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Volumn 19, Issue 6, 1997, Pages 509-518

Collectins: Collectors of microorganisms for the innate immune system

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0031171222     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.950190610     Document Type: Review
Times cited : (85)

References (79)
  • 2
    • 0027976024 scopus 로고
    • Collectins: Collagenous C-type lectins of the innate immune defense system
    • Holmskov, U., Malhotra, R., Sim, R. B. and Jensenius, J. C. (1994). Collectins: collagenous C-type lectins of the innate immune defense system. Immunol. Today 15, 67-74.
    • (1994) Immunol. Today , vol.15 , pp. 67-74
    • Holmskov, U.1    Malhotra, R.2    Sim, R.B.3    Jensenius, J.C.4
  • 3
    • 0028169837 scopus 로고
    • Collectins - Soluble proteins containing collagenous regions and lectin domains - and their roles in innate immunity
    • Hoppe, H. J. and Reid, K. B. M. (1994). Collectins - soluble proteins containing collagenous regions and lectin domains - and their roles in innate immunity. Prot. Sci. 3, 1143-1158
    • (1994) Prot. Sci. , vol.3 , pp. 1143-1158
    • Hoppe, H.J.1    Reid, K.B.M.2
  • 4
    • 0027828449 scopus 로고
    • Similarity in structure between C1q and the collectins as judged by electron microscopy
    • Lu, J., Wiedemann, H., Timpl, R. and Reid, K. B. M. (1993). Similarity in structure between C1q and the collectins as judged by electron microscopy. Behring Inst. Mitt. 93, 6-16.
    • (1993) Behring Inst. Mitt. , vol.93 , pp. 6-16
    • Lu, J.1    Wiedemann, H.2    Timpl, R.3    Reid, K.B.M.4
  • 6
    • 0022336932 scopus 로고
    • Glycosylation and secretion of surfactant-associated protin A
    • Whitsett, J. A., Ross, G., Weaver, T., Rice, W., Dion, C. and Hull, W. (1985). Glycosylation and secretion of surfactant-associated protin A. J. Biol. Chem. 260, 15273-15279.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15273-15279
    • Whitsett, J.A.1    Ross, G.2    Weaver, T.3    Rice, W.4    Dion, C.5    Hull, W.6
  • 7
    • 0028533911 scopus 로고
    • Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil
    • Sheriff, S., Chang, C. Y. and Ezekowitz, R. A. B. (1994). Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil. Nature Struct. Biol. 1, 789-794.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 789-794
    • Sheriff, S.1    Chang, C.Y.2    Ezekowitz, R.A.B.3
  • 8
    • 0028774718 scopus 로고
    • Trimeric structure of a C-type mannose-binding protein
    • Weis, W. I. and Drickamer, K. (1994). Trimeric structure of a C-type mannose-binding protein. Structure 2, 1227-1240.
    • (1994) Structure , vol.2 , pp. 1227-1240
    • Weis, W.I.1    Drickamer, K.2
  • 9
    • 0023890913 scopus 로고
    • Macromolecular organisation of natural and recombinant lung surfactant protein SP 28-36
    • Voss, T., Eistetter, H. and Schafer, K. P. (1988). Macromolecular organisation of natural and recombinant lung surfactant protein SP 28-36. J. Mol. Biol. 201, 219-227.
    • (1988) J. Mol. Biol. , vol.201 , pp. 219-227
    • Voss, T.1    Eistetter, H.2    Schafer, K.P.3
  • 10
    • 0026085036 scopus 로고
    • Structural comparison of recombinant pulmonary surfactant protein SP-A derived from two human coding sequences: Implications for the chain composition of natural human SP-A
    • Voss, T., Melchers, K., Scheirle, G. and Schafer, K. P. (1991). Structural comparison of recombinant pulmonary surfactant protein SP-A derived from two human coding sequences: implications for the chain composition of natural human SP-A. Am. J. Respir. Cell Mol. Biol. 4, 88-94.
    • (1991) Am. J. Respir. Cell Mol. Biol. , vol.4 , pp. 88-94
    • Voss, T.1    Melchers, K.2    Scheirle, G.3    Schafer, K.P.4
  • 11
    • 0027227391 scopus 로고
    • Structural similarity between lung surfactant protein D and conglutinin. Two distinct, C-type lectins containing collagen-like sequences
    • Lu, J., Wiedemann, H., Holmskov, U., Thiel, S., Timpl, R. and Reid, K. B. M. (1993). Structural similarity between lung surfactant protein D and conglutinin. Two distinct, C-type lectins containing collagen-like sequences. Eur. J. Biochem. 215, 793-799.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 793-799
    • Lu, J.1    Wiedemann, H.2    Holmskov, U.3    Thiel, S.4    Timpl, R.5    Reid, K.B.M.6
  • 12
    • 0028233879 scopus 로고
    • Molecular structure of pulmonary surfactant protein D (SP-D)
    • Crouch, E., Persson, A., Chang, D. and Heuser, J. (1994). Molecular structure of pulmonary surfactant protein D (SP-D). J. Biol. Chem. 269, 17311-17319.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17311-17319
    • Crouch, E.1    Persson, A.2    Chang, D.3    Heuser, J.4
  • 13
    • 0022442546 scopus 로고
    • Ultrastructure and composition of bovine conglutinin
    • Strang, C. J., Slayter, H. S., Lachmann, P. J. and Davis, A. E. (1986). Ultrastructure and composition of bovine conglutinin. Biochem. J. 234, 381-389.
    • (1986) Biochem. J. , vol.234 , pp. 381-389
    • Strang, C.J.1    Slayter, H.S.2    Lachmann, P.J.3    Davis, A.E.4
  • 14
    • 0022844505 scopus 로고
    • Mannose-binding proteins isolated from rat liver contain carbohydrate recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein
    • Drickamer, K., Dordal, M. S. and Reynolds, L. (1986). Mannose-binding proteins isolated from rat liver contain carbohydrate recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein. J. Biol. Chem. 261, 6878-6887.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6878-6887
    • Drickamer, K.1    Dordal, M.S.2    Reynolds, L.3
  • 15
    • 0025879803 scopus 로고
    • Molecular characterization of the mouse mannose-binding proteins. The mannose-binding protein A but not C is an acute phase reactant
    • Sastry, K., Zahedi, K., Lellas, J. M., Whitehead, A. S. and Ezekowitz, R. A. B. (1991). Molecular characterization of the mouse mannose-binding proteins. The mannose-binding protein A but not C is an acute phase reactant. J. Immunol. 147, 692-697.
    • (1991) J. Immunol. , vol.147 , pp. 692-697
    • Sastry, K.1    Zahedi, K.2    Lellas, J.M.3    Whitehead, A.S.4    Ezekowitz, R.A.B.5
  • 16
    • 0023645042 scopus 로고
    • Serum lectin with known structure activates complement through the classical pathway
    • Ikeda, K., Sannoh, T., Kawasaki, N., Kawasaki, T. and Yamashina, I. (1987). Serum lectin with known structure activates complement through the classical pathway. J. Biol. Chem. 262, 7451-7454.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7451-7454
    • Ikeda, K.1    Sannoh, T.2    Kawasaki, N.3    Kawasaki, T.4    Yamashina, I.5
  • 17
    • 0025230703 scopus 로고
    • Binding of the pentamer/hexamer forms of mannan-binding protein to zymosan activates the proenzyme C1r2C1s2 complex, of the classical pathway of complement, without the involvement of C1q
    • Lu, J., Thiel, S., Wiedemann, H., Timpl, R. and Reid, K. B. M. (1990) Binding of the pentamer/hexamer forms of mannan-binding protein to zymosan activates the proenzyme C1r2C1s2 complex, of the classical pathway of complement, without the involvement of C1q. J. Immunol. 144, 2287-2294.
    • (1990) J. Immunol. , vol.144 , pp. 2287-2294
    • Lu, J.1    Thiel, S.2    Wiedemann, H.3    Timpl, R.4    Reid, K.B.M.5
  • 18
    • 0028928607 scopus 로고
    • Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins
    • Holmskov, U. et al. (1995). Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins. Biochem. J. 305, 889-896.
    • (1995) Biochem. J. , vol.305 , pp. 889-896
    • Holmskov, U.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, G. C., Blake, D. J. and Reid, K. B. M. (1991). 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. 274, 481-490.
    • (1991) Biochem. J. , vol.274 , pp. 481-490
    • Sellar, G.C.1    Blake, D.J.2    Reid, K.B.M.3
  • 20
    • 0024366011 scopus 로고
    • Structure and evolutionary origin of the gene encoding a human serum mannose-binding protein
    • Taylor, M. E., Brickell, P. M., Cralg, R. K. and Summerfiled, J. A. (1989). Structure and evolutionary origin of the gene encoding a human serum mannose-binding protein. Biochem. J. 262, 763-771.
    • (1989) Biochem. J. , vol.262 , pp. 763-771
    • Taylor, M.E.1    Brickell, P.M.2    Cralg, R.K.3    Summerfiled, J.A.4
  • 21
    • 0024415548 scopus 로고
    • The human mannose-binding protein gene. Exon structure reveals its evolutionary relationship to a human pulmonary surfactant gene and localization to chromosome 10
    • Sastry, K. et al. (1989). The human mannose-binding protein gene. Exon structure reveals its evolutionary relationship to a human pulmonary surfactant gene and localization to chromosome 10. J. Exp. Med. 170, 1175-1189.
    • (1989) J. Exp. Med. , vol.170 , pp. 1175-1189
    • Sastry, K.1
  • 22
    • 0022006738 scopus 로고
    • Isolation and characterization of human pulmonary surfactant apoprotein gene
    • White, R. T. et al. (1985). Isolation and characterization of human pulmonary surfactant apoprotein gene. Nature 317, 361-363
    • (1985) Nature , vol.317 , pp. 361-363
    • White, R.T.1
  • 23
    • 0023000540 scopus 로고
    • Isolation and characterization of cDNA clones for the 35 kDa pulmonary surfactant-associated protein
    • Floras, J. et al. (1986). Isolation and characterization of cDNA clones for the 35 kDa pulmonary surfactant-associated protein. J. Biol. Chem. 261, 9029-9033.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9029-9033
    • Floras, J.1
  • 24
    • 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, S. B., Thiel, S., Jensenius, J. C. and Reid, K. B. M. (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.M.5
  • 25
    • 0020530882 scopus 로고
    • Identification of mannan-binding protein from rat livers as hepatocyte protein distinct from the mannose receptor on sinusoidal cells
    • Mori, K., Kawasaki, T. and Yamashina, I. (1984). Identification of mannan-binding protein from rat livers as hepatocyte protein distinct from the mannose receptor on sinusoidal cells. Arch. Biochem. Biophys. 222, 542-552.
    • (1984) Arch. Biochem. Biophys. , vol.222 , pp. 542-552
    • Mori, K.1    Kawasaki, T.2    Yamashina, I.3
  • 26
    • 0028200815 scopus 로고
    • Primary structure of bovine collectin-43 (CL-43)
    • Lim, B. L. et al. (1994). Primary structure of bovine collectin-43 (CL-43). J. Biol. Chem. 269, 11820-11824.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11820-11824
    • Lim, B.L.1
  • 27
    • 0022456402 scopus 로고
    • Immunocytochemical localization of the major surfactant proteins in type II cells, Clara cells and alveolar macrophages of rat lung
    • Walker, S. R., Williams, M. C. and Benson, B. (1986) Immunocytochemical localization of the major surfactant proteins in type II cells, Clara cells and alveolar macrophages of rat lung. J. Histochem. Cytochem. 34, 1137-1148.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 1137-1148
    • Walker, S.R.1    Williams, M.C.2    Benson, B.3
  • 28
    • 0026659644 scopus 로고
    • Surfactant protein D: Subcellular localization in nonciliated bronchiolar epithelial cells
    • Crouch, E., Parghi, D., Kuan, S. F. and Persson, N. (1992). Surfactant protein D: subcellular localization in nonciliated bronchiolar epithelial cells. Am. J. Physiol. 263, L60-L66.
    • (1992) Am. J. Physiol. , vol.263
    • Crouch, E.1    Parghi, D.2    Kuan, S.F.3    Persson, N.4
  • 29
    • 0026085459 scopus 로고
    • Function and regulation of expression of pulmonary surfactant-associated proteins
    • Weaver, T. and Whitsett, J. A. (1991). Function and regulation of expression of pulmonary surfactant-associated proteins. Biochem. J. 273, 249-264.
    • (1991) Biochem. J. , vol.273 , pp. 249-264
    • Weaver, T.1    Whitsett, J.A.2
  • 30
    • 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, J. S., Thiel, S., Haagsman, H. P., Laursen, S. B., Larsen, B. and Jensenius, J. C. (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
  • 31
    • 0029967458 scopus 로고    scopus 로고
    • Calcium dependent association of surfactant protein A with pulmonary surfactant: Application to simple surfactant protein A purification
    • Suwabe, A., Mason, R. J. and Voelker, D. R. (1996). Calcium dependent association of surfactant protein A with pulmonary surfactant: application to simple surfactant protein A purification. Arch. Biochem. Biophys. 327, 285-291.
    • (1996) Arch. Biochem. Biophys. , vol.327 , pp. 285-291
    • Suwabe, A.1    Mason, R.J.2    Voelker, D.R.3
  • 32
    • 0028997650 scopus 로고
    • Altered carbohydrate recognition specificity engineered into surfactant protein D reveals different binding mechanisms for phosphatidylinositol and glucosylceramide
    • Ogasawara, Y. and Voelker. D. R. (1995). Altered carbohydrate recognition specificity engineered into surfactant protein D reveals different binding mechanisms for phosphatidylinositol and glucosylceramide. J. Biol. Chem. 270, 14725-14732.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14725-14732
    • Ogasawara, Y.1    Voelker, D.R.2
  • 33
    • 0025213354 scopus 로고
    • Surfactant protein D is a divalent cation-dependent carbohydrate-binding protein
    • Persson, A., Chang, D. and Crouch, E. (1990). Surfactant protein D is a divalent cation-dependent carbohydrate-binding protein. J. Biol. Chem. 265, 5755-5760.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5755-5760
    • Persson, A.1    Chang, D.2    Crouch, E.3
  • 34
    • 0029020234 scopus 로고
    • Pulmonary surfactant protein A (SP-A) is expressed by epithelial cells of small and large intestine
    • Rubio, S., Lacaze-Masmonteil, T., Chailley-Heu, B., Kahn, A., Bourbon, J. R. and Ducroc, R. (1995). Pulmonary surfactant protein A (SP-A) is expressed by epithelial cells of small and large intestine. J. Biol. Chem. 270, 12162-12169.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12162-12169
    • Rubio, S.1    Lacaze-Masmonteil, T.2    Chailley-Heu, B.3    Kahn, A.4    Bourbon, J.R.5    Ducroc, R.6
  • 35
    • 0029181346 scopus 로고
    • Expression of pulmonary surfactant protein D in rat gastic mucosa
    • Fisher, J. H. and Mason, R. J. (1995). Expression of pulmonary surfactant protein D in rat gastic mucosa. Am. J. Respir. Cell Mol. Biol. 12, 13-18.
    • (1995) Am. J. Respir. Cell Mol. Biol. , vol.12 , pp. 13-18
    • Fisher, J.H.1    Mason, R.J.2
  • 36
    • 9544243825 scopus 로고    scopus 로고
    • Altered surfactant function and structure in SP-A gene targeted mice
    • Korfhagen, T. R. et al. (1996). Altered surfactant function and structure in SP-A gene targeted mice. Proc. Natl. Acad. Sci. USA 93, 9594-9599.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9594-9599
    • Korfhagen, T.R.1
  • 37
    • 0027418167 scopus 로고
    • Elevated levels of lung surfactant protein A in sera from patients with idopathic pulmonary fibrosis and pulmonary alveolar proteinosis
    • Kuroki, Y. et al. (1993). Elevated levels of lung surfactant protein A in sera from patients with idopathic pulmonary fibrosis and pulmonary alveolar proteinosis. Am. Rev. Respir. Dis. 147, 723-729.
    • (1993) Am. Rev. Respir. Dis. , vol.147 , pp. 723-729
    • Kuroki, Y.1
  • 38
    • 0028820752 scopus 로고
    • Pulmonary surfactant protein D in sera and bronchoalveolar lavage fluids
    • Honda, Y. et al. (1995). Pulmonary surfactant protein D in sera and bronchoalveolar lavage fluids. Am. J. Respir. Crit. Care Med. 152, 1860-1866.
    • (1995) Am. J. Respir. Crit. Care Med. , vol.152 , pp. 1860-1866
    • Honda, Y.1
  • 39
    • 0022913249 scopus 로고
    • Regulation of pulmonary surfactant protein SP 28-36 gene in human fetal lung
    • Ballard, P. L. et al. (1986). Regulation of pulmonary surfactant protein SP 28-36 gene in human fetal lung. Proc. Natl. Acad. Sci. USA 83, 9527-9531.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 9527-9531
    • Ballard, P.L.1
  • 40
    • 0016589012 scopus 로고
    • Appearence of apoproteins of pulmonary surfactant in human amniotic fluid
    • King, R. J., Ruth, J., Gikas, E. G., Platzker, A. C. G. and Creasy, R. K. (1975). Appearence of apoproteins of pulmonary surfactant in human amniotic fluid. J. Appl. Physiol. 39, 735-741.
    • (1975) J. Appl. Physiol. , vol.39 , pp. 735-741
    • King, R.J.1    Ruth, J.2    Gikas, E.G.3    Platzker, A.C.G.4    Creasy, R.K.5
  • 41
    • 84988073248 scopus 로고
    • Increases in the 35 kDa surfactant-associated protein and its mRNA following in vivo dexamethasone threatment of fetal and neonatal rat
    • Phelps, D. S., Church, S., Kourembanas, S., Taeusch, H. M. and Floras, J. (1987). Increases in the 35 kDa surfactant-associated protein and its mRNA following in vivo dexamethasone threatment of fetal and neonatal rat. Electrophoresis 8, 235-238.
    • (1987) Electrophoresis , vol.8 , pp. 235-238
    • Phelps, D.S.1    Church, S.2    Kourembanas, S.3    Taeusch, H.M.4    Floras, J.5
  • 43
    • 0027716353 scopus 로고
    • Perinatal changes in serum mannose-binding protein (MBP) levels
    • Terai, I. and Kobayashi, K. (1993). Perinatal changes in serum mannose-binding protein (MBP) levels. Immunol. Lett. 38, 185-187.
    • (1993) Immunol. Lett. , vol.38 , pp. 185-187
    • Terai, I.1    Kobayashi, K.2
  • 45
    • 0030391388 scopus 로고    scopus 로고
    • Age-dependent variation in the serum concentration of mannan-binding protein
    • Aittoniemi, J. et al. (1996). Age-dependent variation in the serum concentration of mannan-binding protein. Acta Paediatrica 85, 906-909.
    • (1996) Acta Paediatrica , vol.85 , pp. 906-909
    • Aittoniemi, J.1
  • 46
    • 0029045792 scopus 로고
    • Interplay between promoter and structural gene variants control basal serum level of mannan-binding protein
    • Madsen, H. O. et al. (1995). Interplay between promoter and structural gene variants control basal serum level of mannan-binding protein. J. Immunol. 155, 3013-3020.
    • (1995) J. Immunol. , vol.155 , pp. 3013-3020
    • Madsen, H.O.1
  • 47
    • 0030008251 scopus 로고    scopus 로고
    • Mutations in the human mannose-binding protein gene - Frequencies in several population groups
    • Lipscombe, R. J. et al. (1996). Mutations in the human mannose-binding protein gene - frequencies in several population groups. Eur. J. Hum. Genet. 4, 13-19.
    • (1996) Eur. J. Hum. Genet. , vol.4 , pp. 13-19
    • Lipscombe, R.J.1
  • 48
    • 0026699355 scopus 로고
    • The concentration of the C-type lectin, mannan-binding protein, in human plasma increases during an acute phase response
    • Thiel, S., Holmskov, U., Hviid, L., Laursen, S. B. and Jensenius, J. C. (1992). The concentration of the C-type lectin, mannan-binding protein, in human plasma increases during an acute phase response. Clin. Exp. Immunol. 90, 31-35.
    • (1992) Clin. Exp. Immunol. , vol.90 , pp. 31-35
    • Thiel, S.1    Holmskov, U.2    Hviid, L.3    Laursen, S.B.4    Jensenius, J.C.5
  • 49
    • 0017962626 scopus 로고
    • Serum levels of conglutinin, complement and immunoconglutinin in cattle infected with Anaplasma marginale
    • Rose, J. E., Amerault, T. E., Roby, T. O. and Martin, W. H. (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
  • 50
    • 0021950144 scopus 로고
    • Localization of the conglutinin binding site on the third component of human complement
    • Hirani, S., Lambris, J. D. and Muller-Eberhard, H. J. (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
  • 51
    • 0027466290 scopus 로고
    • Genomic organization of human surfactant protein D (SP-D). SP-D is encoded on chromosome 10q22.2-23.1
    • Crouch, E., Rust, K., Veile, R., Donis-Keller, H. and Grosso, L. (1993). Genomic organization of human surfactant protein D (SP-D). SP-D is encoded on chromosome 10q22.2-23.1. J. Biol. Chem. 268, 2976-2983.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2976-2983
    • Crouch, E.1    Rust, K.2    Veile, R.3    Donis-Keller, H.4    Grosso, L.5
  • 52
    • 0028364621 scopus 로고
    • Gene organization and 5′-flanking region sequence of conglutinin: A C-type mammalian lectin containing a collagen-like domain
    • Kawasaki, N. Itoh, N. and Kawasaki, T. (1994). Gene organization and 5′-flanking region sequence of conglutinin: a C-type mammalian lectin containing a collagen-like domain. Biochem. Biophys. Res. Commun. 198, 597-604.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 597-604
    • Kawasaki, N.1    Itoh, N.2    Kawasaki, T.3
  • 53
    • 0027296942 scopus 로고
    • Assignment of the human pulmonary surfactant protein D gene (SFTP4) to 10q22-q23 close to the surfactant protein A gene cluster
    • Kolble, K., Lu, J., Mole, S. E., Kaluz, S. and Reid, K. B. M. (1993). Assignment of the human pulmonary surfactant protein D gene (SFTP4) to 10q22-q23 close to the surfactant protein A gene cluster. Genomics 17, 294-298.
    • (1993) Genomics , vol.17 , pp. 294-298
    • Kolble, K.1    Lu, J.2    Mole, S.E.3    Kaluz, S.4    Reid, K.B.M.5
  • 54
    • 0028675629 scopus 로고
    • The murine mannose-binding protein genes (mbl 1 and mbl 2) localize to chromosomes 14 and 19
    • White, R. A., Dowler, L. L., Adkison, L. R., Ezekowitz, R. A. B. and Sastry, K. N. (1994). The murine mannose-binding protein genes (mbl 1 and mbl 2) localize to chromosomes 14 and 19. Mamm. Genome. 5, 807-809.
    • (1994) Mamm. Genome. , vol.5 , pp. 807-809
    • White, R.A.1    Dowler, L.L.2    Adkison, L.R.3    Ezekowitz, R.A.B.4    Sastry, K.N.5
  • 55
    • 0028971996 scopus 로고
    • Mouse surfactant protein D - cDNA cloning, characterization, and gene localization to chromosome 14
    • Motwani, M., White, R. A., Guo, N., Dowler, L. L., Tauber, A. I. and Sastry, K. N. (1995). Mouse surfactant protein D - cDNA cloning, characterization, and gene localization to chromosome 14. J. Immunol. 155, 5671-5677.
    • (1995) J. Immunol. , vol.155 , pp. 5671-5677
    • Motwani, M.1    White, R.A.2    Guo, N.3    Dowler, L.L.4    Tauber, A.I.5    Sastry, K.N.6
  • 56
    • 0024446048 scopus 로고
    • Association of low levels of mannan-binding protein with a common defect of opsonisation
    • Super, M., Thiel, S., Lu, J., Levinsky, R. J. and Turner, M. W. (1989). Association of low levels of mannan-binding protein with a common defect of opsonisation. Lancet 2, 1236-1239.
    • (1989) Lancet , vol.2 , pp. 1236-1239
    • Super, M.1    Thiel, S.2    Lu, J.3    Levinsky, R.J.4    Turner, M.W.5
  • 57
    • 0026439234 scopus 로고
    • Engineering galactose-binding activity into a C-type mannose-binding protein
    • Drickamer, K. (1992). Engineering galactose-binding activity into a C-type mannose-binding protein. Nature 360, 183-186.
    • (1992) Nature , vol.360 , pp. 183-186
    • Drickamer, K.1
  • 58
    • 0029001510 scopus 로고
    • Selectin-carbohydrate interactions and the initiation of the inflammatory response
    • Lasky, L. A. (1995). Selectin-carbohydrate interactions and the initiation of the inflammatory response. Annu. Rev. Biochem. 64, 113-139.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 113-139
    • Lasky, L.A.1
  • 60
    • 0025145598 scopus 로고
    • The mechanism of carbohydrate-mediated complement activation by the serum mannan-binding protein
    • Ohta, M., Okada, M., Yamashina, I. and Kawasaki, T. (1990). The mechanism of carbohydrate-mediated complement activation by the serum mannan-binding protein. J. Biol. Chem. 265, 1980-1984.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1980-1984
    • Ohta, M.1    Okada, M.2    Yamashina, I.3    Kawasaki, T.4
  • 61
    • 0026445745 scopus 로고
    • Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease
    • Matsushita, M. and Fujita, T. (1992). Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine protease. J. Exp. Med. 176, 1497-1502.
    • (1992) J. Exp. Med. , vol.176 , pp. 1497-1502
    • Matsushita, M.1    Fujita, T.2
  • 62
    • 0024231102 scopus 로고
    • The C4 and C2 but not C1 components of complement are responsible for the complement activation triggered by the Ra-reactive factor
    • Ji, Y., Matsushita, M., Okada, H., Fujita, T. and Kawakami, M. (1988). The C4 and C2 but not C1 components of complement are responsible for the complement activation triggered by the Ra-reactive factor. J. Immunol. 141, 4271-4278.
    • (1988) J. Immunol. , vol.141 , pp. 4271-4278
    • Ji, Y.1    Matsushita, M.2    Okada, H.3    Fujita, T.4    Kawakami, M.5
  • 63
    • 0343394071 scopus 로고    scopus 로고
    • Identification of a new mannan-binding lectin associated serine protease (MASP-2)
    • abstract
    • Thiel, S. et al. (1996). Identification of a new mannan-binding lectin associated serine protease (MASP-2). Mol. Immunol. 33 (suppl. 1), 91 (abstract).
    • (1996) Mol. Immunol. , vol.33 , Issue.1 SUPPL. , pp. 91
    • Thiel, S.1
  • 65
    • 0025076044 scopus 로고
    • Human leukocyte C1q receptor binds other soluble proteins with collagen domains
    • Malhotra, R., Thiel, S., Reid, K. B. M. and Sim, R. B. (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.M.3    Sim, R.B.4
  • 66
    • 0027511510 scopus 로고
    • Structure and homology of human C1r receptor (collectin receptor)
    • Malhotra, R., Willis, A. C., Jensenius, J. C., Jackson, J. and Sim, R. B. (1993). Structure and homology of human C1r receptor (collectin receptor). Immunology 78, 341-448.
    • (1993) Immunology , vol.78 , pp. 341-448
    • Malhotra, R.1    Willis, A.C.2    Jensenius, J.C.3    Jackson, J.4    Sim, R.B.5
  • 69
    • 0024553735 scopus 로고
    • The human mannose-binding protein functions as an opsonin
    • Kuhlman, M., Joiner, K. and Ezekowitz, R. A. B. (1989). The human mannose-binding protein functions as an opsonin. J. Exp. Med. 169, 1733-1745.
    • (1989) J. Exp. Med. , vol.169 , pp. 1733-1745
    • Kuhlman, M.1    Joiner, K.2    Ezekowitz, R.A.B.3
  • 70
    • 0028880756 scopus 로고
    • Mannose binding protein (MBP) enhances mononuclear phagocyte function via a receptor that contains the 126,000 Mr component of the C1q receptor
    • Tenner, A. J., Robinson, S. L. and Ezekowitz, R. A. B. (1995). Mannose binding protein (MBP) enhances mononuclear phagocyte function via a receptor that contains the 126,000 Mr 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.B.3
  • 71
    • 0039255371 scopus 로고    scopus 로고
    • C1q and pulmonary surfactant protein A (SPA) trigger enhanced phagocytic capacity with identical kinetics and via the same 126,000 Mr cell surface 'C1q receptor.'
    • abstract
    • Ruiz, S. and Tenner, A. J. (1996). C1q and pulmonary surfactant protein A (SPA) trigger enhanced phagocytic capacity with identical kinetics and via the same 126,000 Mr cell surface 'C1q receptor.' Mol. Immunol. 33 (suppl. 1), 65 (abstract).
    • (1996) Mol. Immunol. , vol.33 , Issue.1 SUPPL. , pp. 65
    • Ruiz, S.1    Tenner, A.J.2
  • 72
    • 0029558595 scopus 로고
    • Lung surfactant protein S (SP-A) activates a phosphoinositide/calcium signaling pathway in alveolar macrophages
    • Ohmer-Schrock, D., Schlatterer, C., Platter, H. and Schlepper-Schafer, J. (1995). Lung surfactant protein S (SP-A) activates a phosphoinositide/calcium signaling pathway in alveolar macrophages. J. Cell Sci. 108, 3695-3702.
    • (1995) J. Cell Sci. , vol.108 , pp. 3695-3702
    • Ohmer-Schrock, D.1    Schlatterer, C.2    Platter, H.3    Schlepper-Schafer, J.4
  • 73
    • 0028832349 scopus 로고
    • Pulmonary surfactant protein A mediates enhanced phagocytosis of Mycobacterium tuberculosis by a direct interaction with human macrophages
    • Gaynor, C. D., McCormack, F. X., Voelker, D. R., McGowan, S. E. and Schlesinger, S. L. (1995). Pulmonary surfactant protein A mediates enhanced phagocytosis of Mycobacterium tuberculosis by a direct interaction with human macrophages. J. Immunol. 155, 5343-5351.
    • (1995) J. Immunol. , vol.155 , pp. 5343-5351
    • Gaynor, C.D.1    McCormack, F.X.2    Voelker, D.R.3    McGowan, S.E.4    Schlesinger, S.L.5
  • 74
    • 0029796408 scopus 로고    scopus 로고
    • Human surfactant protein A with two distinct oligomeric structures which exhibit different capacities to interact with alveolar type II cells
    • Hattori, A., Kuroki, Y., Sohma, H., Ogasawara, Y. and Akino, T. (1996). Human surfactant protein A with two distinct oligomeric structures which exhibit different capacities to interact with alveolar type II cells. Biochem. J. 317, 939-944.
    • (1996) Biochem. J. , vol.317 , pp. 939-944
    • Hattori, A.1    Kuroki, Y.2    Sohma, H.3    Ogasawara, Y.4    Akino, T.5
  • 75
    • 0027278514 scopus 로고
    • Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains
    • Ichijo, H. et al. (1993). Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen-and collagen-like domains. J. Biol. Chem. 268, 14505-14513.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14505-14513
    • Ichijo, H.1
  • 76
    • 0030034860 scopus 로고    scopus 로고
    • Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9
    • Lu, J., Tay, P. N., Kon, O. L. and Reid, K. B. M. (1996). Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9. Biochem. J. 313, 473-478.
    • (1996) Biochem. J. , vol.313 , pp. 473-478
    • Lu, J.1    Tay, P.N.2    Kon, O.L.3    Reid, K.B.M.4
  • 77
    • 0030068057 scopus 로고    scopus 로고
    • A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin
    • Matsushita, M. et al. (1996). A novel human serum lectin with collagen-and fibrinogen-like domains that functions as an opsonin. J. Biol. Chem. 271, 2448-2454.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2448-2454
    • Matsushita, M.1
  • 78
    • 0029821215 scopus 로고    scopus 로고
    • Biosynthesis of human ficolin, an E. coli-binding protein, by adherent monocytes and comparison with the synthesis of two macrophage-specific proteins, C1q and the mannose receptor
    • Lu, J., Le, Y., Kon, O. L., Chan, J. and Lee, S. H. (1996). Biosynthesis of human ficolin, an E. coli-binding protein, by adherent monocytes and comparison with the synthesis of two macrophage-specific proteins, C1q and the mannose receptor. Immunology 89, 289-294.
    • (1996) Immunology , vol.89 , pp. 289-294
    • Lu, J.1    Le, Y.2    Kon, O.L.3    Chan, J.4    Lee, S.H.5
  • 79
    • 0026740587 scopus 로고
    • Purification, characterization and cDNA cloning of human pulmonary surfactant protein D
    • Lu, J., Willis, A. C. and Reid, K. B. M. (1992). Purification, characterization and cDNA cloning of human pulmonary surfactant protein D. Biochem. J. 284, 795-802.
    • (1992) Biochem. J. , vol.284 , pp. 795-802
    • Lu, J.1    Willis, A.C.2    Reid, K.B.M.3


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