메뉴 건너뛰기




Volumn 9, Issue 4, 2006, Pages 265-275

Conglutinin, CL-43 and CL-46 - Three bovine collectins

Author keywords

Biological activity; CL 43 and CL 46; Conglutinin; Structure

Indexed keywords

COLLECTIN; COLLECTIN 43 PROTEIN, BOVINE; COLLECTIN-43 PROTEIN, BOVINE; CONGLUTININ; SERUM GLOBULIN;

EID: 33845714303     PISSN: 15051773     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (17)

References (100)
  • 1
    • 0026098401 scopus 로고
    • Conglutinin binds the HIV-1 envelope glycoprotein gp 160 and inhibits its interaction with cell membrane CD4
    • Andersen O, Sorensen AM, Svehag SE, Fenouillet E (1991) Conglutinin binds the HIV-1 envelope glycoprotein gp 160 and inhibits its interaction with cell membrane CD4. Scand J Immunol 33: 81-88.
    • (1991) Scand J Immunol , vol.33 , pp. 81-88
    • Andersen, O.1    Sorensen, A.M.2    Svehag, S.E.3    Fenouillet, E.4
  • 3
    • 0026704058 scopus 로고
    • Purification, subunit characterization and ultrastructure of three soluble bovine lectins: Conglutinin, mannose-binding protein and the pentraxin serum amyloid P-component
    • Andersen O, Friis P, Holm Nielsen E, Vilsgaard K, Leslie RG, Svehag SE (1992b)Purification, subunit characterization and ultrastructure of three soluble bovine lectins: conglutinin, mannose-binding protein and the pentraxin serum amyloid P-component. Scand J Immunol 36: 131-141.
    • (1992) Scand J Immunol , vol.36 , pp. 131-141
    • Andersen, O.1    Friis, P.2    Holm Nielsen, E.3    Vilsgaard, K.4    Leslie, R.G.5    Svehag, S.E.6
  • 4
    • 0021239018 scopus 로고
    • Conglutinin microtiter plate ELISA system for detecting circulating immune complexes
    • Araga S, Irie H, Takahashi K (1984) Conglutinin microtiter plate ELISA system for detecting circulating immune complexes. J Neuroimmunol 6: 161-168.
    • (1984) J Neuroimmunol , vol.6 , pp. 161-168
    • Araga, S.1    Irie, H.2    Takahashi, K.3
  • 5
    • 0035900697 scopus 로고    scopus 로고
    • Identification of a site on mannan-binding lectin critical for enhancement of phagocytosis
    • Arora M, Munoz E, Tenner AJ (2001) Identification of a site on mannan-binding lectin critical for enhancement of phagocytosis. J Biol Chem 16;276: 43087-43094.
    • (2001) J Biol Chem , vol.16 , Issue.276 , pp. 43087-43094
    • Arora, M.1    Munoz, E.2    Tenner, A.J.3
  • 6
    • 4644334684 scopus 로고    scopus 로고
    • Enhanced lung injury and delayed clearance of Pneumocystis carinii in surfactant protein A-deficient mice: Attenuation of cytokine responses and reactive oxygen-nitrogen species
    • Atochina EN, Beck JM, Preston AM, Haczku A, Tomer Y, Scanlon ST, Fusaro T, Casey J, Hawgood S, Gow AJ, Beers MF (2004) Enhanced lung injury and delayed clearance of Pneumocystis carinii in surfactant protein A-deficient mice: attenuation of cytokine responses and reactive oxygen-nitrogen species. Infect Immun 72: 6002-6011.
    • (2004) Infect Immun , vol.72 , pp. 6002-6011
    • Atochina, E.N.1    Beck, J.M.2    Preston, A.M.3    Haczku, A.4    Tomer, Y.5    Scanlon, S.T.6    Fusaro, T.7    Casey, J.8    Hawgood, S.9    Gow, A.J.10    Beers, M.F.11
  • 7
    • 0023111156 scopus 로고
    • Modulation of FcR function by complement: Subcomponent C1q enhances the phagocytosis of IgG-opsonized targets by human monocytes and culture-derived macrophages
    • Bobak DA, Gaither TA, Frank MM, Tenner AJ (1987) Modulation of FcR function by complement: subcomponent C1q enhances the phagocytosis of IgG-opsonized targets by human monocytes and culture-derived macrophages. J Immunol 15; 138: 1150-1156.
    • (1987) J Immunol , vol.15 , Issue.138 , pp. 1150-1156
    • Bobak, D.A.1    Gaither, T.A.2    Frank, M.M.3    Tenner, A.J.4
  • 9
    • 0019409404 scopus 로고
    • Antigen-specific detection of soluble immune complexes in conglutinin-binding assays
    • D'Amelio R, Brighouse G, Barnet M, Lambert PH (1981) Antigen-specific detection of soluble immune complexes in conglutinin-binding assays. Clin Exp Immunol 45: 283-289.
    • (1981) Clin Exp Immunol , vol.45 , pp. 283-289
    • D'Amelio, R.1    Brighouse, G.2    Barnet, M.3    Lambert, P.H.4
  • 10
    • 0029936341 scopus 로고    scopus 로고
    • Recombinant bovine conglutinin, lacking the N-terminal and collagenous domains, has less conglutination activity but is able to inhibit haemagglutination by influenza A virus
    • Eda S, Suzuki Y, Kase T, Kawai T, Ohtani K, Sakamoto T, Kurimura T, Wakamiya N (1996) Recombinant bovine conglutinin, lacking the N-terminal and collagenous domains, has less conglutination activity but is able to inhibit haemagglutination by influenza A virus. Biochem J 316: 43-48.
    • (1996) Biochem J , vol.316 , pp. 43-48
    • Eda, S.1    Suzuki, Y.2    Kase, T.3    Kawai, T.4    Ohtani, K.5    Sakamoto, T.6    Kurimura, T.7    Wakamiya, N.8
  • 12
    • 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 (1994b) Characterization of the human neutrophil C1q receptor and functional effects of free ligand on activated neutrophils. Blood 84: 1640-1649.
    • (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
  • 14
    • 0028363383 scopus 로고
    • Mannan-binding protein and bovine conglutinin mediate enhancement of herpes simplex virus type 2 infection in mice
    • Fischer PB, Ellermann-Eriksen S, Thiel S, Jensenius JC, Mogensen SC (1994) Mannan-binding protein and bovine conglutinin mediate enhancement of herpes simplex virus type 2 infection in mice. Scand J Immunol 39: 439-445.
    • (1994) Scand J Immunol , vol.39 , pp. 439-445
    • Fischer, P.B.1    Ellermann-Eriksen, S.2    Thiel, S.3    Jensenius, J.C.4    Mogensen, S.C.5
  • 15
    • 0026338749 scopus 로고
    • Conglutinin exhibits a complement-dependent enhancement of the respiratory burst of phagocytes stimulated by E. coli
    • Friis P, Svehag SE, Andersen O, Gahrn-Hansen B, Leslie RG (1991) Conglutinin exhibits a complement-dependent enhancement of the respiratory burst of phagocytes stimulated by E. coli. Immunology 74: 680-684.
    • (1991) Immunology , vol.74 , pp. 680-684
    • Friis, P.1    Svehag, S.E.2    Andersen, O.3    Gahrn-Hansen, B.4    Leslie, R.G.5
  • 17
    • 0027770519 scopus 로고
    • Somatic cell mapping of conglutinin (CGN1) to cattle syntenic group U29 and fluorescence in situ localization to Chromosome 28
    • Gallagher DS Jr, Ryan AM, Liou LS, Sastry KN, Womack JE (1993) Somatic cell mapping of conglutinin (CGN1) to cattle syntenic group U29 and fluorescence in situ localization to Chromosome 28. Mamm Genome 4: 716-719.
    • (1993) Mamm Genome , vol.4 , pp. 716-719
    • Gallagher Jr., D.S.1    Ryan, A.M.2    Liou, L.S.3    Sastry, K.N.4    Womack, J.E.5
  • 18
    • 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 (1984) Identification of the Raji cell membrane-derived C1q inhibitor as a receptor for human C1q. Purification and immunochemical characterization. J Exp Med 160: 1375-1389.
    • (1984) J Exp Med , vol.160 , pp. 1375-1389
    • Ghebrehiwet, B.1    Silvestri, L.2    McDevitt, C.3
  • 19
    • 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 (2003) Calreticulin is at the surface of circulating neutrophils and uses CD59 as an adaptor molecule. J Biol Chem 278: 21024-21031.
    • (2003) J Biol Chem , vol.278 , pp. 21024-21031
    • Ghiran, I.1    Klickstein, L.B.2    Nicholson-Weller, A.3
  • 20
    • 3843105685 scopus 로고    scopus 로고
    • The genes encoding bovine SP-A, SP-D, MBL-A, conglutinin, CL-43 and CL-46 form a distinct collectin locus on Bos taurus chromosome 28 (BTA28) at position q.1.8-1.9
    • Gjerstorff M, Hansen S, Jensen B, Dueholm B, Horn P, Bendixen C, Holmskov U (2004) The genes encoding bovine SP-A, SP-D, MBL-A, conglutinin, CL-43 and CL-46 form a distinct collectin locus on Bos taurus chromosome 28 (BTA28) at position q.1.8-1.9. Anim Genet 35: 333-337.
    • (2004) Anim Genet , vol.35 , pp. 333-337
    • Gjerstorff, M.1    Hansen, S.2    Jensen, B.3    Dueholm, B.4    Horn, P.5    Bendixen, C.6    Holmskov, U.7
  • 21
    • 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 (1994) Cell-surface protein identified on phagocytic cells modulates the C1q-mediated enhancement of phagocytosis. J Immunol 152: 4005-4016.
    • (1994) J Immunol , vol.152 , pp. 4005-4016
    • Guan, E.1    Robinson, S.L.2    Goodman, E.B.3    Tenner, A.J.4
  • 22
    • 0033815279 scopus 로고    scopus 로고
    • Collectin structure: A review
    • Hakansson K, Reid KB (2000) Collectin structure: a review. Protein Sci 9: 1607-1617.
    • (2000) Protein Sci , vol.9 , pp. 1607-1617
    • Hakansson, K.1    Reid, K.B.2
  • 23
    • 0031686350 scopus 로고    scopus 로고
    • Structural aspects of collectins and receptors for collectins
    • Hansen S, Holmskov U (1998) Structural aspects of collectins and receptors for collectins. Immunobiology 199: 165-189.
    • (1998) Immunobiology , vol.199 , pp. 165-189
    • Hansen, S.1    Holmskov, U.2
  • 26
    • 0026653795 scopus 로고
    • Two distinct serum mannose-binding lectins function as beta inhibitors of influenza virus: Identification of bovine serum beta inhibitor as conglutinin
    • Hartley CA, Jackson DC, Anders EM (1992) Two distinct serum mannose-binding lectins function as beta inhibitors of influenza virus: identification of bovine serum beta inhibitor as conglutinin. J Virol 66: 4358-4363.
    • (1992) J Virol , vol.66 , pp. 4358-4363
    • Hartley, C.A.1    Jackson, D.C.2    Anders, E.M.3
  • 28
    • 0029903353 scopus 로고    scopus 로고
    • Interactions of recombinant human pulmonary surfactant protein D and SP-D multimers with influenza A
    • Hartshorn K, Chang D, Rust K, White M, Heuser J, Crouch E (1996a) Interactions of recombinant human pulmonary surfactant protein D and SP-D multimers with influenza A. Am J Physiol 271: L753-762.
    • (1996) Am J Physiol , vol.271
    • Hartshorn, K.1    Chang, D.2    Rust, K.3    White, M.4    Heuser, J.5    Crouch, E.6
  • 29
    • 0029868458 scopus 로고    scopus 로고
    • Neutrophil deactivation by influenza A viruses: Mechanisms of protection after viral opsonization with collectins and hemagglutination-inhibiting antibodies
    • Hartshorn KL, Reid KB, White MR, Jensenius JC, Morris SM, Tauber AI, Crouch E (1996b) Neutrophil deactivation by influenza A viruses: mechanisms of protection after viral opsonization with collectins and hemagglutination- inhibiting antibodies. Blood 87: 3450-3461.
    • (1996) Blood , vol.87 , pp. 3450-3461
    • Hartshorn, K.L.1    Reid, K.B.2    White, M.R.3    Jensenius, J.C.4    Morris, S.M.5    Tauber, A.I.6    Crouch, E.7
  • 30
    • 0031416787 scopus 로고    scopus 로고
    • Mechanisms of anti-influenza activity of surfactant proteins A and D: Comparison with serum collectins
    • Hartshorn KL, White MR, Shepherd V, Reid K, Jensenius JC, Crouch EC (1997) Mechanisms of anti-influenza activity of surfactant proteins A and D: comparison with serum collectins. Am J Physiol 273: L1156-1166.
    • (1997) Am J Physiol , vol.273
    • Hartshorn, K.L.1    White, M.R.2    Shepherd, V.3    Reid, K.4    Jensenius, J.C.5    Crouch, E.C.6
  • 34
    • 0027320098 scopus 로고
    • Studies on the carbohydrate-binding characteristics of human pulmonary surfactant-associated protein A and comparison with two other collectins: Mannan-binding protein and conglutinin
    • Haurum JS, Thiel S, Haagsman HP, Laursen SB, Larsen B, Jensenius JC (1993) Studies on the carbohydrate-binding characteristics of human pulmonary surfactant-associated protein A and comparison with two other collectins: mannan-binding protein and conglutinin. Biochem J 293: 873-878.
    • (1993) Biochem J , vol.293 , pp. 873-878
    • Haurum, J.S.1    Thiel, S.2    Haagsman, H.P.3    Laursen, S.B.4    Larsen, B.5    Jensenius, J.C.6
  • 36
    • 0021950144 scopus 로고
    • Localization of the conglutinin binding site on the third component of human complement
    • Hirani S, Lambris JD, Muller-Eberhard HJ (1985) Localization of the conglutinin binding site on the third component of human complement. J Immunol. 134: 1105-1109.
    • (1985) J Immunol. , vol.134 , pp. 1105-1109
    • Hirani, S.1    Lambris, J.D.2    Muller-Eberhard, H.J.3
  • 37
    • 0022629028 scopus 로고
    • Structural analysis of the asparagine-linked oligosaccharides of human complement component C3
    • Hirani S, Lambris JD, Muller-Eberhard HJ (1986) Structural analysis of the asparagine-linked oligosaccharides of human complement component C3. Biochem J 233: 613-616.
    • (1986) Biochem J , vol.233 , pp. 613-616
    • Hirani, S.1    Lambris, J.D.2    Muller-Eberhard, H.J.3
  • 38
    • 0026516265 scopus 로고
    • Calcium-dependent and calcium-independent signals in the conglutinin-binding assay (KgBa) for immune complexes. Influence of anti-collagen-antibodies
    • Holmskov U, Haas H, Teisner B, Andersen O, Jensenius JC (1992) Calcium-dependent and calcium-independent signals in the conglutinin-binding assay (KgBa) for immune complexes. Influence of anti-collagen-antibodies. J Immunol Methods 148: 225-232.
    • (1992) J Immunol Methods , vol.148 , pp. 225-232
    • Holmskov, U.1    Haas, H.2    Teisner, B.3    Andersen, O.4    Jensenius, J.C.5
  • 40
    • 0027174826 scopus 로고
    • Purification and characterization of a bovine serum lectin (CL-43) with structural homology to conglutinin and SP-D and carbohydrate specificity similar to mannan-binding protein
    • 1993
    • Holmskov U, Teisner B, Willis AC, Reid KB, Jensenius JC (1993) Purification and characterization of a bovine serum lectin (CL-43) with structural homology to conglutinin and SP-D and carbohydrate specificity similar to mannan-binding protein. J Biol Chem 1993 268: 10120-10125.
    • (1993) J Biol Chem , vol.268 , pp. 10120-10125
    • Holmskov, U.1    Teisner, B.2    Willis, A.C.3    Reid, K.B.4    Jensenius, J.C.5
  • 42
    • 0031595083 scopus 로고    scopus 로고
    • The plasma levels of coglutinin are heritable in cattle and low levels predispose to infection
    • Holmskov U, Jensenius JC, Tornoe I, Lovendahl P (1998) The plasma levels of coglutinin are heritable in cattle and low levels predispose to infection. Immunology 93: 431-436.
    • (1998) Immunology , vol.93 , pp. 431-436
    • Holmskov, U.1    Jensenius, J.C.2    Tornoe, I.3    Lovendahl, P.4
  • 43
    • 0033650448 scopus 로고    scopus 로고
    • Collectins and collectin receptors in innate immunity
    • Holmskov UL (2000) Collectins and collectin receptors in innate immunity. APMIS Suppl 100: 1-59.
    • (2000) APMIS Suppl , vol.100 , pp. 1-59
    • Holmskov, U.L.1
  • 44
    • 0028169837 scopus 로고
    • Collectins-soluble proteins containing collagenous regions and lectin domains-and their roles in innate immunity
    • Hoppe HJ, Reid KB (1994) Collectins-soluble proteins containing collagenous regions and lectin domains-and their roles in innate immunity. Protein Sci 3: 1143-1158.
    • (1994) Protein Sci , vol.3 , pp. 1143-1158
    • Hoppe, H.J.1    Reid, K.B.2
  • 45
    • 77950350896 scopus 로고
    • The conglutination phenomenon. XIII. in vivo interactions of conglutinin and experimental bacterial infection
    • Ingram DG (1959a) The conglutination phenomenon. XIII. In vivo interactions of conglutinin and experimental bacterial infection. Immunology 2: 322-333.
    • (1959) Immunology , vol.2 , pp. 322-333
    • Ingram, D.G.1
  • 46
    • 0008003594 scopus 로고
    • The conglutination phenomenon. XIV. The resistance enhancing effect of conglutinin and immuno-conglutinin in experimental bacterial infections
    • Ingram DG (1959b) The conglutination phenomenon. XIV. The resistance enhancing effect of conglutinin and immuno-conglutinin in experimental bacterial infections. Immunology 2: 334-345.
    • (1959) Immunology , vol.2 , pp. 334-345
    • Ingram, D.G.1
  • 47
    • 24044465651 scopus 로고
    • Fluctuations in the level of conglutinin in bovine serum
    • Ingram DG, Barnum DA (1965) Fluctuations in the level of conglutinin in bovine serum. Can Vet J 11: 162-169.
    • (1965) Can Vet J , vol.11 , pp. 162-169
    • Ingram, D.G.1    Barnum, D.A.2
  • 48
    • 0014750610 scopus 로고
    • Conglutinin levels in dairy cattle: Changes associated with parturition
    • Ingram DG, Mitchell WR (1970) Conglutinin levels in dairy cattle: changes associated with parturition. Am J Vet Res 31: 487-492.
    • (1970) Am J Vet Res , vol.31 , pp. 487-492
    • Ingram, D.G.1    Mitchell, W.R.2
  • 49
    • 0014979653 scopus 로고
    • Conglutinin levels in dairy cattle: Seasonal fluctuations
    • Ingram DG, Mitchell WR (1971a) Conglutinin levels in dairy cattle: seasonal fluctuations. Am J Vet Res 32: 23-28.
    • (1971) Am J Vet Res , vol.32 , pp. 23-28
    • Ingram, D.G.1    Mitchell, W.R.2
  • 50
    • 0015073022 scopus 로고
    • Conglutinin level in dairy cattle: Changes associated with disease
    • Ingram DG, Mitchell WR (1971b) Conglutinin level in dairy cattle: changes associated with disease. Am J Vet Res 32: 875-878.
    • (1971) Am J Vet Res , vol.32 , pp. 875-878
    • Ingram, D.G.1    Mitchell, W.R.2
  • 51
    • 0016148717 scopus 로고
    • The effect of breed and age on the distribution of conglutinin and immunoconglutinin in normal cattle
    • Kakoma I, Kinyanjui M (1974) The effect of breed and age on the distribution of conglutinin and immunoconglutinin in normal cattle. Res Vet Sci 17: 122-124.
    • (1974) Res Vet Sci , vol.17 , pp. 122-124
    • Kakoma, I.1    Kinyanjui, M.2
  • 52
    • 0027290030 scopus 로고
    • Differentiation of conglutination activity and sugar-binding activity of conglutinin after removal of NH2-terminal 54 amino acid residues by endogenous serine protease(s)
    • Kawasaki N, Yokota Y, Kawasaki T (1993) Differentiation of conglutination activity and sugar-binding activity of conglutinin after removal of NH2-terminal 54 amino acid residues by endogenous serine protease(s). Arch Biochem Biophys 305: 533-540.
    • (1993) Arch Biochem Biophys , vol.305 , pp. 533-540
    • Kawasaki, N.1    Yokota, Y.2    Kawasaki, T.3
  • 57
    • 0029917167 scopus 로고    scopus 로고
    • Structural basis of galactose recognition by C-type animal lectins
    • Kolatkar AR, Weis WI (1996) Structural basis of galactose recognition by C-type animal lectins. Biol Chem 271: 6679-6685.
    • (1996) Biol Chem , vol.271 , pp. 6679-6685
    • Kolatkar, A.R.1    Weis, W.I.2
  • 60
    • 0005766932 scopus 로고
    • A comparison of some properties of bovine conglutinin with those of rabbit immuno-conglutinin
    • Lachmann PJ (1962) A comparison of some properties of bovine conglutinin with those of rabbit immuno-conglutinin. Immunology 5: 687-705.
    • (1962) Immunology , vol.5 , pp. 687-705
    • Lachmann, P.J.1
  • 61
    • 0014043398 scopus 로고
    • Conglutinin and immunoconglutinins
    • Lachmann PJ (1967) Conglutinin and immunoconglutinins. Adv Immunol 6: 479-527.
    • (1967) Adv Immunol , vol.6 , pp. 479-527
    • Lachmann, P.J.1
  • 62
    • 0028146354 scopus 로고
    • Bovine conglutinin binds to an oligosaccharide determinant presented by iC3b, but not by C3, C3b or C3c
    • Laursen SB, Thiel S, Teisner B, Holmskov U, Wang Y, Sim RB, Jensenius JC (1994) Bovine conglutinin binds to an oligosaccharide determinant presented by iC3b, but not by C3, C3b or C3c. Immunology 81: 648-654.
    • (1994) Immunology , vol.81 , pp. 648-654
    • Laursen, S.B.1    Thiel, S.2    Teisner, B.3    Holmskov, U.4    Wang, Y.5    Sim, R.B.6    Jensenius, J.C.7
  • 63
    • 0025727155 scopus 로고
    • Primary structure of bovine conglutinin, a member of the C-type animal lectin family
    • Lee YM, Leiby KR, Allar J, Paris K, Lerch B, Okarma TB (1991a) Primary structure of bovine conglutinin, a member of the C-type animal lectin family. J Biol Chem 266: 2715-2723.
    • (1991) J Biol Chem , vol.266 , pp. 2715-2723
    • Lee, Y.M.1    Leiby, K.R.2    Allar, J.3    Paris, K.4    Lerch, B.5    Okarma, T.B.6
  • 64
    • 0025906415 scopus 로고
    • Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A). Homology of binding site architecture with mammalian and chicken hepatic lectins
    • Lee RT, Ichikawa Y, Fay M, Drickamer K, Shao MC, Lee YC (1991b) Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A). Homology of binding site architecture with mammalian and chicken hepatic lectins. J Biol Chem 266: 4810-4815.
    • (1991) J Biol Chem , vol.266 , pp. 4810-4815
    • Lee, R.T.1    Ichikawa, Y.2    Fay, M.3    Drickamer, K.4    Shao, M.C.5    Lee, Y.C.6
  • 65
    • 0027459854 scopus 로고
    • Structural similarity between bovine conglutinin and bovine lung surfactant protein D and demonstration of liver as a site of synthesis of conglutinin
    • Lim BL, Lu J, Reid KB (1993) Structural similarity between bovine conglutinin and bovine lung surfactant protein D and demonstration of liver as a site of synthesis of conglutinin. Immunology 78: 159-165.
    • (1993) Immunology , vol.78 , pp. 159-165
    • Lim, B.L.1    Lu, J.2    Reid, K.B.3
  • 66
    • 0028200815 scopus 로고
    • Primary structure of bovine collectin-43 (CL-43). Comparison with conglutinin and lung surfactant protein-D
    • Lim BL, Willis AC, Reid KB, Lu J, Laursen SB, Jensenius JC, Holmskov U (1994) Primary structure of bovine collectin-43 (CL-43). Comparison with conglutinin and lung surfactant protein-D. J Biol Chem 269: 11820-11824
    • (1994) J Biol Chem , vol.269 , pp. 11820-11824
    • Lim, B.L.1    Willis, A.C.2    Reid, K.B.3    Lu, J.4    Laursen, S.B.5    Jensenius, J.C.6    Holmskov, U.7
  • 67
    • 0028226590 scopus 로고
    • Bovine conglutinin (BC) mRNA expressed in liver: Cloning and characterization of the BC cDNA reveals strong homology to surfactant protein-D
    • Liou LS, Sastry R, Hartshorn KL, Lee YM, Okarma TB, Tauber AI, Sastry KN (1994) Bovine conglutinin (BC) mRNA expressed in liver: cloning and characterization of the BC cDNA reveals strong homology to surfactant protein-D. Gene 141: 277-281.
    • (1994) Gene , vol.141 , pp. 277-281
    • Liou, L.S.1    Sastry, R.2    Hartshorn, K.L.3    Lee, Y.M.4    Okarma, T.B.5    Tauber, A.I.6    Sastry, K.N.7
  • 68
    • 0029080979 scopus 로고
    • Collectin-43 is a serum lectin with a distinct pattern of carbohydrate recognition
    • Loveless RW, Holmskov U, Feizi T (1995) Collectin-43 is a serum lectin with a distinct pattern of carbohydrate recognition. Immunology 85: 651-659.
    • (1995) Immunology , vol.85 , pp. 651-659
    • Loveless, R.W.1    Holmskov, U.2    Feizi, T.3
  • 69
    • 0031171222 scopus 로고    scopus 로고
    • Collectins: Collectors of microorganisms for the innate immune system
    • Lu J (1997) Collectins: collectors of microorganisms for the innate immune system. Bioessays 19: 509-518.
    • (1997) Bioessays , vol.19 , pp. 509-518
    • Lu, J.1
  • 70
    • 0027212781 scopus 로고
    • The cDNA cloning of conglutinin and identification of liver as a primary site of synthesis of conglutinin in members of the Bovidae
    • Lu J, Laursen SB, Thiel S, Jensenius JC, Reid KB (1993) The cDNA cloning of conglutinin and identification of liver as a primary site of synthesis of conglutinin in members of the Bovidae. Biochem J 292: 157-162.
    • (1993) Biochem J , vol.292 , pp. 157-162
    • Lu, J.1    Laursen, S.B.2    Thiel, S.3    Jensenius, J.C.4    Reid, K.B.5
  • 71
    • 18944400714 scopus 로고    scopus 로고
    • Susceptibility of mice genetically deficient in the surfactant protein (SP)-A or SP-D gene to pulmonary hypersensitivity induced by antigens and allergens of AspergilIus fumigatus
    • Madan T, Reid KB, Singh M, Sarma PU, Kishore U (2005) Susceptibility of mice genetically deficient in the surfactant protein (SP)-A or SP-D gene to pulmonary hypersensitivity induced by antigens and allergens of AspergilIus fumigatus. J Immunol 174: 6943-6954.
    • (2005) J Immunol , vol.174 , pp. 6943-6954
    • Madan, T.1    Reid, K.B.2    Singh, M.3    Sarma, P.U.4    Kishore, U.5
  • 72
    • 0024421499 scopus 로고
    • Chemical and hydrodynamic characterization of the human leucocyte receptor for complement subcomponent C1q
    • Malhotra R, Sim RB (1989) Chemical and hydrodynamic characterization of the human leucocyte receptor for complement subcomponent C1q. Biochem J 262: 625-631.
    • (1989) Biochem J , vol.262 , pp. 625-631
    • Malhotra, R.1    Sim, R.B.2
  • 73
    • 0025076044 scopus 로고
    • Human leukocyte C1q receptor binds other soluble proteins with collagen domains
    • Malhotra R, Thiel S, Reid KB, Sim RB (1990) Human leukocyte C1q receptor binds other soluble proteins with collagen domains. J Exp Med 172: 955-959.
    • (1990) J Exp Med , vol.172 , pp. 955-959
    • Malhotra, R.1    Thiel, S.2    Reid, K.B.3    Sim, R.B.4
  • 74
    • 0026608869 scopus 로고
    • Interaction of C1q receptor with lung surfactant protein a
    • Malhotra R, Haurum J, Thiel S, Sim RB (1992) Interaction of C1q receptor with lung surfactant protein A. Eur J Immunol 22: 1437-1445.
    • (1992) Eur J Immunol , vol.22 , pp. 1437-1445
    • Malhotra, R.1    Haurum, J.2    Thiel, S.3    Sim, R.B.4
  • 75
    • 0027297280 scopus 로고
    • Localization of the receptor-binding site in the collectin family of proteins
    • Malhotra R, Laursen SB, Willis AC, Sim RB (1993) Localization of the receptor-binding site in the collectin family of proteins. Biochem J 293: 15-19.
    • (1993) Biochem J , vol.293 , pp. 15-19
    • Malhotra, R.1    Laursen, S.B.2    Willis, A.C.3    Sim, R.B.4
  • 77
    • 0024328036 scopus 로고
    • A library of oligosaccharide probes (neoglycolipids) from N-glycosylated proteins reveals that conglutinin binds to certain complex-type as well as high mannose-type oligosaccharide chains
    • Mizuochi T, Loveless RW, Lawson AM, Chai W, Lachmann PJ, Childs RA, Thiel S, Feizi T (1989) A library of oligosaccharide probes (neoglycolipids) from N-glycosylated proteins reveals that conglutinin binds to certain complex-type as well as high mannose-type oligosaccharide chains. J Biol Chem 264: 13834-13839.
    • (1989) J Biol Chem , vol.264 , pp. 13834-13839
    • Mizuochi, T.1    Loveless, R.W.2    Lawson, A.M.3    Chai, W.4    Lachmann, P.J.5    Childs, R.A.6    Thiel, S.7    Feizi, T.8
  • 78
    • 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 (1998) C1qRP, the C1q receptor that enhances phagocytosis, is detected specifically in human cells of myeloid lineage, endothelial cells, and platelets. J Immunol 160: 1929-1935.
    • (1998) J Immunol , vol.160 , pp. 1929-1935
    • Nepomuceno, R.R.1    Tenner, A.J.2
  • 79
    • 0030069340 scopus 로고    scopus 로고
    • Structural analysis of monosaccharide recognition by rat liver mannose-binding protein
    • Ng KK, Drickamer K, Weis WI (1996) Structural analysis of monosaccharide recognition by rat liver mannose-binding protein. Biol Chem 271: 663-674.
    • (1996) Biol Chem , vol.271 , pp. 663-674
    • Ng, K.K.1    Drickamer, K.2    Weis, W.I.3
  • 80
    • 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 (2001) C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J Exp Med 194: 781-795.
    • (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
  • 84
    • 0022309305 scopus 로고
    • The natural resistance of cattle to artificial infection with Cowdria ruminantium: The role played by conglutinin
    • Du Plessis JL (1985) The natural resistance of cattle to artificial infection with Cowdria ruminantium: the role played by conglutinin. Onderstepoort J Vet Res 52: 273-277.
    • (1985) Onderstepoort J Vet Res , vol.52 , pp. 273-277
    • Du Plessis, J.L.1
  • 85
    • 0034329813 scopus 로고    scopus 로고
    • Conglutinin and immunoconglutinin titers in stressed calves in a feedlot
    • Purdy CW, Loan RW, Straus DC, Briggs RE, Frank GH (2000) Conglutinin and immunoconglutinin titers in stressed calves in a feedlot. Am J Vet Res 61: 1403-1409.
    • (2000) Am J Vet Res , vol.61 , pp. 1403-1409
    • Purdy, C.W.1    Loan, R.W.2    Straus, D.C.3    Briggs, R.E.4    Frank, G.H.5
  • 86
    • 4544264420 scopus 로고    scopus 로고
    • Pathogenesis of intestinal and systemic rotavirus infection
    • Ramig RF (2004) Pathogenesis of intestinal and systemic rotavirus infection. J Virol 78: 10213-10220.
    • (2004) J Virol , vol.78 , pp. 10213-10220
    • Ramig, R.F.1
  • 87
    • 0031710735 scopus 로고    scopus 로고
    • Antiviral activity of bovine collectins against rotaviruses
    • Reading PC, Holmskov U, Anders EM (1998) Antiviral activity of bovine collectins against rotaviruses. J Gen Virol 79: 2255-2263.
    • (1998) J Gen Virol , vol.79 , pp. 2255-2263
    • Reading, P.C.1    Holmskov, U.2    Anders, E.M.3
  • 88
    • 0017962626 scopus 로고
    • Serum levels of conglutinin, complement, and immunoconglutinin in cattle infected with Anaplasma marginale
    • Rose JE, Amerault TE, Roby TO, Martin WH (1978) Serum levels of conglutinin, complement, and immunoconglutinin in cattle infected with Anaplasma marginale. Am J Vet Res 39: 791-793.
    • (1978) Am J Vet Res , vol.39 , pp. 791-793
    • Rose, J.E.1    Amerault, T.E.2    Roby, T.O.3    Martin, W.H.4
  • 89
    • 0029100385 scopus 로고
    • Binding of host collectins to the pathogenic yeast Cryptococcus neoformans: Human surfactant protein D acts as an agglutinin for acapsular yeast cells
    • Schelenz S, Malhotra R, Sim RB, Holmskov U, Bancroft GJ (1995) Binding of host collectins to the pathogenic yeast Cryptococcus neoformans: human surfactant protein D acts as an agglutinin for acapsular yeast cells. Infect Immun 63: 3360-3366.
    • (1995) Infect Immun , vol.63 , pp. 3360-3366
    • Schelenz, S.1    Malhotra, R.2    Sim, R.B.3    Holmskov, U.4    Bancroft, G.J.5
  • 92
    • 0031459567 scopus 로고    scopus 로고
    • The C1q and collectin binding site within C1q receptor (cell surface calreticulin)
    • Stuart GR, Lynch NJ, Day AJ, Schwaeble WJ, Sim RB (1997) The C1q and collectin binding site within C1q receptor (cell surface calreticulin). Immunopharmacology 38: 73-80.
    • (1997) Immunopharmacology , vol.38 , pp. 73-80
    • Stuart, G.R.1    Lynch, N.J.2    Day, A.J.3    Schwaeble, W.J.4    Sim, R.B.5
  • 94
    • 0024380059 scopus 로고
    • Human pulmonary surfactant protein (SP-A), a protein structurally homologous to C1q, can enhance FcR- And CR1-mediated phagocytosis
    • Tenner AJ, Robinson SL, Borchelt J, Wright JR (1989) Human pulmonary surfactant protein (SP-A), a protein structurally homologous to C1q, can enhance FcR- and CR1-mediated phagocytosis. J Biol Chem 264: 13923-13928.
    • (1989) J Biol Chem , vol.264 , pp. 13923-13928
    • Tenner, A.J.1    Robinson, S.L.2    Borchelt, J.3    Wright, J.R.4
  • 95
    • 0028880756 scopus 로고
    • Mannose binding protein (MBP) enhances mononuclear phagocyte function via a receptor that contains the 126,000 M(r) component of the C1q receptor
    • Tenner AJ, Robinson SL, Ezekowitz RA (1995) Mannose binding protein (MBP) enhances mononuclear phagocyte function via a receptor that contains the 126,000 M(r) component of the C1q receptor. Immunity 3: 485-493.
    • (1995) Immunity , vol.3 , pp. 485-493
    • Tenner, A.J.1    Robinson, S.L.2    Ezekowitz, R.A.3
  • 96
    • 22544453859 scopus 로고    scopus 로고
    • Clinical manifestations of mannan-binding lectin deficiency
    • Thiel S, Frederiksen PD, Jensenius JC (2006) Clinical manifestations of mannan-binding lectin deficiency. Mol Immunol 43: 86-96.
    • (2006) Mol Immunol , vol.43 , pp. 86-96
    • Thiel, S.1    Frederiksen, P.D.2    Jensenius, J.C.3
  • 98
    • 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 (2002) 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 169: 3978-3986.
    • (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
  • 100
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis WI, Drickamer K, Hendrickson WA (1992) Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 360: 127-134.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.