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Volumn 172, Issue 12, 2004, Pages 7592-7602

Pulmonary collectins enhance phagocytosis of Mycobacterium avium through increased activity of mannose receptor

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE SERUM ALBUMIN; CALCIUM ION; COLLECTIN; IODINE 125; LIPOARABINOMANNAN; MANNAN; MANNOSE BINDING LECTIN; MANNOSE RECEPTOR; SURFACTANT PROTEIN A; SURFACTANT PROTEIN D; ZYMOSAN;

EID: 2942622147     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.172.12.7592     Document Type: Article
Times cited : (105)

References (61)
  • 1
    • 0015611306 scopus 로고
    • Isolation of apoproteins from canine surface active materials
    • King, R. J., D. J. Klass, E. G. Gikas, and J. A. Clements. 1973. Isolation of apoproteins from canine surface active materials. Am. J. Physiol. 224:788.
    • (1973) Am. J. Physiol. , vol.224 , pp. 788
    • King, R.J.1    Klass, D.J.2    Gikas, E.G.3    Clements, J.A.4
  • 2
    • 0027996784 scopus 로고
    • Pulmonary surfactant proteins
    • Kuroki, Y., and D. R. Voelker. 1994. Pulmonary surfactant proteins. J. Biol. Chem. 269:25943.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25943
    • Kuroki, Y.1    Voelker, D.R.2
  • 3
    • 0030784825 scopus 로고    scopus 로고
    • Immunomodulatory functions of surfactant
    • Wright, J. R. 1997. Immunomodulatory functions of surfactant. Physiol. Rev. 77:931.
    • (1997) Physiol. Rev. , vol.77 , pp. 931
    • Wright, J.R.1
  • 4
    • 0028196754 scopus 로고
    • The C-type carbohydrate recognition domain (CRD) superfamily
    • Day, A. J. 1994. The C-type carbohydrate recognition domain (CRD) superfamily. Biochem. Soc. Trans. 22:83.
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 83
    • Day, A.J.1
  • 5
    • 0032135111 scopus 로고    scopus 로고
    • Collectins and pulmonary host defense
    • Crouch, E. C. 1998. Collectins and pulmonary host defense. Am. J. Respir. Cell Mol. Biol. 19:177.
    • (1998) Am. J. Respir. Cell Mol. Biol. , vol.19 , pp. 177
    • Crouch, E.C.1
  • 6
    • 0033983738 scopus 로고    scopus 로고
    • The roles of surfactant proteins A and D in innate immunity
    • Lawson, P. R., and K. B. Reid. 2000. The roles of surfactant proteins A and D in innate immunity. Immunol. Rev. 173:66.
    • (2000) Immunol. Rev. , vol.173 , pp. 66
    • Lawson, P.R.1    Reid, K.B.2
  • 7
    • 0028411525 scopus 로고
    • Lectin-mediated interactions of surfactant protein D with alveolar macrophages
    • Kuan, S. F., A. Persson, D. Parghi, and E. Crouch. 1994. Lectin-mediated interactions of surfactant protein D with alveolar macrophages. Am. J. Respir. Cell Mol. Biol. 10:430.
    • (1994) Am. J. Respir. Cell Mol. Biol. , vol.10 , pp. 430
    • Kuan, S.F.1    Persson, A.2    Parghi, D.3    Crouch, E.4
  • 9
    • 0026655080 scopus 로고
    • Specific binding of surfactant protein SP-A to rat alveolar macrophages
    • Pison, U., J. R. Wright, and S. Hawgood. 1992. Specific binding of surfactant protein SP-A to rat alveolar macrophages. Am. J. Physiol. 262:L412.
    • (1992) Am. J. Physiol. , vol.262
    • Pison, U.1    Wright, J.R.2    Hawgood, S.3
  • 12
    • 0028471364 scopus 로고
    • Aggregation and opsonization of type A but not type B Haemophilus influenzae by surfactant protein A
    • McNeely, T. B., and J. D. Coonrod. 1994. Aggregation and opsonization of type A but not type B Haemophilus influenzae by surfactant protein A. Am. J. Respir. Cell. Mol. Biol. 11:114.
    • (1994) Am. J. Respir. Cell. Mol. Biol. , vol.11 , pp. 114
    • McNeely, T.B.1    Coonrod, J.D.2
  • 13
    • 0030910697 scopus 로고    scopus 로고
    • SP-A enhances phagocytosis of Klebsiella by interaction with capsular polysaccharides and alveolar macrophages
    • Kabha, K., J. Schmegner, Y. Keisari, H. Parolis, J. Schlepper-Schaefer, and I. Ofek. 1997. SP-A enhances phagocytosis of Klebsiella by interaction with capsular polysaccharides and alveolar macrophages. Am. J. Physiol. 272:L344.
    • (1997) Am. J. Physiol. , vol.272
    • Kabha, K.1    Schmegner, J.2    Keisari, Y.3    Parolis, H.4    Schlepper-Schaefer, J.5    Ofek, I.6
  • 14
    • 85047690807 scopus 로고    scopus 로고
    • Surfactant proteins A and D inhibit the growth of Gram-negative bacteria by increasing membrane permeability
    • Wu, H., A. Kuzmenko, S. Wan, L. Schaffer, A. Weiss, J. Fisher, H., K. S. Kim, and F. X. McCormack. 2003. Surfactant proteins A and D inhibit the growth of Gram-negative bacteria by increasing membrane permeability. J. Clin. Invest. 111:1589.
    • (2003) J. Clin. Invest. , vol.111 , pp. 1589
    • Wu, H.1    Kuzmenko, A.2    Wan, S.3    Schaffer, L.4    Weiss, A.5    Fisher, J.6    Kim, K.S.7    McCormack, F.X.8
  • 20
    • 0033168699 scopus 로고    scopus 로고
    • Pulmonary surfactant protein A modulates the cellular responses to smooth and rough lipopolysaccharides by interactions with CD14
    • Sano, H., H. Sohma, T. Muta, S. Nomura, D. R. Voelker, and Y. Kuroki. 1999. Pulmonary surfactant protein A modulates the cellular responses to smooth and rough lipopolysaccharides by interactions with CD14. J. Immunol. 163:387.
    • (1999) J. Immunol. , vol.163 , pp. 387
    • Sano, H.1    Sohma, H.2    Muta, T.3    Nomura, S.4    Voelker, D.R.5    Kuroki, Y.6
  • 21
    • 0036510531 scopus 로고    scopus 로고
    • Surfactant protein A inhibits peptidoglycan-induced tumor necrosis factor-α secretion in U937 cells and alveolar macrophages by direct interaction with Toll-like receptor 2
    • Murakami, S., D. Iwaki, H. Mitsuzawa, H. Sano, H. Takahashi, D. R. Voelker, T. Akino, and Y. Kuroki. 2002. Surfactant protein A inhibits peptidoglycan-induced tumor necrosis factor-α secretion in U937 cells and alveolar macrophages by direct interaction with Toll-like receptor 2. J. Biol. Chem. 277:6830.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6830
    • Murakami, S.1    Iwaki, D.2    Mitsuzawa, H.3    Sano, H.4    Takahashi, H.5    Voelker, D.R.6    Akino, T.7    Kuroki, Y.8
  • 22
    • 0038205797 scopus 로고    scopus 로고
    • Direct binding of Toll-like receptor 2 to zymosan, and zymosan-induced NF-κB activation and TNF-α secretion are down-regulated by lung collectin surfactant protein A
    • Sato, M., H. Sano, D. Iwaki, K. Kudo, M. Konishi, H. Takahashi, T. Takahashi, H. Imaizumi, Y. Asai, and Y. Kuroki. 2003. Direct binding of Toll-like receptor 2 to zymosan, and zymosan-induced NF-κB activation and TNF-α secretion are down-regulated by lung collectin surfactant protein A. J. Immunol. 171:417.
    • (2003) J. Immunol. , vol.171 , pp. 417
    • Sato, M.1    Sano, H.2    Iwaki, D.3    Kudo, K.4    Konishi, M.5    Takahashi, H.6    Takahashi, T.7    Imaizumi, H.8    Asai, Y.9    Kuroki, Y.10
  • 23
    • 0141918823 scopus 로고    scopus 로고
    • By binding SIRPα or calreticulin/CD91, lung collectin act as dual function surveillance molecules to suppress or enhance inflammation
    • Gardai, S. J., Y.-Q. Xiao, M. Dickinson, J. A. Nick, D. R. Voelker, K. E. Greene, and P. H. Henson. 2003. By binding SIRPα or calreticulin/CD91, lung collectin act as dual function surveillance molecules to suppress or enhance inflammation. Cell 115:13.
    • (2003) Cell , vol.115 , pp. 13
    • 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.H.7
  • 24
    • 0028864127 scopus 로고
    • The variable surface glycolipids of mycobacteria: Structures, synthesis of epitopes and biological properties
    • Aspinall, G. O., D. Chattergee, and P. J. Brennan. 1995. The variable surface glycolipids of mycobacteria: structures, synthesis of epitopes and biological properties. Adv. Carbohydr. Chem. Biochem. 51:169.
    • (1995) Adv. Carbohydr. Chem. Biochem. , vol.51 , pp. 169
    • Aspinall, G.O.1    Chattergee, D.2    Brennan, P.J.3
  • 26
    • 0031050819 scopus 로고    scopus 로고
    • Structure, function and biogenesis of the mycobacterial cell wall
    • Brennan, P. J., and G. S. Besra. 1997. Structure, function and biogenesis of the mycobacterial cell wall. Biochem. Soc. Trans. 25:188.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 188
    • Brennan, P.J.1    Besra, G.S.2
  • 27
    • 0000939824 scopus 로고    scopus 로고
    • Immunopathogenesis of Mycobacterium avium infection
    • Cooper, A. M., R. Appelberg, and I. M. Orme. 1998. Immunopathogenesis of Mycobacterium avium infection. Front. Biosci. 3:141.
    • (1998) Front. Biosci. , vol.3 , pp. 141
    • Cooper, A.M.1    Appelberg, R.2    Orme, I.M.3
  • 28
    • 0034548139 scopus 로고    scopus 로고
    • Regulation of Toll-like receptor 2 expression by macrophages following Mycobacterium avium infection
    • Wang, T., W. P. Lafuse, and B. S. Zwilling. 2000. Regulation of Toll-like receptor 2 expression by macrophages following Mycobacterium avium infection. J. Immunol. 165:6308.
    • (2000) J. Immunol. , vol.165 , pp. 6308
    • Wang, T.1    Lafuse, W.P.2    Zwilling, B.S.3
  • 29
    • 0344407007 scopus 로고    scopus 로고
    • Surfactant protein A decreases nitric oxide production by macrophages in a tumor necrosis factor-α-dependent mechanism
    • Hussain, S., J. R. Wright, and W. J. Martin II. 2003. Surfactant protein A decreases nitric oxide production by macrophages in a tumor necrosis factor-α-dependent mechanism. Am. J. Respir. Cell Mol. Biol. 28:520.
    • (2003) Am. J. Respir. Cell Mol. Biol. , vol.28 , pp. 520
    • Hussain, S.1    Wright, J.R.2    Martin II, W.J.3
  • 30
    • 0028832349 scopus 로고
    • Pulmonary surfactant protein A mediates enhanced phagocytosis of Mycobacterium tuberculosis by a direct interaction with human macrophages
    • Gaynor, C. D., F. X. McCormack, D. R. Voelker, S. E. McGowan, and L. S. Schlesinger. 1995. Pulmonary surfactant protein A mediates enhanced phagocytosis of Mycobacterium tuberculosis by a direct interaction with human macrophages. J. Immunol. 155:5343.
    • (1995) J. Immunol. , vol.155 , pp. 5343
    • Gaynor, C.D.1    McCormack, F.X.2    Voelker, D.R.3    McGowan, S.E.4    Schlesinger, L.S.5
  • 31
    • 0034723272 scopus 로고    scopus 로고
    • Lipoglycans are putative ligands for the human pulmonary surfactant protein A attachment to mycobacteria: Critical role of the lipids for lectin-carbohydrate recognition
    • Sidobre, S., J. Nigou, G. Puzo, and M. Riviere. 2000. Lipoglycans are putative ligands for the human pulmonary surfactant protein A attachment to mycobacteria: critical role of the lipids for lectin-carbohydrate recognition. J. Biol. Chem. 275:2415.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2415
    • Sidobre, S.1    Nigou, J.2    Puzo, G.3    Riviere, M.4
  • 32
    • 0036784647 scopus 로고    scopus 로고
    • Pulmonary surfactant protein A up-regulates activity of the mannose receptor, a pattern recognition receptor expressed on human macrophages
    • Beharka, A. A., C. D. Gaynor, B. K. Kang, D. R. Voelker, F. X. McCormack, and L. S. Schlesinger. 2002. Pulmonary surfactant protein A up-regulates activity of the mannose receptor, a pattern recognition receptor expressed on human macrophages. J. Immunol. 169:3565.
    • (2002) J. Immunol. , vol.169 , pp. 3565
    • Beharka, A.A.1    Gaynor, C.D.2    Kang, B.K.3    Voelker, D.R.4    McCormack, F.X.5    Schlesinger, L.S.6
  • 33
    • 0033168175 scopus 로고    scopus 로고
    • Surfactant protein D binds to Mycobacterium tuberculosis bacilli and lipoarabinomannan via carbohydrate-lectin interactions resulting in reduced phagocytosis of the bacteria by macrophages
    • Ferguson, J. S., D. R. Voelker, F. X. McCormack, and L. S. Schlesinger. 1999. Surfactant protein D binds to Mycobacterium tuberculosis bacilli and lipoarabinomannan via carbohydrate-lectin interactions resulting in reduced phagocytosis of the bacteria by macrophages. J. Immunol. 163:312.
    • (1999) J. Immunol. , vol.163 , pp. 312
    • Ferguson, J.S.1    Voelker, D.R.2    McCormack, F.X.3    Schlesinger, L.S.4
  • 34
    • 0036467562 scopus 로고    scopus 로고
    • Surfactant protein D inhibition of human macrophage uptake of Mycobacterium tuberculosis is independent of bacterial agglutination
    • Ferguson, J. S., D. R. Voelker, J. A. Ufnar, A. J. Dawson, and L. S. Schlesinger. 2002. Surfactant protein D inhibition of human macrophage uptake of Mycobacterium tuberculosis is independent of bacterial agglutination. J. Immunol. 168:1309.
    • (2002) J. Immunol. , vol.168 , pp. 1309
    • Ferguson, J.S.1    Voelker, D.R.2    Ufnar, J.A.3    Dawson, A.J.4    Schlesinger, L.S.5
  • 35
    • 0025799690 scopus 로고
    • Surfactant protein D (SP-D) counteracts the inhibitory effect of surfactant protein A (SP-A) on phospholipid secretion by alveolar type II cells. Interaction of native SP-D with SP-A
    • Kuroki, Y., M. Shiratori, Y. Murata, and T. Akino. 1991. Surfactant protein D (SP-D) counteracts the inhibitory effect of surfactant protein A (SP-A) on phospholipid secretion by alveolar type II cells. Interaction of native SP-D with SP-A. Biochem. J. 279:115.
    • (1991) Biochem. J. , vol.279 , pp. 115
    • Kuroki, Y.1    Shiratori, M.2    Murata, Y.3    Akino, T.4
  • 36
    • 0027418167 scopus 로고
    • Elevated levels of lung surfactant protein A in sera from patients with idiopathic pulmonary fibrosis and pulmonary alveolar proteinosis
    • Kuroki, Y., S. Tsutahara, N. Shijubo, H. Takahashi, M. Shiratori, A. Hattori, Y. Honda, S. Abe, and T. Akino. 1993. Elevated levels of lung surfactant protein A in sera from patients with idiopathic pulmonary fibrosis and pulmonary alveolar proteinosis. Am. Rev. Respir. Dis. 147:723.
    • (1993) Am. Rev. Respir. Dis. , vol.147 , pp. 723
    • Kuroki, Y.1    Tsutahara, S.2    Shijubo, N.3    Takahashi, H.4    Shiratori, M.5    Hattori, A.6    Honda, Y.7    Abe, S.8    Akino, T.9
  • 37
    • 0022475802 scopus 로고
    • Induction of intra- and extra-cellular phospholipids in the lungs of rats exposed to silica
    • Dethloff, L. A., L. B. Gilmore, A. R. Brody, and G. E. R. Hook. 1986. Induction of intra- and extra-cellular phospholipids in the lungs of rats exposed to silica. Biochem. J. 233:111.
    • (1986) Biochem. J. , vol.233 , pp. 111
    • Dethloff, L.A.1    Gilmore, L.B.2    Brody, A.R.3    Hook, G.E.R.4
  • 38
    • 0023759627 scopus 로고
    • Alveolar type II cells express a high-affinity receptor for pulmonary surfactant protein A
    • Kuroki, Y., R. J. Mason, and D. R. Voelker. 1988. Alveolar type II cells express a high-affinity receptor for pulmonary surfactant protein A. Proc. Natl. Acad. Sci. USA 85:5566.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5566
    • Kuroki, Y.1    Mason, R.J.2    Voelker, D.R.3
  • 39
    • 0027970082 scopus 로고
    • 197 are essential for receptor binding, phospholipid aggregation, regulation of secretion, and the facilitated uptake of phospholipid by type II cells
    • 197 are essential for receptor binding, phospholipid aggregation, regulation of secretion, and the facilitated uptake of phospholipid by type II cells. J. Biol. Chem. 269:29801.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29801
    • McCormack, F.X.1    Kuroki, Y.2    Stewart, J.J.3    Mason, R.J.4    Voelker, D.R.5
  • 40
    • 0033151764 scopus 로고    scopus 로고
    • Introduction of mannose-binding protein-type phosphatidylinositol recognition into pulmonary surfactant protein A
    • Chiba, H., H. Sano, M. Saitoh, H. Sohma, D. R. Voelker, T. Akino, and Y. Kuroki. 1999. Introduction of mannose-binding protein-type phosphatidylinositol recognition into pulmonary surfactant protein A. Biochemistry 38:7321.
    • (1999) Biochemistry , vol.38 , pp. 7321
    • Chiba, H.1    Sano, H.2    Saitoh, M.3    Sohma, H.4    Voelker, D.R.5    Akino, T.6    Kuroki, Y.7
  • 41
    • 0029964034 scopus 로고    scopus 로고
    • Surfactant protein A stimulates phagocytosis of specific pulmonary pathogens by alveolar macrophages
    • Tino, M. J., and J. R. Wright. 1996. Surfactant protein A stimulates phagocytosis of specific pulmonary pathogens by alveolar macrophages. Am. J. Physiol. 270: L677.
    • (1996) Am. J. Physiol. , vol.270
    • Tino, M.J.1    Wright, J.R.2
  • 42
    • 0035830893 scopus 로고    scopus 로고
    • Variation in mannose-capped terminal arabinan motifs of lipoarabinomannans from clinical isolates of Mycobacterium tuberculosis and Mycobacterium avium complex
    • Khoo, K.-H., J.-B. Tang, and D. Chatterjee. 2001. Variation in mannose-capped terminal arabinan motifs of lipoarabinomannans from clinical isolates of Mycobacterium tuberculosis and Mycobacterium avium complex. J. Biol. Chem. 276:3863.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3863
    • Khoo, K.-H.1    Tang, J.-B.2    Chatterjee, D.3
  • 44
    • 0027943406 scopus 로고
    • Epitope mapping for monoclonal antibodies identified functional domains of pulmonary surfactant protein A that interact with lipids
    • Kuroki, Y., F. X. McCormack, Y. Ogasawara, R. J. Mason, and D. R. Voelker. 1994. Epitope mapping for monoclonal antibodies identified functional domains of pulmonary surfactant protein A that interact with lipids. J. Biol. Chem. 269:29793.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29793
    • Kuroki, Y.1    McCormack, F.X.2    Ogasawara, Y.3    Mason, R.J.4    Voelker, D.R.5
  • 45
    • 0023857603 scopus 로고
    • Pulmonary surfactant apoprotein A structure and modulation of surfactant secretion by rat alveolar type II cells
    • Kuroki, Y., R. J. Mason, and D. R. Voelker. 1988. Pulmonary surfactant apoprotein A structure and modulation of surfactant secretion by rat alveolar type II cells. J. Biol. Chem. 263:3388.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3388
    • Kuroki, Y.1    Mason, R.J.2    Voelker, D.R.3
  • 46
    • 0027173039 scopus 로고
    • Macrophage phagocytosis of virulent but not attenuated strains of Mycobacterium tuberculosis is mediated by mannose receptors in addition to complement receptors
    • Schlesinger, L. S. 1993. Macrophage phagocytosis of virulent but not attenuated strains of Mycobacterium tuberculosis is mediated by mannose receptors in addition to complement receptors. J. Immunol. 150:2920.
    • (1993) J. Immunol. , vol.150 , pp. 2920
    • Schlesinger, L.S.1
  • 47
    • 0020471629 scopus 로고
    • Expression of a mannosyl-fucosyl receptor for endocytosis on cultured primary macrophages and their hybrids
    • Stahl, P., and S. Gordon. 1982. Expression of a mannosyl-fucosyl receptor for endocytosis on cultured primary macrophages and their hybrids. J. Cell Biol. 93:49.
    • (1982) J. Cell Biol. , vol.93 , pp. 49
    • Stahl, P.1    Gordon, S.2
  • 48
    • 0020661782 scopus 로고
    • Yeast mannans inhibit binding and phagocytosis of zymosan by mouse peritoneal macrophages
    • Sung, S. S., R. S. Nelson, and S. C. Silverstein. 1983. Yeast mannans inhibit binding and phagocytosis of zymosan by mouse peritoneal macrophages. J. Cell Biol. 96:160.
    • (1983) J. Cell Biol. , vol.96 , pp. 160
    • Sung, S.S.1    Nelson, R.S.2    Silverstein, S.C.3
  • 49
    • 0033046220 scopus 로고    scopus 로고
    • Mechanisms of phagocytosis in macrophages
    • Aderem, A., and D. M. Underhill. 1999. Mechanisms of phagocytosis in macrophages. Annu. Rev. Immunol. 17:593.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 593
    • Aderem, A.1    Underhill, D.M.2
  • 50
    • 0025216480 scopus 로고
    • Phagocytosis of Mycobacterium tuberculosis is mediated by human monocyte complement receptors and complement component C3
    • Schlesinger, L. S., C. G. Bellinger-Kawahara, N. R. Payne, and M. A. Horwitz. 1990. Phagocytosis of Mycobacterium tuberculosis is mediated by human monocyte complement receptors and complement component C3. J. Immunol. 144:2771.
    • (1990) J. Immunol. , vol.144 , pp. 2771
    • Schlesinger, L.S.1    Bellinger-Kawahara, C.G.2    Payne, N.R.3    Horwitz, M.A.4
  • 51
    • 0027137823 scopus 로고
    • Mycobacteria-macrophage interactions. Macrophage phenotype determines the non-opsonic binding of Mycobacterium tuberculosis to murine macrophages
    • Stokes, R. W., I. D. Haidl, W. A. Jefferies, and D. P. Speert. 1993. Mycobacteria-macrophage interactions. Macrophage phenotype determines the non-opsonic binding of Mycobacterium tuberculosis to murine macrophages. J. Immunol. 151:7067.
    • (1993) J. Immunol. , vol.151 , pp. 7067
    • Stokes, R.W.1    Haidl, I.D.2    Jefferies, W.A.3    Speert, D.P.4
  • 52
    • 0030331770 scopus 로고    scopus 로고
    • Selective receptor blockade during phagocytosis does not alter the survival and growth of Mycobacterium tuberculosis in human macrophages
    • Zimmerrli, S., S. Edwards, and J. D. Ernst. 1996. Selective receptor blockade during phagocytosis does not alter the survival and growth of Mycobacterium tuberculosis in human macrophages. Am. J. Respir. Cell Mol. Biol. 15:760.
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.15 , pp. 760
    • Zimmerrli, S.1    Edwards, S.2    Ernst, J.D.3
  • 53
    • 0021989909 scopus 로고
    • A β-glucan inhibitable receptor on human monocytes: Its identity with the phagocytic receptor for particulate activators of the alternative complement pathway
    • Czop, J. K., and K. F. Austen. 1985. A β-glucan inhibitable receptor on human monocytes: its identity with the phagocytic receptor for particulate activators of the alternative complement pathway. J. Immunol. 134:2588.
    • (1985) J. Immunol. , vol.134 , pp. 2588
    • Czop, J.K.1    Austen, K.F.2
  • 54
    • 0027787943 scopus 로고
    • Both mannose and β-glucan receptors are involved in phagocytosis of unopsonized, heat-killed Saccharomyces cerevisiae by murine macrophages
    • Giaimis, L., P. Lombard, P. Fonteneau, C. D. Muller, R. Levy, M. Mukaya-Kumba, J. Lazdin, and P. Poindron. 1993. Both mannose and β-glucan receptors are involved in phagocytosis of unopsonized, heat-killed Saccharomyces cerevisiae by murine macrophages. J. Leukocyte Biol. 54:564.
    • (1993) J. Leukocyte Biol. , vol.54 , pp. 564
    • Giaimis, L.1    Lombard, P.2    Fonteneau, P.3    Muller, C.D.4    Levy, R.5    Mukaya-Kumba, M.6    Lazdin, J.7    Poindron, P.8
  • 55
    • 0020661782 scopus 로고
    • Yeast mannans inhibit binding and phagocytosis of zymosan by mouse peritoneal macrophages
    • Sung, S. S., R. S. Nelson, and S. C. Silverstein. 1983. Yeast mannans inhibit binding and phagocytosis of zymosan by mouse peritoneal macrophages. J. Cell Biol. 96:160.
    • (1983) J. Cell Biol. , vol.96 , pp. 160
    • Sung, S.S.1    Nelson, R.S.2    Silverstein, S.C.3
  • 57
    • 0024215606 scopus 로고
    • Chemical modification of surfactant protein A alters high affinity binding to rat alveolar type II cells and regulation of phospholipid secretion
    • Kuroki, Y., R. J. Mason, and D. R. Voelker. 1988. Chemical modification of surfactant protein A alters high affinity binding to rat alveolar type II cells and regulation of phospholipid secretion. J. Biol. Chem. 263:17596.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17596
    • Kuroki, Y.1    Mason, R.J.2    Voelker, D.R.3
  • 58
    • 0024511029 scopus 로고
    • Biosynthesis and processing of the mannose receptor in human macrophages
    • Lennartz, M. R., F. S. Cole, and P. D. Stahl. 1989. Biosynthesis and processing of the mannose receptor in human macrophages. J. Biol. Chem. 264:2385.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2385
    • Lennartz, M.R.1    Cole, F.S.2    Stahl, P.D.3
  • 59
    • 0021251432 scopus 로고
    • Monensin inhibits recycling of macrophage mannose-glycoprotein receptors and ligand delivery to lysosomes
    • Wileman, T., R. L. Boshans, P. Schlesinger, and P. Stahl. 1984. Monensin inhibits recycling of macrophage mannose-glycoprotein receptors and ligand delivery to lysosomes. Biochem. J. 220:665.
    • (1984) Biochem. J. , vol.220 , pp. 665
    • Wileman, T.1    Boshans, R.L.2    Schlesinger, P.3    Stahl, P.4
  • 60
    • 0025735185 scopus 로고
    • Increased recovery of surfactant protein A in AIDS-related pneumonia
    • Phelps, D. S., and R. M. Rose. 1991. Increased recovery of surfactant protein A in AIDS-related pneumonia. Am. Rev. Respir. Dis. 143:1072.
    • (1991) Am. Rev. Respir. Dis. , vol.143 , pp. 1072
    • Phelps, D.S.1    Rose, R.M.2
  • 61
    • 0029035691 scopus 로고
    • Surfactant protein A promotes attachment of Mycobacterium tuberculosis to alveolar macrophages during infection with human immunodeficiency virus
    • Downing, J. F., R. Pasula, J. R. Wright, H. L. Twigg III, and W. J. Martin, II. 1995. Surfactant protein A promotes attachment of Mycobacterium tuberculosis to alveolar macrophages during infection with human immunodeficiency virus. Proc. Natl. Acad. Sci. USA 92:4848.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4848
    • Downing, J.F.1    Pasula, R.2    Wright, J.R.3    Twigg III, H.L.4    Martin II, W.J.5


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