메뉴 건너뛰기




Volumn 287, Issue 18, 2012, Pages 14897-14911

Goodpasture antigen-binding protein/ceramide transporter binds to human serum amyloid P-component and is present in brain amyloid plaques

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; AMYLOID DEPOSITS; AMYLOID PLAQUES; ANTIGEN-BINDING; BASEMENT MEMBRANE; COLOCALIZE; DECAMERS; EXTRACELLULAR MATRICES; HUMAN SERUM; INNATE IMMUNE SYSTEMS; PATHOLOGICAL CONDITIONS; PENTAMERS; SERUM AMYLOID P;

EID: 84860365186     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.299545     Document Type: Article
Times cited : (32)

References (52)
  • 1
    • 0031587295 scopus 로고    scopus 로고
    • Pentameric and decameric structures in solution of serum amyloid P component by x-ray and neutron scattering and molecular modeling analyses
    • Ashton, A. W., Boehm, M. K., Gallimore, J. R., Pepys, M. B., and Perkins, S. J. (1997) Pentameric and decameric structures in solution of serum amyloid P component by x-ray and neutron scattering and molecular modeling analyses. J. Mol. Biol. 272, 408-422
    • (1997) J. Mol. Biol. , vol.272 , pp. 408-422
    • Ashton, A.W.1    Boehm, M.K.2    Gallimore, J.R.3    Pepys, M.B.4    Perkins, S.J.5
  • 2
    • 0000493952 scopus 로고
    • Immunologic Studies on a Protein Extracted from Human Secondary Amyloid
    • Cathcart, E. S., Comerford, F. R., and Cohen, A. S. (1965) Immunologic Studies on a Protein Extracted from Human Secondary Amyloid. N. Engl. J. Med. 273, 143-146
    • (1965) N. Engl. J. Med. , vol.273 , pp. 143-146
    • Cathcart, E.S.1    Comerford, F.R.2    Cohen, A.S.3
  • 3
    • 47849127085 scopus 로고    scopus 로고
    • Inflammatory aspects of Alzheimer disease and other neurodegenerative disorders
    • Schwab, C., and McGeer, P. L. (2008) Inflammatory aspects of Alzheimer disease and other neurodegenerative disorders. J. Alzheimers Dis. 13, 359-369
    • (2008) J. Alzheimers Dis. , vol.13 , pp. 359-369
    • Schwab, C.1    McGeer, P.L.2
  • 4
    • 0038417096 scopus 로고    scopus 로고
    • Amyloid β plaqueassociated proteins C1q and SAP enhance the Aβ1-42 peptide-induced cytokine secretion by adult human microglia in vitro
    • Veerhuis, R., Van Breemen, M. J., Hoozemans, J. M., Morbin, M., Ouladhadj, J., Tagliavini, F., and Eikelenboom, P. (2003) Amyloid β plaqueassociated proteins C1q and SAP enhance the Aβ1-42 peptide-induced cytokine secretion by adult human microglia in vitro. Acta Neuropathol. 105, 135-144
    • (2003) Acta Neuropathol. , vol.105 , pp. 135-144
    • Veerhuis, R.1    Van Breemen, M.J.2    Hoozemans, J.M.3    Morbin, M.4    Ouladhadj, J.5    Tagliavini, F.6    Eikelenboom, P.7
  • 5
    • 0029010736 scopus 로고
    • Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis
    • Tennent, G. A., Lovat, L. B., and Pepys, M. B. (1995) Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. Proc. Natl. Acad. Sci. U.S.A. 92, 4299-4303
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 4299-4303
    • Tennent, G.A.1    Lovat, L.B.2    Pepys, M.B.3
  • 6
    • 0020000306 scopus 로고
    • The structure and binding characteristics of serum amyloid protein (9.5S α 1-glycoprotein)
    • Painter, R. H., De Escallón, I., Massey, A., Pinteric, L., and Stern, S. B. (1982) The structure and binding characteristics of serum amyloid protein (9.5S α 1-glycoprotein). Ann. N.Y. Acad. Sci. 389, 199-215
    • (1982) Ann. N.Y. Acad. Sci. , vol.389 , pp. 199-215
    • Painter, R.H.1    De Escallón, I.2    Massey, A.3    Pinteric, L.4    Stern, S.B.5
  • 7
    • 0028988187 scopus 로고
    • 2+-dependent binding of human serum amyloid P component to Alzheimer β-amyloid peptide
    • 2+-dependent binding of human serum amyloid P component to Alzheimer β-amyloid peptide. J. Biol. Chem. 270, 10392-10394
    • (1995) J. Biol. Chem. , vol.270 , pp. 10392-10394
    • Hamazaki, H.1
  • 8
    • 0023644521 scopus 로고
    • 2+-mediated association of human serum amyloid P component with heparan sulfate and dermatan sulfate
    • 2+-mediated association of human serum amyloid P component with heparan sulfate and dermatan sulfate. J. Biol. Chem. 262, 1456-1460
    • (1987) J. Biol. Chem. , vol.262 , pp. 1456-1460
    • Hamazaki, H.1
  • 9
    • 17544374217 scopus 로고    scopus 로고
    • Characterization of the binding of serum amyloid P to type IV collagen
    • Zahedi, K. (1996) Characterization of the binding of serum amyloid P to type IV collagen. J. Biol. Chem. 271, 14897-14902
    • (1996) J. Biol. Chem. , vol.271 , pp. 14897-14902
    • Zahedi, K.1
  • 10
    • 0031019170 scopus 로고    scopus 로고
    • Characterization of the binding of serum amyloid P to laminin
    • Zahedi, K. (1997) Characterization of the binding of serum amyloid P to laminin. J. Biol. Chem. 272, 2143-2148
    • (1997) J. Biol. Chem. , vol.272 , pp. 2143-2148
    • Zahedi, K.1
  • 11
    • 0027990760 scopus 로고
    • Calcium-enhanced aggregation of serum amyloid P component and its inhibition by the ligands heparin and heparan sulfate. An electron microscopic and immunoelectrophoretic study
    • Nielsen, E. H., Sørensen, I. J., Vilsgaard, K., Andersen, O., and Svehag, S. E. (1994) Calcium-enhanced aggregation of serum amyloid P component and its inhibition by the ligands heparin and heparan sulfate. An electron microscopic and immunoelectrophoretic study. APMIS 102, 420-426
    • (1994) APMIS , vol.102 , pp. 420-426
    • Nielsen, E.H.1    Sørensen, I.J.2    Vilsgaard, K.3    Andersen, O.4    Svehag, S.E.5
  • 12
    • 0019453750 scopus 로고
    • Fibronectin and C4-binding protein are selectively bound by aggregated amyloid P component
    • de Beer, F. C., Baltz, M. L., Holford, S., Feinstein, A., and Pepys, M. B. (1981) Fibronectin and C4-binding protein are selectively bound by aggregated amyloid P component. J. Exp. Med. 154, 1134-1139
    • (1981) J. Exp. Med. , vol.154 , pp. 1134-1139
    • De Beer, F.C.1    Baltz, M.L.2    Holford, S.3    Feinstein, A.4    Pepys, M.B.5
  • 13
    • 0022966845 scopus 로고
    • Evidence for the binding of human serum amyloid P component to Clq and Fab γ
    • Bristow, C. L., and Boackle, R. J. (1986) Evidence for the binding of human serum amyloid P component to Clq and Fab γ. Mol. Immunol. 23, 1045-1052
    • (1986) Mol. Immunol. , vol.23 , pp. 1045-1052
    • Bristow, C.L.1    Boackle, R.J.2
  • 14
    • 0019471538 scopus 로고
    • Agglutination of complement-coated erythrocytes by serum amyloid P component
    • Hutchcraft, C. L., Gewurz, H., Hansen, B., Dyck, R. F., and Pepys, M. B. (1981) Agglutination of complement-coated erythrocytes by serum amyloid P component. J. Immunol. 126, 1217-1219
    • (1981) J. Immunol. , vol.126 , pp. 1217-1219
    • Hutchcraft, C.L.1    Gewurz, H.2    Hansen, B.3    Dyck, R.F.4    Pepys, M.B.5
  • 15
    • 0028787494 scopus 로고
    • Serum amyloid P component binding to C4b-binding protein
    • García de Frutos, P., Härdig, Y., and Dahlbäck, B. (1995) Serum amyloid P component binding to C4b-binding protein. J. Biol. Chem. 270, 26950-26955
    • (1995) J. Biol. Chem. , vol.270 , pp. 26950-26955
    • García De Frutos, P.1    Härdig, Y.2    Dahlbäck, B.3
  • 16
    • 0027394985 scopus 로고
    • Human serum amyloid P component oligomers bind and activate the classical complement pathway via residues 14-26 and 76-92 of the A chain collagen-like region of C1q
    • Ying, S. C., Gewurz, A. T., Jiang, H., and Gewurz, H. (1993) Human serum amyloid P component oligomers bind and activate the classical complement pathway via residues 14-26 and 76-92 of the A chain collagen-like region of C1q. J. Immunol. 150, 169-176
    • (1993) J. Immunol. , vol.150 , pp. 169-176
    • Ying, S.C.1    Gewurz, A.T.2    Jiang, H.3    Gewurz, H.4
  • 18
    • 0023021790 scopus 로고
    • Binding specificity of mouse serum amyloid P-component for fibronectin
    • Tseng, J., and Mortensen, R. F. (1986) Binding specificity of mouse serum amyloid P-component for fibronectin. Immunol. Invest. 15, 749-761
    • (1986) Immunol. Invest. , vol.15 , pp. 749-761
    • Tseng, J.1    Mortensen, R.F.2
  • 19
    • 0000843533 scopus 로고
    • Goodpasture's syndrome (pulmonary hemorrhage associated with glomerulonephritis)
    • Stanton, M. C., and Tange, J. D. (1958) Goodpasture's syndrome (pulmonary hemorrhage associated with glomerulonephritis). Australas. Ann. Med. 7, 132-144
    • (1958) Australas. Ann. Med. , vol.7 , pp. 132-144
    • Stanton, M.C.1    Tange, J.D.2
  • 20
    • 0033617196 scopus 로고    scopus 로고
    • Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human Goodpasture antigen
    • Raya, A., Revert, F., Navarro, S., and Saus, J. (1999) Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human Goodpasture antigen. J. Biol. Chem. 274, 12642-12649
    • (1999) J. Biol. Chem. , vol.274 , pp. 12642-12649
    • Raya, A.1    Revert, F.2    Navarro, S.3    Saus, J.4
  • 22
    • 57649210159 scopus 로고    scopus 로고
    • Goodpasture antigen-binding protein is a soluble exportable protein that interacts with type IV collagen. Identification of novel membrane-bound isoforms
    • Revert, F., Ventura, I., Martínez-Martínez, P., Granero-Moltó, F., Revert-Ros, F., Macías, J., and Saus, J. (2008) Goodpasture antigen-binding protein is a soluble exportable protein that interacts with type IV collagen. Identification of novel membrane-bound isoforms. J. Biol. Chem. 283, 30246-30255
    • (2008) J. Biol. Chem. , vol.283 , pp. 30246-30255
    • Revert, F.1    Ventura, I.2    Martínez-Martínez, P.3    Granero-Moltó, F.4    Revert-Ros, F.5    Macías, J.6    Saus, J.7
  • 23
    • 84860366497 scopus 로고    scopus 로고
    • Goodpasture antigen-binding protein and its detection
    • May 3, U.S. Patent no. US7935492
    • Saus, J. V., and Revert, F. M. (May 3, 2011) Goodpasture antigen-binding protein and its detection, U.S. Patent no. US7935492
    • (2011)
    • Saus, J.V.1    Revert, F.M.2
  • 25
    • 0034704149 scopus 로고    scopus 로고
    • Goodpasture antigen-binding protein, the kinase that phosphorylates the Goodpasture antigen, is an alternatively spliced variant implicated in autoimmune pathogenesis
    • Raya, A., Revert-Ros, F., Martinez-Martinez, P., Navarro, S., Rosello, E., Vieites, B., Granero, F., Forteza, J., and Saus, J. (2000) Goodpasture antigen-binding protein, the kinase that phosphorylates the Goodpasture antigen, is an alternatively spliced variant implicated in autoimmune pathogenesis. J. Biol. Chem. 275, 40392-40399
    • (2000) J. Biol. Chem. , vol.275 , pp. 40392-40399
    • Raya, A.1    Revert-Ros, F.2    Martinez-Martinez, P.3    Navarro, S.4    Rosello, E.5    Vieites, B.6    Granero, F.7    Forteza, J.8    Saus, J.9
  • 28
    • 77949382968 scopus 로고    scopus 로고
    • Optical thermophoresis for quantifying the buffer dependence of aptamer binding
    • Baaske, P., Wienken, C. J., Reineck, P., Duhr, S., and Braun, D. (2010) Optical thermophoresis for quantifying the buffer dependence of aptamer binding. Angew. Chem. Int. Ed. Engl. 49, 2238-2241
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 2238-2241
    • Baaske, P.1    Wienken, C.J.2    Reineck, P.3    Duhr, S.4    Braun, D.5
  • 29
    • 84855254333 scopus 로고    scopus 로고
    • Protein-binding assays in biological liquids using microscale thermophoresis
    • Wienken, C. J., Baaske, P., Rothbauer, U., Braun, D., and Duhr, S. (2010) Protein-binding assays in biological liquids using microscale thermophoresis. Nat. Commun. 1, 100
    • (2010) Nat. Commun. , vol.1 , pp. 100
    • Wienken, C.J.1    Baaske, P.2    Rothbauer, U.3    Braun, D.4    Duhr, S.5
  • 31
    • 0029013727 scopus 로고
    • Staging of Alzheimer's disease-related neurofibrillary changes
    • discussion 278-284
    • Braak, H., and Braak, E. (1995) Staging of Alzheimer's disease-related neurofibrillary changes. Neurobiol. Aging 16, 271-278; discussion 278-284
    • (1995) Neurobiol. Aging , vol.16 , pp. 271-278
    • Braak, H.1    Braak, E.2
  • 33
    • 0023001765 scopus 로고
    • Amyloid P component is not present in the glomerular basement membrane in Alport-type hereditary nephritis
    • Melvin, T., Kim, Y., and Michael, A. F. (1986) Amyloid P component is not present in the glomerular basement membrane in Alport-type hereditary nephritis. Am. J. Pathol. 125, 460-464
    • (1986) Am. J. Pathol. , vol.125 , pp. 460-464
    • Melvin, T.1    Kim, Y.2    Michael, A.F.3
  • 34
    • 0027450581 scopus 로고
    • Tissue distribution of amyloid P component as defined by a monoclonal antibody produced by immunization with human glomerular basement membranes
    • al-Mutlaq, H., Wheeler, J., Robertson, H., Watchorn, C., and Morley, A. R. (1993) Tissue distribution of amyloid P component as defined by a monoclonal antibody produced by immunization with human glomerular basement membranes. Histochem. J. 25, 219-227
    • (1993) Histochem. J. , vol.25 , pp. 219-227
    • Al-Mutlaq, H.1    Wheeler, J.2    Robertson, H.3    Watchorn, C.4    Morley, A.R.5
  • 35
    • 0022385459 scopus 로고
    • Effect of divalent metal ions and pH upon the binding reactivity of human serum amyloid P component, a C-reactive protein homologue, for zymosan. Preferential reactivity in the presence of copper and acidic pH
    • Potempa, L. A., Kubak, B. M., and Gewurz, H. (1985) Effect of divalent metal ions and pH upon the binding reactivity of human serum amyloid P component, a C-reactive protein homologue, for zymosan. Preferential reactivity in the presence of copper and acidic pH. J. Biol. Chem. 260, 12142-12147
    • (1985) J. Biol. Chem. , vol.260 , pp. 12142-12147
    • Potempa, L.A.1    Kubak, B.M.2    Gewurz, H.3
  • 37
    • 0033748351 scopus 로고    scopus 로고
    • Mapping proteinprotein interaction domains using ordered fragment ladder far Western analysis of hexahistidine-tagged fusion proteins
    • Burgess, R. R., Arthur, T. M., and Pietz, B. C. (2000) Mapping proteinprotein interaction domains using ordered fragment ladder far Western analysis of hexahistidine-tagged fusion proteins. Methods Enzymol. 328, 141-157
    • (2000) Methods Enzymol. , vol.328 , pp. 141-157
    • Burgess, R.R.1    Arthur, T.M.2    Pietz, B.C.3
  • 38
  • 39
    • 0018101816 scopus 로고
    • Comparative clinical study of protein SAP (amyloid P component) and C-reactive protein in serum
    • Pepys, M. B., Dash, A. C., Markham, R. E., Thomas, H. C., Williams, B. D., and Petrie, A. (1978) Comparative clinical study of protein SAP (amyloid P component) and C-reactive protein in serum. Clin. Exp. Immunol. 32, 119-124
    • (1978) Clin. Exp. Immunol. , vol.32 , pp. 119-124
    • Pepys, M.B.1    Dash, A.C.2    Markham, R.E.3    Thomas, H.C.4    Williams, B.D.5    Petrie, A.6
  • 40
    • 77952316540 scopus 로고    scopus 로고
    • An integrated view of humoral innate immunity. Pentraxins as a paradigm
    • Bottazzi, B., Doni, A., Garlanda, C., and Mantovani, A. (2010) An integrated view of humoral innate immunity. Pentraxins as a paradigm. Annu. Rev. Immunol. 28, 157-183
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 157-183
    • Bottazzi, B.1    Doni, A.2    Garlanda, C.3    Mantovani, A.4
  • 42
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young, L., Jernigan, R. L., and Covell, D. G. (1994) A role for surface hydrophobicity in protein-protein recognition. Protein Sci. 3, 717-729
    • (1994) Protein Sci. , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 43
    • 0018899125 scopus 로고
    • Amyloid P-component in human glomerular basement membrane. Abnormal patterns of immunofluorescent staining in glomerular disease
    • Dyck, R. F., Evans, D. J., Lockwood, C. M., Rees, A. J., Turner, D., and Pepys, M. B. (1980) Amyloid P-component in human glomerular basement membrane. Abnormal patterns of immunofluorescent staining in glomerular disease. Lancet 2, 606-609
    • (1980) Lancet , vol.2 , pp. 606-609
    • Dyck, R.F.1    Evans, D.J.2    Lockwood, C.M.3    Rees, A.J.4    Turner, D.5    Pepys, M.B.6
  • 44
    • 0031580201 scopus 로고    scopus 로고
    • Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP
    • Hohenester, E., Hutchinson, W. L., Pepys, M. B., and Wood, S. P. (1997) Crystal structure of a decameric complex of human serum amyloid P component with bound dAMP. J. Mol. Biol. 269, 570-578
    • (1997) J. Mol. Biol. , vol.269 , pp. 570-578
    • Hohenester, E.1    Hutchinson, W.L.2    Pepys, M.B.3    Wood, S.P.4
  • 45
    • 0036077121 scopus 로고    scopus 로고
    • The structures of crystalline complexes of human serum amyloid P component with its carbohydrate ligand, the cyclic pyruvate acetal of galactose
    • Thompson, D., Pepys, M. B., Tickle, I., and Wood, S. (2002) The structures of crystalline complexes of human serum amyloid P component with its carbohydrate ligand, the cyclic pyruvate acetal of galactose. J. Mol. Biol. 320, 1081-1086
    • (2002) J. Mol. Biol. , vol.320 , pp. 1081-1086
    • Thompson, D.1    Pepys, M.B.2    Tickle, I.3    Wood, S.4
  • 46
    • 0031054058 scopus 로고    scopus 로고
    • Production of C-reactive protein and risk of coronary events in stable and unstable angina
    • European Concerted Action on Thrombosis and Disabilities Angina Pectoris Study Group
    • Haverkate, F., Thompson, S. G., Pyke, S. D., Gallimore, J. R., and Pepys, M. B. (1997) Production of C-reactive protein and risk of coronary events in stable and unstable angina. European Concerted Action on Thrombosis and Disabilities Angina Pectoris Study Group. Lancet 349, 462-466
    • (1997) Lancet , vol.349 , pp. 462-466
    • Haverkate, F.1    Thompson, S.G.2    Pyke, S.D.3    Gallimore, J.R.4    Pepys, M.B.5
  • 47
    • 77449112767 scopus 로고    scopus 로고
    • Crystal structures of the CERT START domain with inhibitors provide insights into the mechanism of ceramide transfer
    • Kudo, N., Kumagai, K., Matsubara, R., Kobayashi, S., Hanada, K., Wakatsuki, S., and Kato, R. (2010) Crystal structures of the CERT START domain with inhibitors provide insights into the mechanism of ceramide transfer. J. Mol. Biol. 396, 245-251
    • (2010) J. Mol. Biol. , vol.396 , pp. 245-251
    • Kudo, N.1    Kumagai, K.2    Matsubara, R.3    Kobayashi, S.4    Hanada, K.5    Wakatsuki, S.6    Kato, R.7
  • 49
    • 0028787769 scopus 로고
    • Distribution of β amyloid-associated proteins in plaques in Alzheimer disease and in the non-demented elderly
    • Zhan, S. S., Veerhuis, R., Kamphorst, W., and Eikelenboom, P. (1995) Distribution of β amyloid-associated proteins in plaques in Alzheimer disease and in the non-demented elderly. Neurodegeneration 4, 291-297
    • (1995) Neurodegeneration , vol.4 , pp. 291-297
    • Zhan, S.S.1    Veerhuis, R.2    Kamphorst, W.3    Eikelenboom, P.4
  • 50
    • 33947281600 scopus 로고    scopus 로고
    • Minocycline does not affect amyloid β phagocytosis by human microglial cells
    • Familian, A., Eikelenboom, P., and Veerhuis, R. (2007) Minocycline does not affect amyloid β phagocytosis by human microglial cells. Neurosci. Lett. 416, 87-91
    • (2007) Neurosci. Lett. , vol.416 , pp. 87-91
    • Familian, A.1    Eikelenboom, P.2    Veerhuis, R.3
  • 51
    • 24744435980 scopus 로고    scopus 로고
    • Ligand-assisted aggregation of proteins. Dimerization of serum amyloid P component by bivalent ligands
    • Ho, J. G., Kitov, P. I., Paszkiewicz, E., Sadowska, J., Bundle, D. R., and Ng, K. K. (2005) Ligand-assisted aggregation of proteins. Dimerization of serum amyloid P component by bivalent ligands. J. Biol. Chem. 280, 31999-32008
    • (2005) J. Biol. Chem. , vol.280 , pp. 31999-32008
    • Ho, J.G.1    Kitov, P.I.2    Paszkiewicz, E.3    Sadowska, J.4    Bundle, D.R.5    Ng, K.K.6
  • 52
    • 0025863618 scopus 로고
    • Neuropathological staging of Alzheimerrelated changes
    • Braak, H., and Braak, E. (1991) Neuropathological staging of Alzheimerrelated changes. Acta Neuropathol. 82, 239-259
    • (1991) Acta Neuropathol. , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.