메뉴 건너뛰기




Volumn 169, Issue 9, 2002, Pages 5270-5278

CD11b/CD18-dependent interactions of neutrophils with intestinal epithelium are mediated by fucosylated proteoglycans

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LEVO FUCOSIDASE; BINDING PROTEIN; CARBOHYDRATE; CATION; CD11B ANTIGEN; CD18 ANTIGEN; FUCOIDIN; HEPARAN SULFATE; HEPARIN; LAMINARAN; LIGAND; MANNOSE 6 PHOSPHATE; N ACETYLGLUCOSAMINE; PROTEOGLYCAN; PYRANOSIDE; SIALIDASE;

EID: 0036839560     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.169.9.5270     Document Type: Article
Times cited : (84)

References (54)
  • 1
    • 0019942731 scopus 로고
    • The histopathologic spectrum of acute self-limited colitis (acute infectious-type colitis)
    • Kumar, N. B., T. T. Nostrant, and H. D. Appelman. 1982. The histopathologic spectrum of acute self-limited colitis (acute infectious-type colitis). Am. J. Surg. Pathol. 6:523.
    • (1982) Am. J. Surg. Pathol. , vol.6 , pp. 523
    • Kumar, N.B.1    Nostrant, T.T.2    Appelman, H.D.3
  • 2
    • 0018826448 scopus 로고
    • Electrolyte transport across colonic mucosa from patients with inflammatory bowel disease
    • Hawker, P. C., J. S. McKay, and L. A. Turnberg. 1980. Electrolyte transport across colonic mucosa from patients with inflammatory bowel disease. Gastroenterology. 79:508.
    • (1980) Gastroenterology , vol.79 , pp. 508
    • Hawker, P.C.1    McKay, J.S.2    Turnberg, L.A.3
  • 3
    • 0029764610 scopus 로고    scopus 로고
    • Expression and polarization of intercellular adhesion molecule-1 on human intestinal epithelia: Consequences for CD11b/CD18-mediated interactions with neutrophils
    • Parkos, C. A., S. P. Colgan, M. S. Diamond, A. Nusrat, T. W. Liang, T. A. Springer, and J. L. Madara. 1996. Expression and polarization of intercellular adhesion molecule-1 on human intestinal epithelia: Consequences for CD11b/CD18-mediated interactions with neutrophils. Mol. Med. 2:489.
    • (1996) Mol. Med. , vol.2 , pp. 489
    • Parkos, C.A.1    Colgan, S.P.2    Diamond, M.S.3    Nusrat, A.4    Liang, T.W.5    Springer, T.A.6    Madara, J.L.7
  • 4
    • 0029059578 scopus 로고
    • A binding interface on the I domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1)
    • Huang, C., and T. A. Springer. 1995. A binding interface on the I domain of lymphocyte function-associated antigen-1 (LFA-1) required for specific interaction with intercellular adhesion molecule 1 (ICAM-1). J. Biol. Chem. 270:19008.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19008
    • Huang, C.1    Springer, T.A.2
  • 5
    • 0027483226 scopus 로고
    • 2 integrin CR3 (CD11b/CD18) is essential for ligand binding
    • 2 integrin CR3 (CD11b/CD18) is essential for ligand binding. Cell 72:857.
    • (1993) Cell , vol.72 , pp. 857
    • Michishita, M.1    Vidern, V.2    Arnaout, M.A.3
  • 6
    • 0027530684 scopus 로고
    • The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands
    • Diamond, M. S., J. Garcia-Aguilar, J. K. Bickford, A. L. Corbi, and T. A. Springer. 1993. The I domain is a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands. J. Cell Biol. 120:1031.
    • (1993) J. Cell Biol. , vol.120 , pp. 1031
    • Diamond, M.S.1    Garcia-Aguilar, J.2    Bickford, J.K.3    Corbi, A.L.4    Springer, T.A.5
  • 7
    • 0345552244 scopus 로고    scopus 로고
    • The β-glucan-binding lectin site of mouse CR3 (CD11b/CD18) and its function in generating a primed state of the receptor that mediates cytotoxic activation in response to iC3b-opsonized target cells
    • Xia, Y., V. Vetvicka, J. Yan, M. Hanikyrova, T. Mayadas, and G. D. Ross. 1999. The β-glucan-binding lectin site of mouse CR3 (CD11b/CD18) and its function in generating a primed state of the receptor that mediates cytotoxic activation in response to iC3b-opsonized target cells. J. Immunol 162:2281.
    • (1999) J. Immunol. , vol.162 , pp. 2281
    • Xia, Y.1    Vetvicka, V.2    Yan, J.3    Hanikyrova, M.4    Mayadas, T.5    Ross, G.D.6
  • 9
    • 0028265846 scopus 로고
    • The leukocyte integrin p150,95 (CD11c/CD18) as a receptor for iC3b: Activation by a heterologous β subunit and localization of a ligand recognition site to the I domain
    • Bilsland, C. A., M. S. Diamond, and T. A. Springer. 1994. The leukocyte integrin p150,95 (CD11c/CD18) as a receptor for iC3b: Activation by a heterologous β subunit and localization of a ligand recognition site to the I domain. J. Immunol. 152:4582.
    • (1994) J. Immunol. , vol.152 , pp. 4582
    • Bilsland, C.A.1    Diamond, M.S.2    Springer, T.A.3
  • 10
    • 0019953149 scopus 로고
    • Anti-Mac-1 selectively inhibits the mouse and human type three complement receptor
    • Beller, D. I., T. A. Springer, and R. D. Schreiber. 1982. Anti-Mac-1 selectively inhibits the mouse and human type three complement receptor. J. Exp. Med. 156:1000.
    • (1982) J. Exp. Med. , vol.156 , pp. 1000
    • Beller, D.I.1    Springer, T.A.2    Schreiber, R.D.3
  • 11
    • 0025283473 scopus 로고
    • A unique recognition site mediates the interaction of fibrinogen with the leukocyte integrin Mac-1 (CD11b/CD18)
    • Altieri, D. C., F. R. Agbanyo, J. Plescia, M. H. Ginsberg, T. S. Edgington, and E. F. Plow. 1990. A unique recognition site mediates the interaction of fibrinogen with the leukocyte integrin Mac-1 (CD11b/CD18). J. Biol. Chem. 265:12119.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12119
    • Altieri, D.C.1    Agbanyo, F.R.2    Plescia, J.3    Ginsberg, M.H.4    Edgington, T.S.5    Plow, E.F.6
  • 12
    • 0033109382 scopus 로고    scopus 로고
    • Role of very late adhesion integrins in mediating repair of human airway epithelial cell monolayers after mechanical injury
    • White, S. R., D. R. Dorscheid, K. F. Rabe, K. R. Wojcik, and K. J. Hamann. 1999. Role of very late adhesion integrins in mediating repair of human airway epithelial cell monolayers after mechanical injury. Am. J. Respir. Cell Mol. Biol. 20:787.
    • (1999) Am. J. Respir. Cell Mol. Biol. , vol.20 , pp. 787
    • White, S.R.1    Dorscheid, D.R.2    Rabe, K.F.3    Wojcik, K.R.4    Hamann, K.J.5
  • 14
    • 0029961891 scopus 로고    scopus 로고
    • 2) and modulates polymorphonuclear leukocyte adhesion
    • 2) and modulates polymorphonuclear leukocyte adhesion. J. Exp. Med. 184:1213.
    • (1996) J. Exp. Med. , vol.184 , pp. 1213
    • Cai, T.Q.1    Wright, S.D.2
  • 16
    • 0022003293 scopus 로고
    • Membrane complement receptor type three (CR3) has lectin-like properties analogous to bovine conglutinin as functions as a receptor for zymosan and rabbit erythrocytes as well as a receptor for iC3b
    • Ross, G. D., J. A. Cain, and P. J. Lachmann. 1985. Membrane complement receptor type three (CR3) has lectin-like properties analogous to bovine conglutinin as functions as a receptor for zymosan and rabbit erythrocytes as well as a receptor for iC3b. J. Immunol. 134:3307.
    • (1985) J. Immunol. , vol.134 , pp. 3307
    • Ross, G.D.1    Cain, J.A.2    Lachmann, P.J.3
  • 17
    • 0345281592 scopus 로고    scopus 로고
    • β-glucan, a "specific" biologic response modifier that uses antibodies to target tumors for cytotoxic recognition by leukocyte complement receptor type 3 (CD11b/CD18)
    • Yan, J., V. Vetvicka, Y. Xia, A. Coxon, M. C. Carroll, T. N. Mayadas, and G. D. Ross. 1999. β-glucan, a "specific" biologic response modifier that uses antibodies to target tumors for cytotoxic recognition by leukocyte complement receptor type 3 (CD11b/CD18). J. Immunol. 163:3045.
    • (1999) J. Immunol. , vol.163 , pp. 3045
    • Yan, J.1    Vetvicka, V.2    Xia, Y.3    Coxon, A.4    Carroll, M.C.5    Mayadas, T.N.6    Ross, G.D.7
  • 18
    • 0029166397 scopus 로고
    • Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD1)
    • Diamond, M. S., R. Alon, C. A. Parkos, M. T. Quinn, and T. A. Springer. 1995. Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD1). J. Cell Biol. 130:1473.
    • (1995) J. Cell Biol. , vol.130 , pp. 1473
    • Diamond, M.S.1    Alon, R.2    Parkos, C.A.3    Quinn, M.T.4    Springer, T.A.5
  • 20
    • 0026554217 scopus 로고
    • 3 binds to denatured collagen type I through RGD sites
    • 3 binds to denatured collagen type I through RGD sites. Biochem. Biophys. Res. Commun. 182:1025.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1025
    • Davis, G.E.1
  • 21
    • 0028557171 scopus 로고
    • 2 integrin CR3 (CD11b/CD18) is a receptor for the hookworm-derived neutrophil adhesion inhibitor NIF
    • 2 integrin CR3 (CD11b/CD18) is a receptor for the hookworm-derived neutrophil adhesion inhibitor NIF. J. Cell Biol. 127:2081.
    • (1994) J. Cell Biol. , vol.127 , pp. 2081
    • Rieu, P.1    Ueda, T.2    Haruta, I.3    Sharma, C.P.4    Arnaout, M.A.5
  • 24
    • 0028920183 scopus 로고
    • Carbohydrate recognition by a natural killer cell receptor, Ly-49C
    • Brennan, J., F. Takei, S. Wong, and D. L. Mager. 1995. Carbohydrate recognition by a natural killer cell receptor, Ly-49C. J. Biol. Chem. 270:9691.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9691
    • Brennan, J.1    Takei, F.2    Wong, S.3    Mager, D.L.4
  • 25
    • 0032525025 scopus 로고    scopus 로고
    • Functional mapping of CD11b/CD18 epitopes important in neutrophil-epithelial interactions: A central role of the I domain
    • Balsam, L. B., T. W. Liang, and C. A. Parkos. 1998. Functional mapping of CD11b/CD18 epitopes important in neutrophil-epithelial interactions: A central role of the I domain. J. Immunol. 160:5058.
    • (1998) J. Immunol. , vol.160 , pp. 5058
    • Balsam, L.B.1    Liang, T.W.2    Parkos, C.A.3
  • 26
    • 0035955676 scopus 로고    scopus 로고
    • The role of CD47 in neutrophil transmigration. Increased rate of migration correlates with increased cell surface expression of CD47
    • Liu, Y., D. Merlin, S. L. Burst, M. Pochet, J. L. Madara, and C. A. Parkos. 2001. The role of CD47 in neutrophil transmigration. Increased rate of migration correlates with increased cell surface expression of CD47. J. Biol. Chem. 276:40156.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40156
    • Liu, Y.1    Merlin, D.2    Burst, S.L.3    Pochet, M.4    Madara, J.L.5    Parkos, C.A.6
  • 27
    • 0017531151 scopus 로고
    • Solvolytic desulfation of glycosaminoglycuronan sulfates with dimethyl sulfoxide containing water or methanol
    • Nagasawa, K., Y. Inoue, and T. Kamata. 1977. Solvolytic desulfation of glycosaminoglycuronan sulfates with dimethyl sulfoxide containing water or methanol. Carbohydrate Res. 58:47.
    • (1977) Carbohydrate Res. , vol.58 , pp. 47
    • Nagasawa, K.1    Inoue, Y.2    Kamata, T.3
  • 28
    • 0023694713 scopus 로고
    • Detection of receptors for sulfated polysaccharides in human placenta by biotinylated probes
    • Debbage, P. L., W. Lange, T. Hellmann. and H. J. Gabius. 1988. Detection of receptors for sulfated polysaccharides in human placenta by biotinylated probes. J. Histochem. Cytochem. 36:1097.
    • (1988) J. Histochem. Cytochem. , vol.36 , pp. 1097
    • Debbage, P.L.1    Lange, W.2    Hellmann, T.3    Gabius, H.J.4
  • 29
    • 0035799385 scopus 로고    scopus 로고
    • Screening of a unique lectin from 16 cultivable mushrooms with hybrid glycoprotein and neoproteoglycan probes and purification of a novel N-acetylglucosamine-specific lectin from Oudemansiella platyphylla fruiting body
    • Matsumoto, H., A. Natsume, H. Ueda, T. Saitoh, and H. Ogawa. 2001. Screening of a unique lectin from 16 cultivable mushrooms with hybrid glycoprotein and neoproteoglycan probes and purification of a novel N-acetylglucosamine-specific lectin from Oudemansiella platyphylla fruiting body. Biochim. Biophys. Acta 1526:(37.
    • (2001) Biochim. Biophys. Acta , vol.1526 , pp. 37
    • Matsumoto, H.1    Natsume, A.2    Ueda, H.3    Saitoh, T.4    Ogawa, H.5
  • 30
    • 0033728311 scopus 로고    scopus 로고
    • Identification of perivitelline N-linked glycans as mediators of sperm-egg interaction in chickens
    • Robertson, L., G. J. Wishart, and A. J. Horrocks. 2000. Identification of perivitelline N-linked glycans as mediators of sperm-egg interaction in chickens. J. Reprod. Fertil. 120:397.
    • (2000) J. Reprod. Fertil. , vol.120 , pp. 397
    • Robertson, L.1    Wishart, G.J.2    Horrocks, A.J.3
  • 31
    • 0033556022 scopus 로고    scopus 로고
    • A toxoplasma lectin-like activity specific for sulfated polysaccharides is involved in host cell infection
    • Ortega-Barria, E., and J. C. Boothroyd. 1999. A toxoplasma lectin-like activity specific for sulfated polysaccharides is involved in host cell infection. J. Biol. Chem. 274:1267.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1267
    • Ortega-Barria, E.1    Boothroyd, J.C.2
  • 33
    • 0026321583 scopus 로고
    • Different action of heparin and fucoidan on arterial smooth muscle cell proliferation and thrombospondin and fibronectin metabolism
    • Vischer, P., and E. Buddecke. 1991. Different action of heparin and fucoidan on arterial smooth muscle cell proliferation and thrombospondin and fibronectin metabolism. Eur. J. Cell Biol. 56:407.
    • (1991) Eur. J. Cell Biol. , vol.56 , pp. 407
    • Vischer, P.1    Buddecke, E.2
  • 34
    • 0023656421 scopus 로고
    • Polysaccharide structural features that are critical for the binding of sulfated fucans to bindin, the adhesive protein from sea urchin sperm
    • DeAngelis, P. L., and C. G. Glabe. 1987. Polysaccharide structural features that are critical for the binding of sulfated fucans to bindin, the adhesive protein from sea urchin sperm. J. Biol. Chem. 262:13946.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13946
    • DeAngelis, P.L.1    Glabe, C.G.2
  • 35
    • 0033041119 scopus 로고    scopus 로고
    • Characterization of cell surface lectin-binding patterns of human airway epithelium
    • Dorscheid, D. R., A. E. Conforti, K. J. Hamann, K. F. Rabe, and S. R. White. 1999. Characterization of cell surface lectin-binding patterns of human airway epithelium. Histochem. J. 31:145.
    • (1999) Histochem. J. , vol.31 , pp. 145
    • Dorscheid, D.R.1    Conforti, A.E.2    Hamann, K.J.3    Rabe, K.F.4    White, S.R.5
  • 36
  • 37
    • 0031260175 scopus 로고    scopus 로고
    • Molecular events in neutrophil transepithelial migration
    • Parkos, C. A. 1997. Molecular events in neutrophil transepithelial migration. BioEssays 19:865.
    • (1997) BioEssays , vol.19 , pp. 865
    • Parkos, C.A.1
  • 38
    • 0030836869 scopus 로고    scopus 로고
    • Cell adhesion and migration. I. Neutrophil adhesive interactions with intestinal epithelium
    • Parkos, C. A. 1997. Cell adhesion and migration. I. Neutrophil adhesive interactions with intestinal epithelium. Am. J. Physiol. 273:G763.
    • (1997) Am. J. Physiol. , vol.273
    • Parkos, C.A.1
  • 39
    • 0025723465 scopus 로고
    • Neutrophil migration across a cultured intestinal epithelium: Dependence on a CD11b/CD18-mediated event and enhanced efficiency in physiological direction
    • Parkos, C. A., C. Delp, M. A. Arnaout, and J. L. Madara. 1991. Neutrophil migration across a cultured intestinal epithelium: Dependence on a CD11b/CD18-mediated event and enhanced efficiency in physiological direction. J. Clin. Invest. 88:1605.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1605
    • Parkos, C.A.1    Delp, C.2    Arnaout, M.A.3    Madara, J.L.4
  • 40
    • 0030027828 scopus 로고    scopus 로고
    • Fucoidin, a potent inhibitor of leukocyte rolling, prevents neutrophil influx into phorbol-ester-induced inflammatory sites in rabbit lungs
    • Shimaoka, M., M. Ikeda, T. Iida, N. Taenaka, I. Yoshiya, and T. Honda. 1996. Fucoidin, a potent inhibitor of leukocyte rolling, prevents neutrophil influx into phorbol-ester-induced inflammatory sites in rabbit lungs. Am. J. Respir. Crit. Care Med. 153:307.
    • (1996) Am. J. Respir. Crit. Care Med. , vol.153 , pp. 307
    • Shimaoka, M.1    Ikeda, M.2    Iida, T.3    Taenaka, N.4    Yoshiya, I.5    Honda, T.6
  • 41
    • 0028223988 scopus 로고
    • Inhibition of leukocyte rolling with polysaccharide fucoidin prevents pleocytosis in experimental meningitis in the rabbit
    • Granert, C., J. Raud, X. Xie, L. Lindquist, and L. Lindbom. 1994. Inhibition of leukocyte rolling with polysaccharide fucoidin prevents pleocytosis in experimental meningitis in the rabbit. J. Clin. Invest. 93:929.
    • (1994) J. Clin. Invest. , vol.93 , pp. 929
    • Granert, C.1    Raud, J.2    Xie, X.3    Lindquist, L.4    Lindbom, L.5
  • 42
    • 0034649264 scopus 로고    scopus 로고
    • Heparin also interacts with selectins and modulates the cell adhesion process
    • Yanaka, K., N. Kato, and T. Nose. 2000. Heparin also interacts with selectins and modulates the cell adhesion process. Circulation 102:E169.
    • (2000) Circulation , vol.102
    • Yanaka, K.1    Kato, N.2    Nose, T.3
  • 43
    • 0033166496 scopus 로고    scopus 로고
    • Identification of human complement factor H as a ligand for L-selectin
    • Malhotra, R., M. Ward, R. B. Sim, and M. I. Bird. 1999. Identification of human complement factor H as a ligand for L-selectin. Biochem. J. 341:61.
    • (1999) Biochem. J. , vol.341 , pp. 61
    • Malhotra, R.1    Ward, M.2    Sim, R.B.3    Bird, M.I.4
  • 44
    • 0023755935 scopus 로고
    • Role of basic amino acids in the interaction of bindin with sulfated fucans
    • DeAngelis, P. L., and C. G. Glabe. 1988. Role of basic amino acids in the interaction of bindin with sulfated fucans. Biochemistry 27:8189.
    • (1988) Biochemistry , vol.27 , pp. 8189
    • DeAngelis, P.L.1    Glabe, C.G.2
  • 45
    • 0035669220 scopus 로고    scopus 로고
    • An in vitro system for testing leucocyte and leukaemic cell line adhesion to synthetic fibres
    • Barbe, L. L., B. M. Boval, M. P. Wautier, and J. L. Wautier. 2001. An in vitro system for testing leucocyte and leukaemic cell line adhesion to synthetic fibres. Br. J. Haematol. 115:664.
    • (2001) Br. J. Haematol. , vol.115 , pp. 664
    • Barbe, L.L.1    Boval, B.M.2    Wautier, M.P.3    Wautier, J.L.4
  • 46
    • 0035903204 scopus 로고    scopus 로고
    • Secreted forms of the amyloid-β precursor protein are ligands for the class A scavenger receptor
    • Santiago-Garcia, J., J. Mas-Oliva, T. L. Innerarity, and R. E. Pitas. 2001. Secreted forms of the amyloid-β precursor protein are ligands for the class A scavenger receptor. J. Biol. Chem. 276:30655.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30655
    • Santiago-Garcia, J.1    Mas-Oliva, J.2    Innerarity, T.L.3    Pitas, R.E.4
  • 47
    • 0033942744 scopus 로고    scopus 로고
    • Increased uptake of α-hydroxy aldehyde-modified low density lipoprotein by macrophage scavenger receptors
    • Kawamura, M., J. W. Heinecke, and A. Chait. 2000. Increased uptake of a-hydroxy aldehyde-modified low density lipoprotein by macrophage scavenger receptors. J. Lipid Res. 41:1054.
    • (2000) J. Lipid Res. , vol.41 , pp. 1054
    • Kawamura, M.1    Heinecke, J.W.2    Chait, A.3
  • 48
    • 0033523721 scopus 로고    scopus 로고
    • Sulfation of a high endothelial venule-expressed ligand for L-selectin: Effects on tethering and rolling of lymphocytes
    • Tangemann, K., A. Bistrup, S. Hemmerich. and S. D. Rosen. 1999. Sulfation of a high endothelial venule-expressed ligand for L-selectin: Effects on tethering and rolling of lymphocytes. J. Exp. Med. 190:935.
    • (1999) J. Exp. Med. , vol.190 , pp. 935
    • Tangemann, K.1    Bistrup, A.2    Hemmerich, S.3    Rosen, S.D.4
  • 49
    • 0032414192 scopus 로고    scopus 로고
    • Accumulation and metabolism of low density lipoprotein-derived cholesteryl linoleate hydroperoxide and hydroxide by macrophages
    • Kritharides, L., J. Upston, W. Jessup, and R. T. Dean. 1998. Accumulation and metabolism of low density lipoprotein-derived cholesteryl linoleate hydroperoxide and hydroxide by macrophages. J. Lipid Res. 39:2394.
    • (1998) J. Lipid Res. , vol.39 , pp. 2394
    • Kritharides, L.1    Upston, J.2    Jessup, W.3    Dean, R.T.4
  • 50
    • 0030999099 scopus 로고    scopus 로고
    • Bovine sperm binding to oviductal epithelium involves fucose recognition
    • Lefebvre, R., M. C. Lo, and S. S. Suarez. 1997. Bovine sperm binding to oviductal epithelium involves fucose recognition. Biol. Reprod. 56:1198.
    • (1997) Biol. Reprod. , vol.56 , pp. 1198
    • Lefebvre, R.1    Lo, M.C.2    Suarez, S.S.3
  • 51
    • 0020640609 scopus 로고
    • Possible role for cell-surface carbohydrate-binding molecules in lymphocyte recirculation
    • Stoolman, L. M., and S. D. Rosen. 1983. Possible role for cell-surface carbohydrate-binding molecules in lymphocyte recirculation. J. Cell Biol. 96:722.
    • (1983) J. Cell Biol. , vol.96 , pp. 722
    • Stoolman, L.M.1    Rosen, S.D.2
  • 52
    • 0029655826 scopus 로고    scopus 로고
    • Sulfated polysaccharides inhibit lymphocyte-to-epithelial transmission of human immunodeficiency virus-1
    • Pearce-Pratt, R., and D. M. Phillips. 1996. Sulfated polysaccharides inhibit lymphocyte-to-epithelial transmission of human immunodeficiency virus-1. Biol. Reprod. 54:173.
    • (1996) Biol. Reprod. , vol.54 , pp. 173
    • Pearce-Pratt, R.1    Phillips, D.M.2
  • 53
    • 0024337788 scopus 로고
    • Adhesion of lymphoid cells to fibroblasts in tissue culture
    • Abraham, D., G. Bou-Gharios, H. Muir, and I. Olsen. 1989. Adhesion of lymphoid cells to fibroblasts in tissue culture. Cell. Immunol. 122:33.
    • (1989) Cell. Immunol. , vol.122 , pp. 33
    • Abraham, D.1    Bou-Gharios, G.2    Muir, H.3    Olsen, I.4
  • 54
    • 0034785849 scopus 로고    scopus 로고
    • Role of cell surface glycosylation in mediating repair of human airway epithelial cell monolayers
    • Dorscheid, D. R., K. R. Wojcik, K. Yule, and S. R. White. 2001. Role of cell surface glycosylation in mediating repair of human airway epithelial cell monolayers. Infect. Immun. 281:L982.
    • (2001) Infect. Immun. , vol.281
    • Dorscheid, D.R.1    Wojcik, K.R.2    Yule, K.3    White, S.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.