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Volumn 25, Issue 4, 2005, Pages 305-330

Immune function of C1q and its modulators CD91 and CD93

Author keywords

Apoptosis; C1q; CD91; CD93; Collectins; Phagocytosis

Indexed keywords

CD93 ANTIGEN; COLLAGEN; COMPLEMENT COMPONENT C1; COMPLEMENT COMPONENT C1Q; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 30444440869     PISSN: 10408401     EISSN: None     Source Type: Journal    
DOI: 10.1615/CritRevImmunol.v25.i4.40     Document Type: Review
Times cited : (32)

References (176)
  • 1
    • 0036498603 scopus 로고    scopus 로고
    • Cooperation of C1q receptors and integrins in C1q-mediated endothelial cell adhesion and spreading
    • Feng X, Tonnesen MG, Peerschke EI, Ghebrehiwet B. Cooperation of C1q receptors and integrins in C1q-mediated endothelial cell adhesion and spreading. J Immunol. 2002;168:2441-8.
    • (2002) J Immunol , vol.168 , pp. 2441-2448
    • Feng, X.1    Tonnesen, M.G.2    Peerschke, E.I.3    Ghebrehiwet, B.4
  • 2
    • 0027971888 scopus 로고
    • Effect of C1q on the processing of immune complexes by human neutrophils
    • Ohkuro M, Kobayashi K, Takahashi K, Nagasawa S. Effect of C1q on the processing of immune complexes by human neutrophils. Immunology. 1994;83:507-11.
    • (1994) Immunology , vol.83 , pp. 507-511
    • Ohkuro, M.1    Kobayashi, K.2    Takahashi, K.3    Nagasawa, S.4
  • 3
    • 0031569975 scopus 로고    scopus 로고
    • C1q binds directly and specifically to surface blebs of apoptotic human keratinocytes: Complement deficiency and systemic lupus erythematosus revisited
    • Korb LC, Ahearn JM. C1q binds directly and specifically to surface blebs of apoptotic human keratinocytes: complement deficiency and systemic lupus erythematosus revisited. J Immunol. 1997;158:4525-8.
    • (1997) J Immunol , vol.158 , pp. 4525-4528
    • Korb, L.C.1    Ahearn, J.M.2
  • 5
    • 0019505302 scopus 로고
    • Interaction of C-reactive protein with artificial phosphatidylcholine bilayers and complement
    • Volanakis JE, Narkates AJ. Interaction of C-reactive protein with artificial phosphatidylcholine bilayers and complement. J Immunol. 1981;126:1820-5.
    • (1981) J Immunol , vol.126 , pp. 1820-1825
    • Volanakis, J.E.1    Narkates, A.J.2
  • 6
    • 0036748152 scopus 로고    scopus 로고
    • Interaction of C1q and mannan-binding lectin with viruses
    • Thielens NM, Tacnet-Delorme P, Arlaud GJ. Interaction of C1q and mannan-binding lectin with viruses. Immunobiology. 2002;205:563-74.
    • (2002) Immunobiology , vol.205 , pp. 563-574
    • Thielens, N.M.1    Tacnet-Delorme, P.2    Arlaud, G.J.3
  • 7
    • 0019844466 scopus 로고
    • C1q binding and complement activation by capsular and cell wall components of S. pneumoniae type XIX
    • Prellner K. C1q binding and complement activation by capsular and cell wall components of S. pneumoniae type XIX. Acta Pathol Microbiol Scand [C]. 1981;89:359-64.
    • (1981) Acta Pathol Microbiol Scand [C] , vol.89 , pp. 359-364
    • Prellner, K.1
  • 8
    • 0024397811 scopus 로고
    • Histories and mysteries about C1
    • Borsos T. Histories and mysteries about C1. Behring Inst Mitt. 1989:1-7.
    • (1989) Behring Inst Mitt , pp. 1-7
    • Borsos, T.1
  • 9
    • 0343555026 scopus 로고
    • Chromatographic resolution of the first component of human complement into three activities
    • Lepow IH, Naff GB, Todd EW, Pensky J, Hinz CF. Chromatographic resolution of the first component of human complement into three activities. J Exp Med. 1963;117:983-1008.
    • (1963) J Exp Med , vol.117 , pp. 983-1008
    • Lepow, I.H.1    Naff, G.B.2    Todd, E.W.3    Pensky, J.4    Hinz, C.F.5
  • 10
    • 0031697413 scopus 로고    scopus 로고
    • MASP1 (MBL-associated serine protease 1)
    • Matsushita M, Endo Y, Fujita T. MASP1 (MBL-associated serine protease 1). Immunobiology. 1998;199:340-7.
    • (1998) Immunobiology , vol.199 , pp. 340-347
    • Matsushita, M.1    Endo, Y.2    Fujita, T.3
  • 12
    • 0018151413 scopus 로고
    • Initiation of the alternative pathway of complement: Recognition of activators by bound C3b and assembly of the entire pathway from six isolated proteins
    • Schreiber RD, Pangburn MK, Lesavre PH, Muller-Eberhard HJ. Initiation of the alternative pathway of complement: recognition of activators by bound C3b and assembly of the entire pathway from six isolated proteins. Proc Natl Acad Sci U S A. 1978;75:3948-52.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 3948-3952
    • Schreiber, R.D.1    Pangburn, M.K.2    Lesavre, P.H.3    Muller-Eberhard, H.J.4
  • 13
    • 0027828449 scopus 로고
    • Similarity in structure between C1q and the collectins as judged by electron microscopy
    • Lu J, Wiedemann H, Timpl R, Reid KB. Similarity in structure between C1q and the collectins as judged by electron microscopy. Behring Inst Mitt. 1993:6-16.
    • (1993) Behring Inst Mitt , pp. 6-16
    • Lu, J.1    Wiedemann, H.2    Timpl, R.3    Reid, K.B.4
  • 14
    • 0015444985 scopus 로고
    • Isolation and characterization of C1q, a subcomponent of the first component of complement, from human and rabbit sera
    • Reid KB, Lowe DM, Porter RR. Isolation and characterization of C1q, a subcomponent of the first component of complement, from human and rabbit sera. Biochem J. 1972;130:749-63.
    • (1972) Biochem J , vol.130 , pp. 749-763
    • Reid, K.B.1    Lowe, D.M.2    Porter, R.R.3
  • 15
    • 0015340734 scopus 로고
    • Structural studies on human C1q: Non-covalent and covalent subunits
    • Yonemasu K, Stroud RM. Structural studies on human C1q: non-covalent and covalent subunits. Immunochemistry. 1972;9:545-54.
    • (1972) Immunochemistry , vol.9 , pp. 545-554
    • Yonemasu, K.1    Stroud, R.M.2
  • 16
    • 0017261951 scopus 로고
    • Isolation, by partial pepsin digestion, of the three collagen-like regions present in subcomponent C1q of the first component of human complement
    • Reid KB. Isolation, by partial pepsin digestion, of the three collagen-like regions present in subcomponent C1q of the first component of human complement. Biochem J. 1976;155:5-17.
    • (1976) Biochem J , vol.155 , pp. 5-17
    • Reid, K.B.1
  • 17
    • 0017073905 scopus 로고
    • Circular-dichroism and electron-microscopy studies of human subcomponent C1q before and after limited proteolysis by pepsin
    • Brodsky-Doyle B, Leonard KR, Reid KB. Circular-dichroism and electron-microscopy studies of human subcomponent C1q before and after limited proteolysis by pepsin. Biochem J. 1976;159:279-86.
    • (1976) Biochem J , vol.159 , pp. 279-286
    • Brodsky-Doyle, B.1    Leonard, K.R.2    Reid, K.B.3
  • 18
    • 0022344621 scopus 로고
    • Molecular cloning and characterization of the complementary DNA and gene coding for the B-chain of subcomponent C1q of the human complement system
    • Reid KB. Molecular cloning and characterization of the complementary DNA and gene coding for the B-chain of subcomponent C1q of the human complement system. Biochem J. 1985;231:729-35.
    • (1985) Biochem J , vol.231 , pp. 729-735
    • Reid, K.B.1
  • 19
    • 0026019308 scopus 로고
    • Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q
    • Sellar GC, Blake DJ, Reid KB. Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q. Biochem J. 1991;274(Pt 2):481-90.
    • (1991) Biochem J , vol.274 , Issue.PART 2 , pp. 481-490
    • Sellar, G.C.1    Blake, D.J.2    Reid, K.B.3
  • 20
    • 0021894435 scopus 로고
    • The classical complement pathway: Activation and regulation of the first complement component
    • Cooper NR. The classical complement pathway: activation and regulation of the first complement component. Adv Immunol. 1985;37:151-216.
    • (1985) Adv Immunol , vol.37 , pp. 151-216
    • Cooper, N.R.1
  • 21
    • 0024341918 scopus 로고
    • Chemistry and molecular genetics of C1q
    • Reid KB. Chemistry and molecular genetics of C1q. Behring Inst Mitt. 1989:8-19.
    • (1989) Behring Inst Mitt , pp. 8-19
    • Reid, K.B.1
  • 22
    • 0018355771 scopus 로고
    • Active disassembly of the first complement component, C-1, by C-1 inactivator
    • Ziccardi RJ, Cooper NR. Active disassembly of the first complement component, C-1, by C-1 inactivator. J Immunol. 1979;123:788-92.
    • (1979) J Immunol , vol.123 , pp. 788-792
    • Ziccardi, R.J.1    Cooper, N.R.2
  • 23
    • 0020004989 scopus 로고
    • A new role for C-1-inhibitor in homeostasis: Control of activation of the first component of human complement
    • Ziccardi RJ. A new role for C-1-inhibitor in homeostasis: control of activation of the first component of human complement. J Immunol. 1982;128:2505-8.
    • (1982) J Immunol , vol.128 , pp. 2505-2508
    • Ziccardi, R.J.1
  • 24
    • 0020580435 scopus 로고
    • Neutron scattering studies of the isolated C1r2C1s2 subunit of first component of human complement in solution
    • Boyd J, Burton DR, Perkins SJ, Villiers CL, Dwek RA, Arlaud GJ. Neutron scattering studies of the isolated C1r2C1s2 subunit of first component of human complement in solution. Proc Natl Acad Sci U S A. 1983;80:3769-73.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 3769-3773
    • Boyd, J.1    Burton, D.R.2    Perkins, S.J.3    Villiers, C.L.4    Dwek, R.A.5    Arlaud, G.J.6
  • 25
    • 0019168322 scopus 로고
    • Assembly of subcomponents C1r and C1s of first component of complement: Electron microscopic and ultracentrifugal studies
    • Tschopp J, Villiger W, Fuchs H, Kilchherr E, Engel J. Assembly of subcomponents C1r and C1s of first component of complement: electron microscopic and ultracentrifugal studies. Proc Natl Acad Sci U S A. 1980;77:7014-8.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 7014-7018
    • Tschopp, J.1    Villiger, W.2    Fuchs, H.3    Kilchherr, E.4    Engel, J.5
  • 26
  • 27
    • 0020702354 scopus 로고
    • Measurement of the association constants of the complexes formed between intact C1q or pepsin-treated C1q stalks and the unactivated or activated C1r2C1s2 tetramers
    • Siegel RC, Schumaker VN. Measurement of the association constants of the complexes formed between intact C1q or pepsin-treated C1q stalks and the unactivated or activated C1r2C1s2 tetramers. Mol Immunol. 1983;20:53-66.
    • (1983) Mol Immunol , vol.20 , pp. 53-66
    • Siegel, R.C.1    Schumaker, V.N.2
  • 28
    • 0020033478 scopus 로고
    • Ultrastructure of the first component of human complement: Electron microscopy of the crosslinked complex
    • Strang CJ, Siegel RC, Phillips ML, Poon PH, Schumaker VN. Ultrastructure of the first component of human complement: electron microscopy of the crosslinked complex. Proc Natl Acad Sci U S A. 1982;79:586-90.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 586-590
    • Strang, C.J.1    Siegel, R.C.2    Phillips, M.L.3    Poon, P.H.4    Schumaker, V.N.5
  • 29
    • 0021857415 scopus 로고
    • Immunoglobulin G: Functional sites
    • Burton DR. Immunoglobulin G: functional sites. Mol Immunol. 1985;22:161-206.
    • (1985) Mol Immunol , vol.22 , pp. 161-206
    • Burton, D.R.1
  • 30
    • 0018387528 scopus 로고
    • Isolation of the globular region of the subcomponent q of the C1 component of complement
    • Paques EP, Huber R, Priess H, Wright JK. Isolation of the globular region of the subcomponent q of the C1 component of complement. Hoppe Seylers Z Physiol Chem. 1979;360:177-83.
    • (1979) Hoppe Seylers Z Physiol Chem , vol.360 , pp. 177-183
    • Paques, E.P.1    Huber, R.2    Priess, H.3    Wright, J.K.4
  • 31
    • 0022557568 scopus 로고
    • A molecular mechanism for the activation of the first component of complement by immune complexes
    • Schumaker VN, Hanson DC, Kilchherr E, Phillips ML, Poon PH. A molecular mechanism for the activation of the first component of complement by immune complexes. Mol Immunol. 1986;23:557-65.
    • (1986) Mol Immunol , vol.23 , pp. 557-565
    • Schumaker, V.N.1    Hanson, D.C.2    Kilchherr, E.3    Phillips, M.L.4    Poon, P.H.5
  • 32
    • 0023897194 scopus 로고
    • The binding site for C1q on IgG
    • Duncan AR, Winter G. The binding site for C1q on IgG. Nature. 1988;332:738-40.
    • (1988) Nature , vol.332 , pp. 738-740
    • Duncan, A.R.1    Winter, G.2
  • 33
    • 0026009904 scopus 로고
    • Solution structure of human and mouse immunoglobulin M by synchrotron X-ray scattering and molecular graphics modelling. A possible mechanism for complement activation
    • Perkins SJ, Nealis AS, Sutton BJ, Feinstein A. Solution structure of human and mouse immunoglobulin M by synchrotron X-ray scattering and molecular graphics modelling. A possible mechanism for complement activation. J Mol Biol 1991;221:1345-66.
    • (1991) J Mol Biol , vol.221 , pp. 1345-1366
    • Perkins, S.J.1    Nealis, A.S.2    Sutton, B.J.3    Feinstein, A.4
  • 36
    • 0022499513 scopus 로고
    • Isolation and characterization of macrophage-derived C1q and its similarities to serum C1q
    • Rabs U, Martin H, Hitschold T, Golan MD, Heinz HP, Loos M. Isolation and characterization of macrophage-derived C1q and its similarities to serum C1q. Eur J Immunol. 1986;16:1183-6.
    • (1986) Eur J Immunol , vol.16 , pp. 1183-1186
    • Rabs, U.1    Martin, H.2    Hitschold, T.3    Golan, M.D.4    Heinz, H.P.5    Loos, M.6
  • 37
    • 0018083981 scopus 로고
    • Biosynthesis of the first component of complement by human and guinea pig peritoneal macrophages: Evidence for an independent production of the C1 subunits
    • Muller W, Hanauske-Abel H, Loos M. Biosynthesis of the first component of complement by human and guinea pig peritoneal macrophages: evidence for an independent production of the C1 subunits. J Immunol. 1978;121:1578-84.
    • (1978) J Immunol , vol.121 , pp. 1578-1584
    • Muller, W.1    Hanauske-Abel, H.2    Loos, M.3
  • 38
    • 0022515610 scopus 로고
    • Biosynthesis of the subcomponents C1q, C1r and C1s of the first component of complement (C1) by guinea pig hepatocyte primary cultures
    • Ramadori G, Heinz HP, Martin H, Meyer zum Buschenfelde KH, Loos M. Biosynthesis of the subcomponents C1q, C1r and C1s of the first component of complement (C1) by guinea pig hepatocyte primary cultures. Eur J Immunol. 1986;16:1137-41.
    • (1986) Eur J Immunol , vol.16 , pp. 1137-1141
    • Ramadori, G.1    Heinz, H.P.2    Martin, H.3    Meyer Zum Buschenfelde, K.H.4    Loos, M.5
  • 39
    • 0020080177 scopus 로고
    • Stimulation of a human polymorphonuclear leukocyte oxidative response by the CIq subunit of the first complement component
    • Tenner AJ, Cooper NR. Stimulation of a human polymorphonuclear leukocyte oxidative response by the CIq subunit of the first complement component. J Immunol. 1982;128:2547-52.
    • (1982) J Immunol , vol.128 , pp. 2547-2552
    • Tenner, A.J.1    Cooper, N.R.2
  • 41
    • 0023808083 scopus 로고
    • Identification and partial characterization of human platelet C1q binding sites
    • Peerschke EI, Ghebrehiwet B. Identification and partial characterization of human platelet C1q binding sites. J Immunol. 1988;141:3505-11.
    • (1988) J Immunol , vol.141 , pp. 3505-3511
    • Peerschke, E.I.1    Ghebrehiwet, B.2
  • 42
    • 0019413642 scopus 로고
    • Demonstration of a C1q receptor on the surface of human endothelial cells
    • Andrews BS, Shadforth M, Cunningham P, Davis JS IV. Demonstration of a C1q receptor on the surface of human endothelial cells. J Immunol. 1981;127:1075-80.
    • (1981) J Immunol , vol.127 , pp. 1075-1080
    • Andrews, B.S.1    Shadforth, M.2    Cunningham, P.3    Davis IV, J.S.4
  • 43
    • 0020669135 scopus 로고
    • Biosynthesis of the collagen-like C1q molecule and its receptor functions for Fc and polyanionic molecules on macrophages
    • Loos M. Biosynthesis of the collagen-like C1q molecule and its receptor functions for Fc and polyanionic molecules on macrophages. Curr Top Microbiol Immunol. 1983;102:1-56.
    • (1983) Curr Top Microbiol Immunol , vol.102 , pp. 1-56
    • Loos, M.1
  • 44
    • 0019435320 scopus 로고
    • Identification of types of cells in human peripheral blood that bind C1q
    • Tenner AJ, Cooper NR. Identification of types of cells in human peripheral blood that bind C1q. J Immunol. 1981;126:1174-9.
    • (1981) J Immunol , vol.126 , pp. 1174-1179
    • Tenner, A.J.1    Cooper, N.R.2
  • 45
    • 0020623499 scopus 로고
    • C1Q receptors on cultured human gingival fibroblasts: Analysis of binding properties
    • Bordin S, Kolb WP, Page RC. C1Q receptors on cultured human gingival fibroblasts: analysis of binding properties. J Immunol. 1983;130:1871-5.
    • (1983) J Immunol , vol.130 , pp. 1871-1875
    • Bordin, S.1    Kolb, W.P.2    Page, R.C.3
  • 47
    • 0030944415 scopus 로고    scopus 로고
    • CDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro
    • Nepomuceno RR, Henschen-Edman AH, Burgess WH, Tenner AJ. cDNA cloning and primary structure analysis of C1qR(P), the human C1q/MBL/SPA receptor that mediates enhanced phagocytosis in vitro. Immunity. 1997;6:119-29.
    • (1997) Immunity , vol.6 , pp. 119-129
    • Nepomuceno, R.R.1    Henschen-Edman, A.H.2    Burgess, W.H.3    Tenner, A.J.4
  • 48
    • 0021722951 scopus 로고
    • Identification of the Raji cell membrane-derived C1q inhibitor as a receptor for human C1q. Purification and immunochemical characterization
    • Ghebrehiwet B, Silvestri L, McDevitt C. Identification of the Raji cell membrane-derived C1q inhibitor as a receptor for human C1q. Purification and immunochemical characterization. J Exp Med. 1984;160:1375-89.
    • (1984) J Exp Med , vol.160 , pp. 1375-1389
    • Ghebrehiwet, B.1    Silvestri, L.2    McDevitt, C.3
  • 50
    • 0036086544 scopus 로고    scopus 로고
    • Differential activation of human and guinea pig complement by pentameric and hexameric IgM
    • Collins C, Tsui FW, Shulman MJ. Differential activation of human and guinea pig complement by pentameric and hexameric IgM. Eur J Immunol. 2002;32:1802-10.
    • (2002) Eur J Immunol , vol.32 , pp. 1802-1810
    • Collins, C.1    Tsui, F.W.2    Shulman, M.J.3
  • 51
    • 0035869290 scopus 로고    scopus 로고
    • Topology and structure of the C1q-binding site on C-reactive protein
    • Agrawal A, Shrive AK, Greenhough TJ, Volanakis JE. Topology and structure of the C1q-binding site on C-reactive protein. J Immunol. 2001;166:3998-4004.
    • (2001) J Immunol , vol.166 , pp. 3998-4004
    • Agrawal, A.1    Shrive, A.K.2    Greenhough, T.J.3    Volanakis, J.E.4
  • 52
    • 10144250991 scopus 로고    scopus 로고
    • Binding of complement proteins C1q and C4bp to serum amyloid P component (SAP) in solid contra liquid phase
    • Sorensen IJ, Nielsen EH, Andersen O, Danielsen B, Svehag SE. Binding of complement proteins C1q and C4bp to serum amyloid P component (SAP) in solid contra liquid phase. Scand J Immunol. 1996;44:401-7.
    • (1996) Scand J Immunol , vol.44 , pp. 401-407
    • Sorensen, I.J.1    Nielsen, E.H.2    Andersen, O.3    Danielsen, B.4    Svehag, S.E.5
  • 53
    • 0026463907 scopus 로고
    • The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex
    • Krumdieck R, Hook M, Rosenberg LC, Volanakis JE. The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex. J Immunol. 1992;149:3695-701.
    • (1992) J Immunol , vol.149 , pp. 3695-3701
    • Krumdieck, R.1    Hook, M.2    Rosenberg, L.C.3    Volanakis, J.E.4
  • 54
    • 0027323898 scopus 로고
    • Role of complement component C1q in phagocytosis of Listeria monocytogenes by murine macrophage-like cell lines
    • Alvarez-Dominguez C, Carrasco-Marin E, Leyva-Cobian F. Role of complement component C1q in phagocytosis of Listeria monocytogenes by murine macrophage-like cell lines. Infect Immun. 1993;61:3664-72.
    • (1993) Infect Immun , vol.61 , pp. 3664-3672
    • Alvarez-Dominguez, C.1    Carrasco-Marin, E.2    Leyva-Cobian, F.3
  • 55
    • 0027411542 scopus 로고
    • C1q binding and activation of the complement classical pathway by Klebsiella pneumoniae outer membrane proteins
    • Alberti S, Marques G, Camprubi S, Merino S, Tomas JM, Vivanco F, Benedi VJ. C1q binding and activation of the complement classical pathway by Klebsiella pneumoniae outer membrane proteins. Infect Immun. 1993;61:852-60.
    • (1993) Infect Immun , vol.61 , pp. 852-860
    • Alberti, S.1    Marques, G.2    Camprubi, S.3    Merino, S.4    Tomas, J.M.5    Vivanco, F.6    Benedi, V.J.7
  • 56
    • 0028877890 scopus 로고
    • Solid-phase C1q-directed bacterial capture followed by PCR for detection of Chlamydia trachomatis in clinical specimens
    • Herbrink P, van den Munckhof HA, Niesters HG, Goessens WH, Stolz E, Quint WG. Solid-phase C1q-directed bacterial capture followed by PCR for detection of Chlamydia trachomatis in clinical specimens. J Clin Microbiol. 1995;33:283-6.
    • (1995) J Clin Microbiol , vol.33 , pp. 283-286
    • Herbrink, P.1    Van Den Munckhof, H.A.2    Niesters, H.G.3    Goessens, W.H.4    Stolz, E.5    Quint, W.G.6
  • 58
    • 0029417189 scopus 로고
    • Multivalent binding of complement protein C1Q to the amyloid beta-peptide (A beta) promotes the nucleation phase of a beta aggregation
    • Webster S, Glabe C, Rogers J. Multivalent binding of complement protein C1Q to the amyloid beta-peptide (A beta) promotes the nucleation phase of A beta aggregation. Biochem Biophys Res Commun. 1995;217:869-75.
    • (1995) Biochem Biophys Res Commun , vol.217 , pp. 869-875
    • Webster, S.1    Glabe, C.2    Rogers, J.3
  • 59
    • 0035284867 scopus 로고    scopus 로고
    • The globular heads of C1q specifically recognize surface blebs of apoptotic vascular endothelial cells
    • Navratil JS, Watkins SC, Wisnieski JJ, Ahearn JM. The globular heads of C1q specifically recognize surface blebs of apoptotic vascular endothelial cells. J Immunol. 2001;166:3231-9.
    • (2001) J Immunol , vol.166 , pp. 3231-3239
    • Navratil, J.S.1    Watkins, S.C.2    Wisnieski, J.J.3    Ahearn, J.M.4
  • 60
    • 0034613686 scopus 로고    scopus 로고
    • C-Reactive protein binds to apoptotic cells, protects the cells from assembly of the terminal complement components, and sustains an antiinflammatory innate immune response: Implications for systemic autoimmunity
    • Gershov D, Kim S, Brot N, Elkon KB. C-Reactive protein binds to apoptotic cells, protects the cells from assembly of the terminal complement components, and sustains an antiinflammatory innate immune response: implications for systemic autoimmunity. J Exp Med. 2000;192:1353-64.
    • (2000) J Exp Med , vol.192 , pp. 1353-1364
    • Gershov, D.1    Kim, S.2    Brot, N.3    Elkon, K.B.4
  • 61
    • 23044444891 scopus 로고    scopus 로고
    • C-reactive protein does not opsonize early apoptotic human neutrophils, but binds only membrane-permeable late apoptotic cells and has no effect on their phagocytosis by macrophages
    • Hart SP, Alexander KM, Maccall SM, Dransfield I. C-reactive protein does not opsonize early apoptotic human neutrophils, but binds only membrane-permeable late apoptotic cells and has no effect on their phagocytosis by macrophages. J Inflamm (Lond). 2005;2:5.
    • (2005) J Inflamm (Lond) , vol.2 , pp. 5
    • Hart, S.P.1    Alexander, K.M.2    Maccall, S.M.3    Dransfield, I.4
  • 63
    • 0032055226 scopus 로고    scopus 로고
    • The multiligand-binding protein gC1qR, putative C1q receptor, is a mitochondrial protein
    • Dedio J, Jahnen-Dechent W, Bachmann M, Muller-Esterl W. The multiligand-binding protein gC1qR, putative C1q receptor, is a mitochondrial protein. J Immunol. 1998;160:3534-42.
    • (1998) J Immunol , vol.160 , pp. 3534-3542
    • Dedio, J.1    Jahnen-Dechent, W.2    Bachmann, M.3    Muller-Esterl, W.4
  • 64
    • 0027170227 scopus 로고
    • Activation of the classical pathway of complement by binding of bovine lactoferrin to unencapsulated Streptococcus agalactiae
    • Rainard P. Activation of the classical pathway of complement by binding of bovine lactoferrin to unencapsulated Streptococcus agalactiae. Immunology. 1993;79:648-52.
    • (1993) Immunology , vol.79 , pp. 648-652
    • Rainard, P.1
  • 65
    • 0031065202 scopus 로고    scopus 로고
    • Secreted chondroitin sulfate proteoglycan of human B cell lines binds to the complement protein C1q and inhibits complex formation of C1
    • Kirschfink M, Blase L, Engelmann S, Schwartz-Albiez R. Secreted chondroitin sulfate proteoglycan of human B cell lines binds to the complement protein C1q and inhibits complex formation of C1. J Immunol. 1997;158:1324-31.
    • (1997) J Immunol , vol.158 , pp. 1324-1331
    • Kirschfink, M.1    Blase, L.2    Engelmann, S.3    Schwartz-Albiez, R.4
  • 66
    • 0032510463 scopus 로고    scopus 로고
    • The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor
    • Shapiro L, Scherer PE. The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor. Curr Biol. 1998;8:335-8.
    • (1998) Curr Biol , vol.8 , pp. 335-338
    • Shapiro, L.1    Scherer, P.E.2
  • 69
    • 0027792063 scopus 로고
    • Collectin receptor (C1q receptor): Structure and function
    • Malhotra R. Collectin receptor (C1q receptor): structure and function. Behring Inst Mitt. 1993:254-61.
    • (1993) Behring Inst Mitt , pp. 254-261
    • Malhotra, R.1
  • 71
    • 0035903289 scopus 로고    scopus 로고
    • C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells
    • Ogden CA, deCathelineau A, Hoffmann PR, Bratton D, Ghebrehiwet B, Fadok VA, Henson PM. C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J Exp Med. 2001;194:781-95.
    • (2001) J Exp Med , vol.194 , pp. 781-795
    • Ogden, C.A.1    DeCathelineau, A.2    Hoffmann, P.R.3    Bratton, D.4    Ghebrehiwet, B.5    Fadok, V.A.6    Henson, P.M.7
  • 72
    • 0038756766 scopus 로고    scopus 로고
    • Calreticulin is at the surface of circulating neutrophils and uses CD59 as an adaptor molecule
    • Ghiran I, Klickstein LB, Nicholson-Weller A. Calreticulin is at the surface of circulating neutrophils and uses CD59 as an adaptor molecule. J Biol Chem. 2003;278:21024-31.
    • (2003) J Biol Chem , vol.278 , pp. 21024-21031
    • Ghiran, I.1    Klickstein, L.B.2    Nicholson-Weller, A.3
  • 73
    • 0015365755 scopus 로고
    • Interaction of aggregated-globulin with B lymphocytes
    • Dickler HB, Kunkel HG. Interaction of aggregated-globulin with B lymphocytes. J Exp Med. 1972;136:191-6.
    • (1972) J Exp Med , vol.136 , pp. 191-196
    • Dickler, H.B.1    Kunkel, H.G.2
  • 74
    • 0023730105 scopus 로고
    • Characterization of C1q-binding material released from the membranes of Raji and U937 cells by limited proteolysis with trypsin
    • Erdei A, Reid KB. Characterization of C1q-binding material released from the membranes of Raji and U937 cells by limited proteolysis with trypsin. Biochem J. 1988;255:493-9.
    • (1988) Biochem , vol.255 , pp. 493-499
    • Erdei, A.1    Reid, K.B.2
  • 75
    • 0024421499 scopus 로고
    • Chemical and hydrodynamic characterization of the human leucocyte receptor for complement subcomponent C1q
    • Malhotra R, Sim RB. Chemical and hydrodynamic characterization of the human leucocyte receptor for complement subcomponent C1q. Biochem J. 1989;262:625-31.
    • (1989) Biochem J , vol.262 , pp. 625-631
    • Malhotra, R.1    Sim, R.B.2
  • 76
    • 0028282516 scopus 로고
    • Identification of a novel 33-kDa C1q-binding site on human blood platelets
    • Peerschke EI, Reid KB, Ghebrehiwet B. Identification of a novel 33-kDa C1q-binding site on human blood platelets. J Immunol. 1994;152:5896-901.
    • (1994) J Immunol , vol.152 , pp. 5896-5901
    • Peerschke, E.I.1    Reid, K.B.2    Ghebrehiwet, B.3
  • 77
    • 0031689432 scopus 로고    scopus 로고
    • Interaction of C1q and the collectins with the potential receptors calreticulin (cC1qR/collectin receptor) and megalin
    • Sim RB, Moestrup SK, Stuart GR, Lynch NJ, Lu J, Schwaeble WJ, Malhotra R. Interaction of C1q and the collectins with the potential receptors calreticulin (cC1qR/collectin receptor) and megalin. Immunobiology. 1998;199:208-24.
    • (1998) Immunobiology , vol.199 , pp. 208-224
    • Sim, R.B.1    Moestrup, S.K.2    Stuart, G.R.3    Lynch, N.J.4    Lu, J.5    Schwaeble, W.J.6    Malhotra, R.7
  • 78
  • 80
    • 0030930662 scopus 로고    scopus 로고
    • Clinical relevance of calreticulin in systemic lupus erythematosus
    • Eggleton P, Reid KB, Kishore U, Sontheimer RD. Clinical relevance of calreticulin in systemic lupus erythematosus. Lupus. 1997;6:564-71.
    • (1997) Lupus , vol.6 , pp. 564-571
    • Eggleton, P.1    Reid, K.B.2    Kishore, U.3    Sontheimer, R.D.4
  • 81
    • 0032559021 scopus 로고    scopus 로고
    • Evidence that C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin and interferes with complement activation
    • Kovacs H, Campbell ID, Strong P, Johnson S, Ward FJ, Reid KB, Eggleton P. Evidence that C1q binds specifically to CH2-like immunoglobulin gamma motifs present in the autoantigen calreticulin and interferes with complement activation. Biochemistry. 1998;37:17865-74.
    • (1998) Biochemistry , vol.37 , pp. 17865-17874
    • Kovacs, H.1    Campbell, I.D.2    Strong, P.3    Johnson, S.4    Ward, F.J.5    Reid, K.B.6    Eggleton, P.7
  • 83
    • 0032977771 scopus 로고    scopus 로고
    • Pathophysiological roles of calreticulin in autoimmune disease
    • Eggleton P, Llewellyn DH. Pathophysiological roles of calreticulin in autoimmune disease. Scand J Immunol. 1999;49:466-73.
    • (1999) Scand J Immunol , vol.49 , pp. 466-473
    • Eggleton, P.1    Llewellyn, D.H.2
  • 85
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson JR, Ora A, Van PN, Helenius A. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol Biol Cell. 1995;6:1173-84.
    • (1995) Mol Biol Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 87
    • 4644252585 scopus 로고    scopus 로고
    • A polypeptide binding conformation of calreticulin is induced by heat shock, calcium depletion, or by deletion of the C-terminal acidic region
    • Rizvi SM, Mancino L, Thammavongsa V, Cantley RL, Raghavan M. A polypeptide binding conformation of calreticulin is induced by heat shock, calcium depletion, or by deletion of the C-terminal acidic region. Mol Cell. 2004;15:913-23.
    • (2004) Mol Cell , vol.15 , pp. 913-923
    • Rizvi, S.M.1    Mancino, L.2    Thammavongsa, V.3    Cantley, R.L.4    Raghavan, M.5
  • 88
    • 0035279679 scopus 로고    scopus 로고
    • The ins and outs of calreticulin: From the ER lumen to the extracellular space
    • Johnson S, Michalak M, Opas M, Eggleton P. The ins and outs of calreticulin: from the ER lumen to the extracellular space. Trends Cell Biol. 2001;11:122-9.
    • (2001) Trends Cell Biol , vol.11 , pp. 122-129
    • Johnson, S.1    Michalak, M.2    Opas, M.3    Eggleton, P.4
  • 91
    • 0028325931 scopus 로고
    • Cell-surface protein identified on phagocytic cells modulates the C1q-mediated enhancement of phagocytosis
    • Guan E, Robinson SL, Goodman EB, Tenner AJ. Cell-surface protein identified on phagocytic cells modulates the C1q-mediated enhancement of phagocytosis. J Immunol. 1994;152:4005-16.
    • (1994) J Immunol , vol.152 , pp. 4005-4016
    • Guan, E.1    Robinson, S.L.2    Goodman, E.B.3    Tenner, A.J.4
  • 92
    • 0032862491 scopus 로고    scopus 로고
    • Digestion of C1q collagen-like domain with MMPs-1,-2,-3, and -9 further defines the sequence involved in the stimulation of neutrophil superoxide production
    • Ruiz S, Henschen-Edman AH, Nagase H, Tenner AJ. Digestion of C1q collagen-like domain with MMPs-1,-2,-3, and -9 further defines the sequence involved in the stimulation of neutrophil superoxide production. J Leukoc Biol. 1999;66:416-22.
    • (1999) J Leukoc Biol , vol.66 , pp. 416-422
    • Ruiz, S.1    Henschen-Edman, A.H.2    Nagase, H.3    Tenner, A.J.4
  • 93
    • 0028108266 scopus 로고
    • Characterization of the human neutrophil C1q receptor and functional effects of free ligand on activated neutrophils
    • Eggleton P, Ghebrehiwet B, Coburn JP, Sastry KN, Zaner KS, Tauber AI. Characterization of the human neutrophil C1q receptor and functional effects of free ligand on activated neutrophils. Blood. 1994;84:1640-9.
    • (1994) Blood , vol.84 , pp. 1640-1649
    • Eggleton, P.1    Ghebrehiwet, B.2    Coburn, J.P.3    Sastry, K.N.4    Zaner, K.S.5    Tauber, A.I.6
  • 94
    • 0029059577 scopus 로고
    • C1q triggers neutrophil superoxide production by a unique CD18-dependent mechanism
    • Goodman EB, Anderson DC, Tenner AJ. C1q triggers neutrophil superoxide production by a unique CD18-dependent mechanism. J Leukoc Biol. 1995;58:168-76.
    • (1995) J Leukoc Biol , vol.58 , pp. 168-176
    • Goodman, E.B.1    Anderson, D.C.2    Tenner, A.J.3
  • 95
    • 0026689928 scopus 로고
    • Signal transduction mechanisms of C1q-mediated superoxide production. Evidence for the involvement of temporally distinct staurosporine-insensitive and sensitive pathways
    • Goodman EB, Tenner AJ. Signal transduction mechanisms of C1q-mediated superoxide production. Evidence for the involvement of temporally distinct staurosporine-insensitive and sensitive pathways. J Immunol. 1992;148:3920-8.
    • (1992) J Immunol , vol.148 , pp. 3920-3928
    • Goodman, E.B.1    Tenner, A.J.2
  • 96
    • 0037093864 scopus 로고    scopus 로고
    • Human C1qRp is identical with CD93 and the mNI-11 antigen but does not bind C1q
    • McGreal EP, Ikewaki N, Akatsu H, Morgan BP, Gasque P. Human C1qRp is identical with CD93 and the mNI-11 antigen but does not bind C1q. J Immunol. 2002;168:5222-32.
    • (2002) J Immunol , vol.168 , pp. 5222-5232
    • McGreal, E.P.1    Ikewaki, N.2    Akatsu, H.3    Morgan, B.P.4    Gasque, P.5
  • 97
    • 0033558378 scopus 로고    scopus 로고
    • C1qRP is a heavily O-glycosylated cell surface protein involved in the regulation of phagocytic activity
    • Nepomuceno RR, Ruiz S, Park M, Tenner AJ. C1qRP is a heavily O-glycosylated cell surface protein involved in the regulation of phagocytic activity. J Immunol. 1999;162:3583-9.
    • (1999) J Immunol , vol.162 , pp. 3583-3589
    • Nepomuceno, R.R.1    Ruiz, S.2    Park, M.3    Tenner, A.J.4
  • 98
    • 0032519011 scopus 로고    scopus 로고
    • C1qRP, the C1q receptor that enhances phagocytosis, is detected specifically in human cells of myeloid lineage, endothelial cells, and platelets
    • Nepomuceno RR, Tenner AJ. C1qRP, the C1q receptor that enhances phagocytosis, is detected specifically in human cells of myeloid lineage, endothelial cells, and platelets. J Immunol. 1998;160:1929-35.
    • (1998) J Immunol , vol.160 , pp. 1929-1935
    • Nepomuceno, R.R.1    Tenner, A.J.2
  • 99
    • 0025724098 scopus 로고
    • Phagocytic cell molecules that bind the collagen-like region of C1q. Involvement in the C1q-mediated enhancement of phagocytosis
    • Guan EN, Burgess WH, Robinson SL, Goodman EB, McTigue KJ, Tenner AJ. Phagocytic cell molecules that bind the collagen-like region of C1q. Involvement in the C1q-mediated enhancement of phagocytosis. J Biol Chem. 1991;266:20345-55.
    • (1991) J Biol Chem , vol.266 , pp. 20345-20355
    • Guan, E.N.1    Burgess, W.H.2    Robinson, S.L.3    Goodman, E.B.4    McTigue, K.J.5    Tenner, A.J.6
  • 100
    • 0026515407 scopus 로고
    • Molecular cloning of a cDNA encoding CD34, a sialomucin of human hematopoietic stem cells
    • Simmons DL, Satterthwaite AB, Tenen DG, Seed B. Molecular cloning of a cDNA encoding CD34, a sialomucin of human hematopoietic stem cells. J Immunol. 1992;148:267-71.
    • (1992) J Immunol , vol.148 , pp. 267-271
    • Simmons, D.L.1    Satterthwaite, A.B.2    Tenen, D.G.3    Seed, B.4
  • 103
    • 0024600860 scopus 로고
    • An immobile subset of plasma membrane CD11b/CD18 (Mac-1) is involved in phagocytosis of targets recognized by multiple receptors
    • Graham IL, Gresham HD, Brown EJ. An immobile subset of plasma membrane CD11b/CD18 (Mac-1) is involved in phagocytosis of targets recognized by multiple receptors. J Immunol. 1989;142:2352-8.
    • (1989) J Immunol , vol.142 , pp. 2352-2358
    • Graham, I.L.1    Gresham, H.D.2    Brown, E.J.3
  • 108
    • 0016651955 scopus 로고
    • In vitro synthesis of some complement components (C1q, C3 and C4) by lymphoid tissues and circulating leucocytes in man
    • Lai AFRF, van Furth R. In vitro synthesis of some complement components (C1q, C3 and C4) by lymphoid tissues and circulating leucocytes in man. Immunology. 1975;28:359-68.
    • (1975) Immunology , vol.28 , pp. 359-368
    • Lai, A.F.R.F.1    Van Furth, R.2
  • 109
    • 0030986886 scopus 로고    scopus 로고
    • C1Q synthesis by tissue mononuclear phagocytes from normal and from damaged rat liver: Up-regulation by dexamethasone, down-regulation by interferon gamma, and lipopolysaccharide
    • Armbrust T, Nordmann B, Kreissig M, Ramadori G. C1Q synthesis by tissue mononuclear phagocytes from normal and from damaged rat liver: up-regulation by dexamethasone, down-regulation by interferon gamma, and lipopolysaccharide. Hepatology. 1997;26:98-106.
    • (1997) Hepatology , vol.26 , pp. 98-106
    • Armbrust, T.1    Nordmann, B.2    Kreissig, M.3    Ramadori, G.4
  • 110
    • 0037334392 scopus 로고    scopus 로고
    • Maturation-dependent expression of C1q binding proteins on the cell surface of human monocyte-derived dendritic cells
    • Vegh Z, Goyarts EC, Rozengarten K, Mazumder A, Ghebrehiwet B. Maturation-dependent expression of C1q binding proteins on the cell surface of human monocyte-derived dendritic cells. Int Immunopharmacol. 2003;3:39-51.
    • (2003) Int Immunopharmacol , vol.3 , pp. 39-51
    • Vegh, Z.1    Goyarts, E.C.2    Rozengarten, K.3    Mazumder, A.4    Ghebrehiwet, B.5
  • 111
    • 2442650484 scopus 로고    scopus 로고
    • CC1q-R (calreticulin) and gC1q-R/p33: Ubiquitously expressed multi-ligand binding cellular proteins involved in inflammation and infection
    • Ghebrehiwet B, Peerschke EI. cC1q-R (calreticulin) and gC1q-R/p33: ubiquitously expressed multi-ligand binding cellular proteins involved in inflammation and infection. Mol Immunol. 2004;41:173-83.
    • (2004) Mol Immunol , vol.41 , pp. 173-183
    • Ghebrehiwet, B.1    Peerschke, E.I.2
  • 112
    • 0025217193 scopus 로고
    • Inhibitors of C1q biosynthesis suppress activation of murine macrophages for both antibody-independent and antibody-dependent tumor cytotoxicity
    • Leu RW, Zhou AQ, Shannon BJ, Herriott MJ. Inhibitors of C1q biosynthesis suppress activation of murine macrophages for both antibody-independent and antibody-dependent tumor cytotoxicity. J Immunol. 1990;144:2281-6.
    • (1990) J Immunol , vol.144 , pp. 2281-2286
    • Leu, R.W.1    Zhou, A.Q.2    Shannon, B.J.3    Herriott, M.J.4
  • 113
    • 0036747260 scopus 로고    scopus 로고
    • C1q, autoimmunity and apoptosis
    • Botto M, Walport MJ. C1q, autoimmunity and apoptosis. Immunobiology. 2002;205:395-406.
    • (2002) Immunobiology , vol.205 , pp. 395-406
    • Botto, M.1    Walport, M.J.2
  • 114
    • 0036785571 scopus 로고    scopus 로고
    • Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: Calreticulin and CD91 as a common collectin receptor complex
    • Vandivier RW, Ogden CA, Fadok VA, Hoffmann PR, Brown KK, Botto M, Walport MJ, Fisher JH, Henson PM, Greene KE. Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: calreticulin and CD91 as a common collectin receptor complex. J Immunol. 2002;169:3978-86.
    • (2002) J Immunol , vol.169 , pp. 3978-3986
    • Vandivier, R.W.1    Ogden, C.A.2    Fadok, V.A.3    Hoffmann, P.R.4    Brown, K.K.5    Botto, M.6    Walport, M.J.7    Fisher, J.H.8    Henson, P.M.9    Greene, K.E.10
  • 115
    • 14644409746 scopus 로고    scopus 로고
    • CD93 interacts with the PDZ domain-containing adaptor protein GIPC: Implications in the modulation of phagocytosis
    • Bohlson SS, Zhang M, Ortiz CE, Tenner AJ. CD93 interacts with the PDZ domain-containing adaptor protein GIPC: implications in the modulation of phagocytosis. J Leukoc Biol. 2004;77.
    • (2004) J Leukoc Biol , vol.77
    • Bohlson, S.S.1    Zhang, M.2    Ortiz, C.E.3    Tenner, A.J.4
  • 116
    • 0001665337 scopus 로고
    • Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor
    • Herz J, Hamann U, Rogne S, Myklebost O, Gausepohl H, Stanley KK. Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor. EMBO J. 1988;7:4119-27.
    • (1988) EMBO J , vol.7 , pp. 4119-4127
    • Herz, J.1    Hamann, U.2    Rogne, S.3    Myklebost, O.4    Gausepohl, H.5    Stanley, K.K.6
  • 117
    • 0025666455 scopus 로고
    • Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor
    • Kristensen T, Moestrup SK, Gliemann J, Bendtsen L, Sand O, Sottrup-Jensen L. Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor. FEBS Lett. 1990;276:151-5.
    • (1990) FEBS Lett , vol.276 , pp. 151-155
    • Kristensen, T.1    Moestrup, S.K.2    Gliemann, J.3    Bendtsen, L.4    Sand, O.5    Sottrup-Jensen, L.6
  • 118
  • 119
    • 0034836428 scopus 로고    scopus 로고
    • LRP: A multifunctional scavenger and signaling receptor
    • Herz J, Strickland DK. LRP: a multifunctional scavenger and signaling receptor. J Clin Invest. 2001;108:779-84.
    • (2001) J Clin Invest , vol.108 , pp. 779-784
    • Herz, J.1    Strickland, D.K.2
  • 120
    • 0033615548 scopus 로고    scopus 로고
    • The second and fourth cluster of class a cysteine-rich repeats of the low density lipoprotein receptor-related protein share ligand-binding properties
    • Neels JG, van Den Berg BM, Lookene A, Olivecrona G, Pannekoek H, van Zonneveld AJ. The second and fourth cluster of class A cysteine-rich repeats of the low density lipoprotein receptor-related protein share ligand-binding properties. J Biol Chem. 1999;274:31305-11.
    • (1999) J Biol Chem , vol.274 , pp. 31305-31311
    • Neels, J.G.1    Van Den Berg, B.M.2    Lookene, A.3    Olivecrona, G.4    Pannekoek, H.5    Van Zonneveld, A.J.6
  • 121
    • 0032491379 scopus 로고    scopus 로고
    • An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components
    • Springer TA. An extracellular beta-propeller module predicted in lipoprotein and scavenger receptors, tyrosine kinases, epidermal growth factor precursor, and extracellular matrix components. J Mol Biol. 1998;283:837-62.
    • (1998) J Mol Biol , vol.283 , pp. 837-862
    • Springer, T.A.1
  • 123
    • 0026731852 scopus 로고
    • Distribution of the alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein in human tissues
    • Moestrup SK, Gliemann J, Pallesen G. Distribution of the alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein in human tissues. Cell Tissue Res. 1992;269:375-82.
    • (1992) Cell Tissue Res , vol.269 , pp. 375-382
    • Moestrup, S.K.1    Gliemann, J.2    Pallesen, G.3
  • 124
    • 0026690341 scopus 로고
    • The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin a
    • Kounnas MZ, Morris RE, Thompson MR, FitzGerald DJ, Strickland DK, Saelinger CB. The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A. J Biol Chem. 1992;267:12420-3.
    • (1992) J Biol Chem , vol.267 , pp. 12420-12423
    • Kounnas, M.Z.1    Morris, R.E.2    Thompson, M.R.3    Fitzgerald, D.J.4    Strickland, D.K.5    Saelinger, C.B.6
  • 125
    • 0025080835 scopus 로고
    • Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor
    • Strickland DK, Ashcom JD, Williams S, Burgess WH, Migliorini M, Argraves WS. Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor. J Biol Chem. 1990;265:17401-4.
    • (1990) J Biol Chem , vol.265 , pp. 17401-17404
    • Strickland, D.K.1    Ashcom, J.D.2    Williams, S.3    Burgess, W.H.4    Migliorini, M.5    Argraves, W.S.6
  • 126
    • 0030998766 scopus 로고    scopus 로고
    • Interaction of apo E-containing lipoproteins with the LDL receptor-related protein LRP
    • Kuchenhoff A, Harrach-Ruprecht B, Robenek H. Interaction of apo E-containing lipoproteins with the LDL receptor-related protein LRP. Am J Physiol. 1997;272:C369-82.
    • (1997) Am J Physiol , vol.272
    • Kuchenhoff, A.1    Harrach-Ruprecht, B.2    Robenek, H.3
  • 127
    • 0035070198 scopus 로고    scopus 로고
    • CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin
    • Basu S, Binder RJ, Ramalingam T, Srivastava PK. CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity. 2001;14:303-13.
    • (2001) Immunity , vol.14 , pp. 303-313
    • Basu, S.1    Binder, R.J.2    Ramalingam, T.3    Srivastava, P.K.4
  • 128
    • 0034931306 scopus 로고    scopus 로고
    • Links between complement deficiency and apoptosis
    • Botto M. Links between complement deficiency and apoptosis. Arthritis Res. 2001;3:207-10.
    • (2001) Arthritis Res , vol.3 , pp. 207-210
    • Botto, M.1
  • 133
    • 0033546416 scopus 로고    scopus 로고
    • Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules
    • Arosa FA, de Jesus O, Porto G, Carmo AM, de Sousa M. Calreticulin is expressed on the cell surface of activated human peripheral blood T lymphocytes in association with major histocompatibility complex class I molecules. J Biol Chem. 1999;274:16917-22.
    • (1999) J Biol Chem , vol.274 , pp. 16917-16922
    • Arosa, F.A.1    De Jesus, O.2    Porto, G.3    Carmo, A.M.4    De Sousa, M.5
  • 135
    • 0035969239 scopus 로고    scopus 로고
    • Tethering and tickling: A new role for the phosphatidylserine receptor
    • Somersan S, Bhardwaj N. Tethering and tickling: a new role for the phosphatidylserine receptor. J Cell Biol. 2001;155:501-4.
    • (2001) J Cell Biol , vol.155 , pp. 501-504
    • Somersan, S.1    Bhardwaj, N.2
  • 136
    • 0141918823 scopus 로고    scopus 로고
    • By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation
    • Gardai SJ, Xiao YQ, Dickinson M, Nick JA, Voelker DR, Greene KE, Henson PM. By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation. Cell. 2003;115:13-23.
    • (2003) Cell , vol.115 , pp. 13-23
    • Gardai, S.J.1    Xiao, Y.Q.2    Dickinson, M.3    Nick, J.A.4    Voelker, D.R.5    Greene, K.E.6    Henson, P.M.7
  • 139
    • 0028358392 scopus 로고
    • Molecular dissection of ligand binding sites on the low density lipoprotein receptor-related protein
    • Willnow TE, Orth K, Herz J. Molecular dissection of ligand binding sites on the low density lipoprotein receptor-related protein. J Biol Chem. 1994;269:15827-32.
    • (1994) J Biol Chem , vol.269 , pp. 15827-15832
    • Willnow, T.E.1    Orth, K.2    Herz, J.3
  • 140
    • 0030723177 scopus 로고    scopus 로고
    • C1 inhibitor-C1s complexes are internalized and degraded by the low density lipoprotein receptor-related protein
    • Storm D, Herz J, Trinder P, Loos M. C1 inhibitor-C1s complexes are internalized and degraded by the low density lipoprotein receptor-related protein. J Biol Chem. 1997;272:31043-50.
    • (1997) J Biol Chem , vol.272 , pp. 31043-31050
    • Storm, D.1    Herz, J.2    Trinder, P.3    Loos, M.4
  • 141
    • 0037169492 scopus 로고    scopus 로고
    • The alpha-chains of C4b-binding protein mediate complex formation with low density lipoprotein receptor-related protein
    • Western E, Denis CV, Bouma BN, Lenting PJ. The alpha-chains of C4b-binding protein mediate complex formation with low density lipoprotein receptor-related protein. J Biol Chem. 2002;277:2511-6.
    • (2002) J Biol Chem , vol.277 , pp. 2511-2516
    • Western, E.1    Denis, C.V.2    Bouma, B.N.3    Lenting, P.J.4
  • 142
    • 0033621464 scopus 로고    scopus 로고
    • Metabolism of activated complement component C3 is mediated by the low density lipoprotein receptor-related protein/alpha(2)-macroglobulin receptor
    • Meilinger M, Gschwentner C, Burger I, Haumer M, Wahrmann M, Szollar L, Nimpf J, Huettinger M. Metabolism of activated complement component C3 is mediated by the low density lipoprotein receptor-related protein/alpha(2)- macroglobulin receptor. J Biol Chem. 1999;274:38091-6.
    • (1999) J Biol Chem , vol.274 , pp. 38091-38096
    • Meilinger, M.1    Gschwentner, C.2    Burger, I.3    Haumer, M.4    Wahrmann, M.5    Szollar, L.6    Nimpf, J.7    Huettinger, M.8
  • 143
    • 6344248557 scopus 로고    scopus 로고
    • Biological effects of C1 inhibitor
    • Davis AE III. Biological effects of C1 inhibitor. Drug News Perspect. 2004;17:439-46.
    • (2004) Drug News Perspect , vol.17 , pp. 439-446
    • Davis III, A.E.1
  • 144
    • 0034530108 scopus 로고    scopus 로고
    • Interaction between factor VIII and LDL receptor-related protein. Modulation of coagulation?
    • Neels JG, Bovenschen N, van Zonneveld AJ, Lenting PJ. Interaction between factor VIII and LDL receptor-related protein. Modulation of coagulation? Trends Cardiovasc Med. 2000;10:8-14.
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 8-14
    • Neels, J.G.1    Bovenschen, N.2    Van Zonneveld, A.J.3    Lenting, P.J.4
  • 145
    • 0035805530 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein modulates levels of matrix metalloproteinase 9 (MMP-9) by mediating its cellular catabolism
    • Hahn-Dantona E, Ruiz JF, Bornstein P, Strickland DK. The low density lipoprotein receptor-related protein modulates levels of matrix metalloproteinase 9 (MMP-9) by mediating its cellular catabolism. J Biol Chem. 2001;276:15498-503.
    • (2001) J Biol Chem , vol.276 , pp. 15498-15503
    • Hahn-Dantona, E.1    Ruiz, J.F.2    Bornstein, P.3    Strickland, D.K.4
  • 147
    • 15244352841 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase (MMP) activity by the low-density lipoprotein receptor-related protein (LRP). A new function for an "old friend"
    • Emonard H, Bellon G, de Diesbach P, Mettlen M, Hornebeck W, Courtoy PJ. Regulation of matrix metalloproteinase (MMP) activity by the low-density lipoprotein receptor-related protein (LRP). A new function for an "old friend". Biochimie. 2005;87:369-76.
    • (2005) Biochimie , vol.87 , pp. 369-376
    • Emonard, H.1    Bellon, G.2    De Diesbach, P.3    Mettlen, M.4    Hornebeck, W.5    Courtoy, P.J.6
  • 149
    • 13844292108 scopus 로고    scopus 로고
    • Internalization but not binding of thrombospondin-1 to low density lipoprotein receptor-related protein-1 requires heparan sulfate proteoglycans
    • Wang S, Herndon ME, Ranganathan S, Godyna S, Lawler J, Argraves WS, Liau G. Internalization but not binding of thrombospondin-1 to low density lipoprotein receptor-related protein-1 requires heparan sulfate proteoglycans. J Cell Biochem. 2004;91:766-76.
    • (2004) J Cell Biochem , vol.91 , pp. 766-776
    • Wang, S.1    Herndon, M.E.2    Ranganathan, S.3    Godyna, S.4    Lawler, J.5    Argraves, W.S.6    Liau, G.7
  • 150
    • 0034529953 scopus 로고    scopus 로고
    • Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands
    • Liu Y, Jones M, Hingtgen CM, Bu G, Laribee N, Tanzi RE, Moir RD, Nath A, He JJ. Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands. Nat Med. 2000;6:1380-7.
    • (2000) Nat Med , vol.6 , pp. 1380-1387
    • Liu, Y.1    Jones, M.2    Hingtgen, C.M.3    Bu, G.4    Laribee, N.5    Tanzi, R.E.6    Moir, R.D.7    Nath, A.8    He, J.J.9
  • 151
    • 0346749512 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein modulates protease activity in the brain by mediating the cellular internalization of both neuroserpin and neuroserpin-tissue-type plasminogen activator complexes
    • Makarova A, Mikhailenko I, Bugge TH, List K, Lawrence DA, Strickland DK. The low density lipoprotein receptor-related protein modulates protease activity in the brain by mediating the cellular internalization of both neuroserpin and neuroserpin-tissue-type plasminogen activator complexes. J Biol Chem. 2003;278:50250-8.
    • (2003) J Biol Chem , vol.278 , pp. 50250-50258
    • Makarova, A.1    Mikhailenko, I.2    Bugge, T.H.3    List, K.4    Lawrence, D.A.5    Strickland, D.K.6
  • 152
    • 0034528960 scopus 로고    scopus 로고
    • SERPIN regulation of factor XIa. The novel observation that protease nexin 1 in the presence of heparin is a more potent inhibitor of factor XIa than C1 inhibitor
    • Knauer DJ, Majumdar D, Fong PC, Knauer MF. SERPIN regulation of factor XIa. The novel observation that protease nexin 1 in the presence of heparin is a more potent inhibitor of factor XIa than C1 inhibitor. J Biol Chem. 2000;275:37340-6.
    • (2000) J Biol Chem , vol.275 , pp. 37340-37346
    • Knauer, D.J.1    Majumdar, D.2    Fong, P.C.3    Knauer, M.F.4
  • 153
    • 15544373100 scopus 로고    scopus 로고
    • Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells
    • Theriault JR, Mambula SS, Sawamura T, Stevenson MA, Calderwood SK. Extracellular HSP70 binding to surface receptors present on antigen presenting cells and endothelial/epithelial cells. FEBS Lett. 2005;579:1951-60.
    • (2005) FEBS Lett , vol.579 , pp. 1951-1960
    • Theriault, J.R.1    Mambula, S.S.2    Sawamura, T.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 155
    • 8744266243 scopus 로고    scopus 로고
    • Efficient transfer of receptor-associated protein (RAP) across the blood-brain barrier
    • Pan W, Kasrin AJ, Zankel TC, van Kerkhof P, Terasaki T, Bu G. Efficient transfer of receptor-associated protein (RAP) across the blood-brain barrier. J Cell Sci. 2004;117:5071-8.
    • (2004) J Cell Sci , vol.117 , pp. 5071-5078
    • Pan, W.1    Kasrin, A.J.2    Zankel, T.C.3    Van Kerkhof, P.4    Terasaki, T.5    Bu, G.6
  • 156
    • 0035292695 scopus 로고    scopus 로고
    • Structural, biochemical and signaling properties of the low-density lipoprotein receptor gene family
    • Hussain MM. Structural, biochemical and signaling properties of the low-density lipoprotein receptor gene family. Front Biosci. 2001;6:D417-28.
    • (2001) Front Biosci , vol.6
    • Hussain, M.M.1
  • 157
    • 0142103374 scopus 로고    scopus 로고
    • The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65
    • Kinoshita A, Shah T, Tangredi MM, Strickland DK, Hyman BT. The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65. J Biol Chem. 2003;278:41182-8.
    • (2003) J Biol Chem , vol.278 , pp. 41182-41188
    • Kinoshita, A.1    Shah, T.2    Tangredi, M.M.3    Strickland, D.K.4    Hyman, B.T.5
  • 158
    • 0027645625 scopus 로고
    • Recent advances in lipoprotein metabolism
    • Miyazaki A, Horiuchi S. [Recent advances in lipoprotein metabolism]. Nippon Rinsho. 1993;51:1954-60.
    • (1993) Nippon Rinsho , vol.51 , pp. 1954-1960
    • Miyazaki, A.1    Horiuchi, S.2
  • 159
    • 0027064666 scopus 로고
    • Modulation of the low-density-lipoprotein-receptor-related protein and its relevance to chylomicron-remnant metabolism
    • Szanto A, Balasubramaniam S, Roach PD, Nestel PJ. Modulation of the low-density-lipoprotein-receptor-related protein and its relevance to chylomicron-remnant metabolism. Biochem J. 1992;288(Pt 3):791-4.
    • (1992) Biochem J , vol.288 , Issue.PART 3 , pp. 791-794
    • Szanto, A.1    Balasubramaniam, S.2    Roach, P.D.3    Nestel, P.J.4
  • 161
    • 0029385285 scopus 로고
    • Targeting plant toxins to the urokinase and alpha 2-macroglobulin receptors
    • Cavallaro U, Soria MR. Targeting plant toxins to the urokinase and alpha 2-macroglobulin receptors. Semin Cancer Biol. 1995;6:269-78.
    • (1995) Semin Cancer Biol , vol.6 , pp. 269-278
    • Cavallaro, U.1    Soria, M.R.2
  • 163
    • 0033569725 scopus 로고    scopus 로고
    • Collagenase-3 binds to a specific receptor and requires the low density lipoprotein receptor-related protein for internalization
    • Barmina OY, Walling HW, Fiacco GJ, Freije JM, Lopez-Otin C, Jeffrey JJ, Partridge NC. Collagenase-3 binds to a specific receptor and requires the low density lipoprotein receptor-related protein for internalization. J Biol Chem. 1999;274:30087-93.
    • (1999) J Biol Chem , vol.274 , pp. 30087-30093
    • Barmina, O.Y.1    Walling, H.W.2    Fiacco, G.J.3    Freije, J.M.4    Lopez-Otin, C.5    Jeffrey, J.J.6    Partridge, N.C.7
  • 165
    • 0242322487 scopus 로고    scopus 로고
    • Modulation of the LDL receptor and LRP levels by HIV protease inhibitors
    • Tran H, Robinson S, Mikhailenko I, Strickland DK. Modulation of the LDL receptor and LRP levels by HIV protease inhibitors. J Lipid Res. 2003;44:1859-69.
    • (2003) J Lipid Res , vol.44 , pp. 1859-1869
    • Tran, H.1    Robinson, S.2    Mikhailenko, I.3    Strickland, D.K.4
  • 167
    • 0642366645 scopus 로고    scopus 로고
    • Association between low-density lipoprotein receptor-related protein gene, butyrylcholinesterase gene and Alzheimer's disease in Chinese
    • Bi S, Zhang Y, Wu J, Wang D, Zhao Q. Association between low-density lipoprotein receptor-related protein gene, butyrylcholinesterase gene and Alzheimer's disease in Chinese. Chin Med Sci J. 2001;16:71-5.
    • (2001) Chin Med Sci J , vol.16 , pp. 71-75
    • Bi, S.1    Zhang, Y.2    Wu, J.3    Wang, D.4    Zhao, Q.5
  • 168
    • 0037044693 scopus 로고    scopus 로고
    • Low-density lipoprotein receptor-related protein 8 (apolipoprotein e receptor 2) gene polymorphisms in Alzheimer's disease
    • Ma SL, Ng HK, Baum L, Pang JC, Chiu HF, Woo J, Tang NL, Lam LC. Low-density lipoprotein receptor-related protein 8 (apolipoprotein E receptor 2) gene polymorphisms in Alzheimer's disease. Neurosci Lett. 2002;332:216-8.
    • (2002) Neurosci Lett , vol.332 , pp. 216-218
    • Ma, S.L.1    Ng, H.K.2    Baum, L.3    Pang, J.C.4    Chiu, H.F.5    Woo, J.6    Tang, N.L.7    Lam, L.C.8
  • 170
    • 0034730766 scopus 로고    scopus 로고
    • A protective role of the low density lipoprotein receptor-related protein against amyloid beta-protein toxicity
    • Van Uden E, Sagara Y, Van Uden J, Orlando R, Mallory M, Rockenstein E, Masliah E. A protective role of the low density lipoprotein receptor-related protein against amyloid beta-protein toxicity. J Biol Chem. 2000;275:30525-30.
    • (2000) J Biol Chem , vol.275 , pp. 30525-30530
    • Van Uden, E.1    Sagara, Y.2    Van Uden, J.3    Orlando, R.4    Mallory, M.5    Rockenstein, E.6    Masliah, E.7
  • 171
    • 0033771902 scopus 로고    scopus 로고
    • CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in Caenorhabditis elegans
    • Reddien PW, Horvitz HR. CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in Caenorhabditis elegans. Nat Cell Biol. 2000;2:131-6.
    • (2000) Nat Cell Biol , vol.2 , pp. 131-136
    • Reddien, P.W.1    Horvitz, H.R.2
  • 172
    • 0032473981 scopus 로고    scopus 로고
    • C. elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK180
    • Wu YC, Horvitz HR. C. elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK180. Nature. 1998;392:501-4.
    • (1998) Nature , vol.392 , pp. 501-504
    • Wu, Y.C.1    Horvitz, H.R.2
  • 173
    • 0032511145 scopus 로고    scopus 로고
    • The C. elegans cell corpse engulfment gene ced-7 encodes a protein similar to ABC transporters
    • Wu YC, Horvitz HR. The C. elegans cell corpse engulfment gene ced-7 encodes a protein similar to ABC transporters. Cell. 1998;93:951-60.
    • (1998) Cell , vol.93 , pp. 951-960
    • Wu, Y.C.1    Horvitz, H.R.2
  • 174
    • 0032511234 scopus 로고    scopus 로고
    • Candidate adaptor protein CED-6 promotes the engulfment of apoptotic cells in C. elegans
    • Liu QA, Hengartner MO. Candidate adaptor protein CED-6 promotes the engulfment of apoptotic cells in C. elegans. Cell. 1998;93:961-72.
    • (1998) Cell , vol.93 , pp. 961-972
    • Liu, Q.A.1    Hengartner, M.O.2
  • 175
    • 0037023693 scopus 로고    scopus 로고
    • Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP)
    • Su HP, Nakada-Tsukui K, Tosello-Trampont AC, Li Y, Bu G, Henson PM, Ravichandran KS. Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP). J Biol Chem. 2002;277:11772-9.
    • (2002) J Biol Chem , vol.277 , pp. 11772-11779
    • Su, H.P.1    Nakada-Tsukui, K.2    Tosello-Trampont, A.C.3    Li, Y.4    Bu, G.5    Henson, P.M.6    Ravichandran, K.S.7
  • 176
    • 0035900697 scopus 로고    scopus 로고
    • Identification of a site on mannan-binding lectin critical for enhancement of phagocytosis
    • Arora M, Munoz E, Tenner AJ. Identification of a site on mannan-binding lectin critical for enhancement of phagocytosis. J Biol Chem. 2001;276:43087-94.
    • (2001) J Biol Chem , vol.276 , pp. 43087-43094
    • Arora, M.1    Munoz, E.2    Tenner, A.J.3


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