen as biomarkers of immune-mediated processes at the RPE-Bruch's membrane interface in aging and age-related macular degeneration
    • DOI 10.1016/S1350-9462(01)00010-6, PII S1350946201000106
    • Hageman, G. S., Luthert, P. J., Victor Chong, N. H., Johnson, L. V., Anderson, D. H. and Mullins, R. F. (2001) An integrated hypothesis that considers drusen as biomarkers of immune mediated processes at the RPE-Bruch's membrane interface in aging and age-related macular degeneration. Prog. Retinal Eye Res. 20, 705-732 (Pubitemid 32918285)
    • (2001) Progress in Retinal and Eye Research , vol.20 , Issue.6 , pp. 705-732
    • Hageman, G.S.1    Luthert, P.J.2    Victor, C.N.H.3    Johnson, L.V.4    Anderson, D.H.5    Mullins, R.F.6
  • 23
    • 17244379811 scopus 로고    scopus 로고
    • Complement factor H polymorphism and age-related macular degeneration
    • DOI 10.1126/science.1110189
    • Edwards, A. O., Ritter, III, R., Abel, K. J., Manning, A., Panhuysen, C. and Farrer, L. A. (2005) Complement factor H polymorphism and age-related macular degeneration. Science 308, 421-424 (Pubitemid 40530082)
    • (2005) Science , vol.308 , Issue.5720 , pp. 421-424
    • Edwards, A.O.1    Ritter III, R.2    Abel, K.J.3    Manning, A.4    Panhuysen, C.5    Farrer, L.A.6
  • 26
    • 84855282981 scopus 로고    scopus 로고
    • Complement factor H-ligand interactions: Self-association, multivalency and dissociation constants
    • Perkins, S. J., Nan, R., Li, K., Khan, S. and Miller, A. (2012) Complement factor H-ligand interactions: self-association, multivalency and dissociation constants. Immunobiology 217, 281-297
    • (2012) Immunobiology , vol.217 , pp. 281-297
    • Perkins, S.J.1    Nan, R.2    Li, K.3    Khan, S.4    Miller, A.5
  • 27
    • 73249136226 scopus 로고    scopus 로고
    • Semi-rigid solution structures of heparin by constrained X-ray scattering modelling: New insight into heparin-protein complexes
    • Khan, S., Gor, J., Mulloy, B. and Perkins, S. J. (2010) Semi-rigid solution structures of heparin by constrained X-ray scattering modelling: new insight into heparin-protein complexes. J. Mol. Biol. 395, 504-521
    • (2010) J. Mol. Biol. , vol.395 , pp. 504-521
    • Khan, S.1    Gor, J.2    Mulloy, B.3    Perkins, S.J.4
  • 28
    • 79960113013 scopus 로고    scopus 로고
    • The solution structure of heparan sulphate differs from that of heparin: Implications for function
    • Khan, S., Rodriguez, E., Patel, R., Gor, J., Mulloy, B. and Perkins, S. J. (2011) The solution structure of heparan sulphate differs from that of heparin: implications for function. J. Biol. Chem. 286, 24842-24854
    • (2011) J. Biol. Chem. , vol.286 , pp. 24842-24854
    • Khan, S.1    Rodriguez, E.2    Patel, R.3    Gor, J.4    Mulloy, B.5    Perkins, S.J.6
  • 33
    • 69949145065 scopus 로고    scopus 로고
    • Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights
    • Perkins, S. J., Okemefuna, A. I., Nan, R., Li, K. and Bonner, A. (2009) Constrained solution scattering modelling of human antibodies and complement proteins reveals novel biological insights. J. R. Soc., Interface 6, S679-S696
    • (2009) J. R. Soc., Interface , vol.6
    • Perkins, S.J.1    Okemefuna, A.I.2    Nan, R.3    Li, K.4    Bonner, A.5
  • 34
    • 0027377724 scopus 로고
    • Complement factor I and cofactors in control of complement system convertase enzymes
    • Sim, R. B., Day, A. J., Moffatt, B. E. and Fontaine, M. (1993) Complement factor I and cofactors in control of complement system convertase enzymes. Meth. Enzymol. 223, 13-35
    • (1993) Meth. Enzymol. , vol.223 , pp. 13-35
    • Sim, R.B.1    Day, A.J.2    Moffatt, B.E.3    Fontaine, M.4
  • 35
    • 33947593444 scopus 로고    scopus 로고
    • Associative and Structural Properties of the Region of Complement Factor H Encompassing the Tyr402His Disease-related Polymorphism and its Interactions with Heparin
    • DOI 10.1016/j.jmb.2007.02.038, PII S0022283607002197
    • Fernando, A. N., Furtado, P. B., Clark, S. J., Gilbert, H. E., Day, A. J., Sim, R. B. and Perkins, S. J. (2007) Associative and structural properties of the region of complement factor H encompassing the Tyr402His disease-related polymorphism and its interactions with heparin. J. Mol. Biol. 368, 564-581 (Pubitemid 46483491)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.2 , pp. 564-581
    • Fernando, A.N.1    Furtado, P.B.2    Clark, S.J.3    Gilbert, H.E.4    Day, A.J.5    Sim, R.B.6    Perkins, S.J.7
  • 36
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini, L., Burke, D. F., von Delft, F., Mulloy, B. and Blundell, T. L. (2000) Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 407, 1029-1034
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 37
    • 35449002345 scopus 로고    scopus 로고
    • Analytical ultracentrifugation: Sedimentation velocity and sedimentation equilibrium
    • Cole, J. L., Lary, J. W., Moody, T. P. and Laue, T. M. (2008) Analytical ultracentrifugation: sedimentation velocity and sedimentation equilibrium. Meth. Cell Biol. 84, 143-211
    • (2008) Meth. Cell Biol. , vol.84 , pp. 143-211
    • Cole, J.L.1    Lary, J.W.2    Moody, T.P.3    Laue, T.M.4
  • 38
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins, S. J. (1986) Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157, 169-180
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 39
    • 1842428822 scopus 로고    scopus 로고
    • Calculating Sedimentation Coefficient Distributions by Direct Modeling of Sedimentation Velocity Concentration Profiles
    • DOI 10.1016/S0076-6879(04)84012-6
    • Dam, J. and Schuck, P. (2004) Calculating sedimentation coefficient distribution by direct modeling of sedimentation velocity concentration profiles. Meth. Enzymol. 384, 185-212 (Pubitemid 38420481)
    • (2004) Methods in Enzymology , vol.384 , pp. 185-212
    • Dam, J.1    Schuck, P.2
  • 40
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 43
    • 0026244044 scopus 로고
    • GNOM: A program package for small-angle scattering data-processing
    • Semenyuk, A. V. and Svergun, D. I. (1991) GNOM: a program package for small-angle scattering data-processing. J. Appl. Crystallogr. 24, 537-540
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 44
    • 27644530203 scopus 로고    scopus 로고
    • Kinetic studies on the interactions of heparin and complement proteins using surface plasmon resonance
    • DOI 10.1016/j.bbagen.2005.08.003, PII S0304416505002588
    • Yu, H., Muńoz, E. M., Edens, R. E. and Linhardt, R. J. (2005) Kinetic studies on the interactions of heparin and complement proteins using surface plasmon resonance. Biochim. Biophys. Acta 1726, 168-176 (Pubitemid 41572256)
    • (2005) Biochimica et Biophysica Acta - General Subjects , vol.1726 , Issue.2 , pp. 168-176
    • Yu, H.1    Munoz, E.M.2    Edens, R.E.3    Linhardt, R.J.4
  • 45
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia de la Torre, J., Huertas, M. L. and Carrasco, B. (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78, 719-730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 46
    • 35448951213 scopus 로고    scopus 로고
    • Biosensor-surface plasmon resonance methods for quantitative analysis of biomolecular interactions
    • Tanious, F. A., Nguyen, B. and Wilson, W. D. (2008) Biosensor-surface plasmon resonance methods for quantitative analysis of biomolecular interactions. Meth. Cell Biol. 84, 53-77
    • (2008) Meth. Cell Biol. , vol.84 , pp. 53-77
    • Tanious, F.A.1    Nguyen, B.2    Wilson, W.D.3
  • 47
    • 0033921990 scopus 로고    scopus 로고
    • Host recognition and target differentiation by factor H, a regulator of the alternative pathway of complement
    • Pangburn, M. K. (2000) Host recognition and target differentiation by factor H, a regulator of the alternative pathway of complement. Immunopharmacology 49, 149-157
    • (2000) Immunopharmacology , vol.49 , pp. 149-157
    • Pangburn, M.K.1
  • 48
    • 0025314311 scopus 로고
    • Discrimination between activators and nonactivators of the alternative pathway of complement: Regulation via a sialic acid/polyanion binding site on factor H
    • Meri, S. and Pangburn, M. K. (1990) Discrimination between activators and nonactivators of the alternative pathway of complement: regulation via a sialic acid/polyanion binding site on factor H. Proc. Natl. Acad. Sci. U.S.A. 87, 3982-3986
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3982-3986
    • Meri, S.1    Pangburn, M.K.2
  • 49
    • 0011579669 scopus 로고
    • Complement C3 convertase: Cell surface restriction of βIH control and generation of restriction on neuraminidase treated cells
    • Pangburn, M. K. and M̈uller-Eberhard, H. J. (1978) Complement C3 convertase: cell surface restriction of βIH control and generation of restriction on neuraminidase treated cells. Proc. Natl. Acad. Sci. U.S.A. 75, 2416-2420
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 2416-2420
    • Pangburn, M.K.1    M̈uller-Eberhard, H.J.2
  • 50
    • 33745202838 scopus 로고    scopus 로고
    • Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure
    • Herbert, A. P., Uhrin, D., Lyon, M., Pangburn, M. K. and Barlow, P. N. (2006) Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure. J. Biol. Chem. 281, 16512-16520
    • (2006) J. Biol. Chem. , vol.281 , pp. 16512-16520
    • Herbert, A.P.1    Uhrin, D.2    Lyon, M.3    Pangburn, M.K.4    Barlow, P.N.5
  • 51
    • 33746614761 scopus 로고    scopus 로고
    • Interactions between heparan sulfate and proteins: The concept of specificity
    • DOI 10.1083/jcb.200604035
    • Kreuger, J., Spillmann, D., Li, J. P. and Lindahl, U. (2006) Interactions between heparan sulfate and proteins: the concept of specificity. J. Cell Biol. 174, 323-327 (Pubitemid 44156762)
    • (2006) Journal of Cell Biology , vol.174 , Issue.3 , pp. 323-327
    • Kreuger, J.1    Spillmann, D.2    Li, J.-P.3    Lindahl, U.4
  • 52
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks, W. P. (1981) On the attribution and additivity of binding energies. Proc. Natl. Acad. Sci. U.S.A. 78, 4046-4050
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 53
    • 77956378437 scopus 로고    scopus 로고
    • Therapeutic targets in age-related macular disease
    • Bird, A. C. (2010) Therapeutic targets in age-related macular disease. J. Clin. Invest. 120, 3033-3041
    • (2010) J. Clin. Invest. , vol.120 , pp. 3033-3041
    • Bird, A.C.1
  • 54
    • 77955965634 scopus 로고    scopus 로고
    • Multiple interactions of complement factor H with its ligands in solution: A progress report
    • Perkins, S. J., Nan, R., Okemefuna, A. I., Li, K., Khan, S. and Miller, A. (2010) Multiple interactions of complement factor H with its ligands in solution: a progress report. Adv. Exp. Med. Biol. 703, 25-47
    • (2010) Adv. Exp. Med. Biol. , vol.703 , pp. 25-47
    • Perkins, S.J.1    Nan, R.2    Okemefuna, A.I.3    Li, K.4    Khan, S.5    Miller, A.6
  • 55
    • 33747700932 scopus 로고    scopus 로고
    • His-384 allotypic variant of factor H associated with age-related macular degeneration has different heparin binding properties from the non-disease-associated form
    • DOI 10.1074/jbc.M605083200
    • Clark, S. J., Higman, V. A., Mulloy, B., Perkins, S. J., Lea, S. M., Sim, R. B. and Day, A. J. (2006) H384 allotypic variant of factor H associated with age-related macular degeneration has different heparin-binding properties from the non-disease associated form. J. Biol. Chem. 281, 24713-24720 (Pubitemid 44274245)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24713-24720
    • Clark, S.J.1    Higman, V.A.2    Mulloy, B.3    Perkins, S.J.4    Lea, S.M.5    Sim, R.B.6    Day, A.J.7
  • 56
    • 77956897697 scopus 로고    scopus 로고
    • Impaired binding of the AMD-associated complement factor H 402H allotype to Bruch's membrane in human retina
    • Clark, S. J., Perveen, R., Hakobyan, S., Morgan, B. P., Sim, R. B., Bishop, P. N. and Day, A. J. (2010) Impaired binding of the AMD-associated complement factor H 402H allotype to Bruch's membrane in human retina. J. Biol. Chem. 285, 30192-30202
    • (2010) J. Biol. Chem. , vol.285 , pp. 30192-30202
    • Clark, S.J.1    Perveen, R.2    Hakobyan, S.3    Morgan, B.P.4    Sim, R.B.5    Bishop, P.N.6    Day, A.J.7
  • 57
    • 77952580558 scopus 로고    scopus 로고
    • Pulling the trigger in atypical hemolytic uremic syndrome: The role of pregnancy
    • Goodship, T. H. J. and Kavanagh, D. (2010) Pulling the trigger in atypical hemolytic uremic syndrome: the role of pregnancy. J. Am. Soc. Nephrol. 21, 731-732
    • (2010) J. Am. Soc. Nephrol. , vol.21 , pp. 731-732
    • Goodship, T.H.J.1    Kavanagh, D.2


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