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Volumn 212, Issue 4-5, 2007, Pages 343-353

The α2β1 integrin: A novel collectin/C1q receptor

Author keywords

C1q; Collagen; Collectin; Innate immunity; Integrin; Mast cell

Indexed keywords

COLLECTIN; COMPLEMENT COMPONENT C1Q RECEPTOR; COMPLEMENT RECEPTOR; INTERLEUKIN 6; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 2; VERY LATE ACTIVATION ANTIGEN 2 ANTIBODY; COMPLEMENT 1Q RECEPTOR; MEMBRANE PROTEIN;

EID: 34249752194     PISSN: 01712985     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imbio.2006.11.013     Document Type: Article
Times cited : (63)

References (76)
  • 1
    • 0027395858 scopus 로고
    • Role of integrins and other cell adhesion molecules in tumor progression and metastasis
    • Albelda S.M. Role of integrins and other cell adhesion molecules in tumor progression and metastasis. Lab. Invest. 68 (1993) 4-17
    • (1993) Lab. Invest. , vol.68 , pp. 4-17
    • Albelda, S.M.1
  • 2
    • 0035423368 scopus 로고    scopus 로고
    • Cutting edge: the mouse NK cell-associated antigen recognized by DX5 monoclonal antibody is CD49b (alpha 2 integrin, very late antigen-2)
    • Arase H., Saito T., Phillips J.H., and Lanier L.L. Cutting edge: the mouse NK cell-associated antigen recognized by DX5 monoclonal antibody is CD49b (alpha 2 integrin, very late antigen-2). J. Immunol. 167 (2001) 1141-1144
    • (2001) J. Immunol. , vol.167 , pp. 1141-1144
    • Arase, H.1    Saito, T.2    Phillips, J.H.3    Lanier, L.L.4
  • 3
    • 0033624083 scopus 로고    scopus 로고
    • Beta7 integrin-deficient mice: delayed leukocyte recruitment and attenuated protective immunity in the small intestine during enteric helminth infection
    • Artis D., Humphreys N.E., Potten C.S., Wagner N., Muller W., McDermott J.R., Grencis R.K., and Else K.J. Beta7 integrin-deficient mice: delayed leukocyte recruitment and attenuated protective immunity in the small intestine during enteric helminth infection. Eur. J. Immunol. 30 (2000) 1656-1664
    • (2000) Eur. J. Immunol. , vol.30 , pp. 1656-1664
    • Artis, D.1    Humphreys, N.E.2    Potten, C.S.3    Wagner, N.4    Muller, W.5    McDermott, J.R.6    Grencis, R.K.7    Else, K.J.8
  • 5
    • 0030612224 scopus 로고    scopus 로고
    • The integrin alpha1 A-domain is a ligand binding site for collagens and laminin
    • Calderwood D.A., Tuckwell D.S., Eble J., Kuhn K., and Humphries M.J. The integrin alpha1 A-domain is a ligand binding site for collagens and laminin. J. Biol. Chem. 272 (1997) 12311-12317
    • (1997) J. Biol. Chem. , vol.272 , pp. 12311-12317
    • Calderwood, D.A.1    Tuckwell, D.S.2    Eble, J.3    Kuhn, K.4    Humphries, M.J.5
  • 6
    • 0032493643 scopus 로고    scopus 로고
    • Isolation, cloning, and sequence analysis of the integrin subunit alpha10, a beta1-associated collagen binding integrin expressed on chondrocytes
    • Camper L., Hellman U., and Lundgren-Akerlund E. Isolation, cloning, and sequence analysis of the integrin subunit alpha10, a beta1-associated collagen binding integrin expressed on chondrocytes. J. Biol. Chem. 273 (1998) 20383-20389
    • (1998) J. Biol. Chem. , vol.273 , pp. 20383-20389
    • Camper, L.1    Hellman, U.2    Lundgren-Akerlund, E.3
  • 8
    • 0027497502 scopus 로고
    • Multiple functional forms of the integrin VLA-2 can be derived from a single alpha 2 cDNA clone: interconversion of forms induced by an anti-beta 1 antibody
    • Chan B.M., and Hemler M.E. Multiple functional forms of the integrin VLA-2 can be derived from a single alpha 2 cDNA clone: interconversion of forms induced by an anti-beta 1 antibody. J. Cell Biol. 120 (1993) 537-543
    • (1993) J. Cell Biol. , vol.120 , pp. 537-543
    • Chan, B.M.1    Hemler, M.E.2
  • 9
    • 0036314793 scopus 로고    scopus 로고
    • The alpha(2) integrin subunit-deficient mouse: a multifaceted phenotype including defects of branching morphogenesis and hemostasis
    • Chen J., Diacovo T.G., Grenache D.G., Santoro S.A., and Zutter M.M. The alpha(2) integrin subunit-deficient mouse: a multifaceted phenotype including defects of branching morphogenesis and hemostasis. Am. J. Pathol. 161 (2002) 337-344
    • (2002) Am. J. Pathol. , vol.161 , pp. 337-344
    • Chen, J.1    Diacovo, T.G.2    Grenache, D.G.3    Santoro, S.A.4    Zutter, M.M.5
  • 12
    • 0031866394 scopus 로고    scopus 로고
    • Ligand recognition by the I domain-containing integrins
    • Dickeson S.K., and Santoro S.A. Ligand recognition by the I domain-containing integrins. Cell Mol. Life Sci. 54 (1998) 556-566
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 556-566
    • Dickeson, S.K.1    Santoro, S.A.2
  • 13
    • 0033527550 scopus 로고    scopus 로고
    • Determinants of ligand binding specificity of the alpha(1)beta(1) and alpha(2)beta(1) integrins
    • Dickeson S.K., Mathis N.L., Rahman M., Bergelson J.M., and Santoro S.A. Determinants of ligand binding specificity of the alpha(1)beta(1) and alpha(2)beta(1) integrins. J. Biol. Chem. 274 (1999) 32182-32191
    • (1999) J. Biol. Chem. , vol.274 , pp. 32182-32191
    • Dickeson, S.K.1    Mathis, N.L.2    Rahman, M.3    Bergelson, J.M.4    Santoro, S.A.5
  • 14
    • 0029892080 scopus 로고    scopus 로고
    • Critical protective role of mast cells in a model of acute septic peritonitis
    • Echtenacher B., Mannel D.N., and Hultner L. Critical protective role of mast cells in a model of acute septic peritonitis. Nature 381 (1996) 75-77
    • (1996) Nature , vol.381 , pp. 75-77
    • Echtenacher, B.1    Mannel, D.N.2    Hultner, L.3
  • 15
    • 1542283727 scopus 로고    scopus 로고
    • Mast cell-mediated inflammatory responses require the alpha 2 beta 1 integrin
    • Edelson B.T., Li Z., Pappan L.K., and Zutter M.M. Mast cell-mediated inflammatory responses require the alpha 2 beta 1 integrin. Blood 103 (2004) 2214-2220
    • (2004) Blood , vol.103 , pp. 2214-2220
    • Edelson, B.T.1    Li, Z.2    Pappan, L.K.3    Zutter, M.M.4
  • 17
    • 0028930473 scopus 로고
    • Identification of a gC1q-binding protein (gC1q-R) on the surface of human neutrophils. Subcellular localization and binding properties in comparison with the cC1q-R
    • Eggleton P., Ghebrehiwet B., Sastry K.N., Coburn J.P., Zaner K.S., Reid K.B., and Tauber A.I. Identification of a gC1q-binding protein (gC1q-R) on the surface of human neutrophils. Subcellular localization and binding properties in comparison with the cC1q-R. J. Clin. Invest. 95 (1995) 1569-1578
    • (1995) J. Clin. Invest. , vol.95 , pp. 1569-1578
    • Eggleton, P.1    Ghebrehiwet, B.2    Sastry, K.N.3    Coburn, J.P.4    Zaner, K.S.5    Reid, K.B.6    Tauber, A.I.7
  • 18
    • 0024847956 scopus 로고
    • The human integrin VLA-2 is a collagen receptor on some cells and a collagen/laminin receptor on others
    • Elices M.J., and Hemler M.E. The human integrin VLA-2 is a collagen receptor on some cells and a collagen/laminin receptor on others. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 9906-9910
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 9906-9910
    • Elices, M.J.1    Hemler, M.E.2
  • 19
    • 0023730105 scopus 로고
    • Characterization of C1q-binding material released from the membranes of Raji and U937 cells by limited proteolysis with trypsin
    • Erdei A., and Reid K.B. Characterization of C1q-binding material released from the membranes of Raji and U937 cells by limited proteolysis with trypsin. Biochem. J. 255 (1988) 493-499
    • (1988) Biochem. J. , vol.255 , pp. 493-499
    • Erdei, A.1    Reid, K.B.2
  • 20
    • 0036584407 scopus 로고    scopus 로고
    • Evolution of the lectin-complement pathway and its role in innate immunity
    • Fujita T. Evolution of the lectin-complement pathway and its role in innate immunity. Nat. Rev. Immunol. 2 (2002) 346-353
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 346-353
    • Fujita, T.1
  • 21
    • 2442650484 scopus 로고    scopus 로고
    • cC1q-R (calreticulin) and gC1q-R/p33: ubiquitously expressed multi-ligand binding cellular proteins involved in inflammation and infection
    • Ghebrehiwet B., and Peerschke E.I. cC1q-R (calreticulin) and gC1q-R/p33: ubiquitously expressed multi-ligand binding cellular proteins involved in inflammation and infection. Mol. Immunol. 41 (2004) 173-183
    • (2004) Mol. Immunol. , vol.41 , pp. 173-183
    • Ghebrehiwet, B.1    Peerschke, E.I.2
  • 22
    • 0141918823 scopus 로고    scopus 로고
    • By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation
    • Gardai S.J., Xiao Y.Q., Dickinson M., Nick J.A., Voelker D.R., Greene K.E., and Henson P.M. By binding SIRPalpha or calreticulin/CD91, lung collectins act as dual function surveillance molecules to suppress or enhance inflammation. Cell 115 (2003) 13-23
    • (2003) Cell , vol.115 , pp. 13-23
    • Gardai, S.J.1    Xiao, Y.Q.2    Dickinson, M.3    Nick, J.A.4    Voelker, D.R.5    Greene, K.E.6    Henson, P.M.7
  • 23
    • 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., and McDevitt C. Identification of the Raji cell membrane-derived C1q inhibitor as a receptor for human C1q. Purification and immunochemical characterization. J. Exp. Med. 160 (1984) 1375-1389
    • (1984) J. Exp. Med. , vol.160 , pp. 1375-1389
    • Ghebrehiwet, B.1    Silvestri, L.2    McDevitt, C.3
  • 24
    • 0034997841 scopus 로고    scopus 로고
    • gC1q-R/p33, a member of a new class of multifunctional and multicompartmental cellular proteins, is involved in inflammation and infection
    • Ghebrehiwet B., Lim B.L., Kumar R., Feng X., and Peerschke E.I. gC1q-R/p33, a member of a new class of multifunctional and multicompartmental cellular proteins, is involved in inflammation and infection. Immunol. Rev. 180 (2001) 65-77
    • (2001) Immunol. Rev. , vol.180 , pp. 65-77
    • Ghebrehiwet, B.1    Lim, B.L.2    Kumar, R.3    Feng, X.4    Peerschke, E.I.5
  • 26
    • 0033794569 scopus 로고    scopus 로고
    • Complexity and specificity of integrin signalling
    • Giancotti F.G. Complexity and specificity of integrin signalling. Nat. Cell Biol. 2 (2000) E13-E14
    • (2000) Nat. Cell Biol. , vol.2
    • Giancotti, F.G.1
  • 27
    • 0034671980 scopus 로고    scopus 로고
    • A role for CD21/CD35 and CD19 in responses to acute septic peritonitis: a potential mechanism for mast cell activation
    • Gommerman J.L., Oh D.Y., Zhou X., Tedder T.F., Maurer M., Galli S.J., and Carroll M.C. A role for CD21/CD35 and CD19 in responses to acute septic peritonitis: a potential mechanism for mast cell activation. J. Immunol. 165 (2000) 6915-6921
    • (2000) J. Immunol. , vol.165 , pp. 6915-6921
    • Gommerman, J.L.1    Oh, D.Y.2    Zhou, X.3    Tedder, T.F.4    Maurer, M.5    Galli, S.J.6    Carroll, M.C.7
  • 28
    • 0028325931 scopus 로고
    • Cell-surface protein identified on phagocytic cells modulates the C1q-mediated enhancement of phagocytosis
    • Guan E., Robinson S.L., Goodman E.B., and Tenner A.J. Cell-surface protein identified on phagocytic cells modulates the C1q-mediated enhancement of phagocytosis. J. Immunol. 152 (1994) 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
  • 29
    • 0025340884 scopus 로고
    • The alpha 1/beta 1 and alpha 6/beta 1 integrin heterodimers mediate cell attachment to distinct sites on laminin
    • Hall D.R., Reichardt L.F., Crowley E., Holley B., Moezzi H., Sonnenberg A., and Damsky C.H. The alpha 1/beta 1 and alpha 6/beta 1 integrin heterodimers mediate cell attachment to distinct sites on laminin. J. Cell Biol. 110 (1990) 2175-2184
    • (1990) J. Cell Biol. , vol.110 , pp. 2175-2184
    • Hall, D.R.1    Reichardt, L.F.2    Crowley, E.3    Holley, B.4    Moezzi, H.5    Sonnenberg, A.6    Damsky, C.H.7
  • 31
    • 0025218924 scopus 로고
    • VLA proteins in the integrin family: structures, functions, and their role on leukocytes
    • Hemler M.E. VLA proteins in the integrin family: structures, functions, and their role on leukocytes. Annu. Rev. Immunol. 8 (1990) 365-400
    • (1990) Annu. Rev. Immunol. , vol.8 , pp. 365-400
    • Hemler, M.E.1
  • 32
    • 0021845246 scopus 로고
    • VLA-1: a T cell surface antigen which defines a novel late stage of human T cell activation
    • Hemler M.E., Jacobson J.G., Brenner M.B., Mann D., and Strominger J.L. VLA-1: a T cell surface antigen which defines a novel late stage of human T cell activation. Eur. J. Immunol. 15 (1985) 502-508
    • (1985) Eur. J. Immunol. , vol.15 , pp. 502-508
    • Hemler, M.E.1    Jacobson, J.G.2    Brenner, M.B.3    Mann, D.4    Strominger, J.L.5
  • 33
    • 0029931383 scopus 로고    scopus 로고
    • Isolation and characterization of the kininogen-binding protein p33 from endothelial cells. Identity with the gC1q receptor
    • Herwald H., Dedio J., Kellner R., Loos M., and Muller-Esterl W. Isolation and characterization of the kininogen-binding protein p33 from endothelial cells. Identity with the gC1q receptor. J. Biol. Chem. 271 (1996) 13040-13047
    • (1996) J. Biol. Chem. , vol.271 , pp. 13040-13047
    • Herwald, H.1    Dedio, J.2    Kellner, R.3    Loos, M.4    Muller-Esterl, W.5
  • 34
    • 0037192771 scopus 로고    scopus 로고
    • Integrin alpha 2-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen
    • Holtkotter O., Nieswandt B., Smyth N., Muller W., Hafner M., Schulte V., Krieg T., and Eckes B. Integrin alpha 2-deficient mice develop normally, are fertile, but display partially defective platelet interaction with collagen. J. Biol. Chem. 277 (2002) 10789-10794
    • (2002) J. Biol. Chem. , vol.277 , pp. 10789-10794
    • Holtkotter, O.1    Nieswandt, B.2    Smyth, N.3    Muller, W.4    Hafner, M.5    Schulte, V.6    Krieg, T.7    Eckes, B.8
  • 35
    • 0024093898 scopus 로고
    • Identification of a neuronal laminin receptor: an Mr 200K/120K integrin heterodimer that binds laminin in a divalent cation-dependent manner
    • Ignatius M.J., and Reichardt L.F. Identification of a neuronal laminin receptor: an Mr 200K/120K integrin heterodimer that binds laminin in a divalent cation-dependent manner. Neuron 1 (1988) 713-725
    • (1988) Neuron , vol.1 , pp. 713-725
    • Ignatius, M.J.1    Reichardt, L.F.2
  • 37
    • 0028241409 scopus 로고
    • Regulation of C1q receptor expression on human polymorphonuclear leukocytes
    • Jack R.M., Lowenstein B.A., and Nicholson-Weller A. Regulation of C1q receptor expression on human polymorphonuclear leukocytes. J. Immunol. 153 (1994) 262-269
    • (1994) J. Immunol. , vol.153 , pp. 262-269
    • Jack, R.M.1    Lowenstein, B.A.2    Nicholson-Weller, A.3
  • 38
    • 0027268377 scopus 로고
    • Interaction of type IV collagen with the isolated integrins alpha 1 beta 1 and alpha 2 beta 1
    • Kern A., Eble J., Golbik R., and Kuhn K. Interaction of type IV collagen with the isolated integrins alpha 1 beta 1 and alpha 2 beta 1. Eur. J. Biochem. 215 (1993) 151-159
    • (1993) Eur. J. Biochem. , vol.215 , pp. 151-159
    • Kern, A.1    Eble, J.2    Golbik, R.3    Kuhn, K.4
  • 40
    • 0037136421 scopus 로고    scopus 로고
    • Collectins and ficolins: sugar pattern recognition molecules of the mammalian innate immune system
    • Lu J., Teh C., Kishore U., and Reid K.B. Collectins and ficolins: sugar pattern recognition molecules of the mammalian innate immune system. Biochim. Biophys. Acta 1572 (2002) 387-400
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 387-400
    • Lu, J.1    Teh, C.2    Kishore, U.3    Reid, K.B.4
  • 41
    • 0029981928 scopus 로고    scopus 로고
    • Mast cell modulation of neutrophil influx and bacterial clearance at sites of infection through TNF-alpha
    • Malaviya R., Ikeda T., Ross E., and Abraham S.N. Mast cell modulation of neutrophil influx and bacterial clearance at sites of infection through TNF-alpha. Nature 381 (1996) 77-80
    • (1996) Nature , vol.381 , pp. 77-80
    • Malaviya, R.1    Ikeda, T.2    Ross, E.3    Abraham, S.N.4
  • 42
    • 0033529313 scopus 로고    scopus 로고
    • The mast cell tumor necrosis factor alpha response to FimH-expressing Escherichia coli is mediated by the glycosylphosphatidylinositol-anchored molecule CD48
    • Malaviya R., Gao Z., Thankavel K., van der Merwe P.A., and Abraham S.N. The mast cell tumor necrosis factor alpha response to FimH-expressing Escherichia coli is mediated by the glycosylphosphatidylinositol-anchored molecule CD48. Proc. Natl. Acad. Sci. USA 96 (1999) 8110-8115
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8110-8115
    • Malaviya, R.1    Gao, Z.2    Thankavel, K.3    van der Merwe, P.A.4    Abraham, S.N.5
  • 43
    • 0024421499 scopus 로고
    • Chemical and hydrodynamic characterization of the human leucocyte receptor for complement subcomponent C1q
    • Malhotra R., and Sim R.B. Chemical and hydrodynamic characterization of the human leucocyte receptor for complement subcomponent C1q. Biochem. J. 262 (1989) 625-631
    • (1989) Biochem. J. , vol.262 , pp. 625-631
    • Malhotra, R.1    Sim, R.B.2
  • 45
    • 5044238408 scopus 로고    scopus 로고
    • Mast-cell responses to pathogens
    • Marshall J.S. Mast-cell responses to pathogens. Nat. Rev. Immunol. 4 (2004) 787-799
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 787-799
    • Marshall, J.S.1
  • 46
    • 0035216122 scopus 로고    scopus 로고
    • Toll-like receptor 4-mediated activation of murine mast cells
    • McCurdy J.D., Lin T.J., and Marshall J.S. Toll-like receptor 4-mediated activation of murine mast cells. J. Leukoc. Biol. 70 (2001) 977-984
    • (2001) J. Leukoc. Biol. , vol.70 , pp. 977-984
    • McCurdy, J.D.1    Lin, T.J.2    Marshall, J.S.3
  • 47
    • 0343526467 scopus 로고    scopus 로고
    • Integrins minireview series
    • McDonald J.A. Integrins minireview series. J. Biol. Chem. 275 (2000) 21783
    • (2000) J. Biol. Chem. , vol.275 , pp. 21783
    • McDonald, J.A.1
  • 48
    • 0036864199 scopus 로고    scopus 로고
    • Structure-function studies of the receptors for complement C1q
    • McGreal E., and Gasque P. Structure-function studies of the receptors for complement C1q. Biochem. Soc. Trans. 30 (2002) 1010-1014
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 1010-1014
    • McGreal, E.1    Gasque, P.2
  • 49
    • 0027965672 scopus 로고
    • Identification of collagen and laminin receptor integrins on murine T lymphocytes
    • Miyake S., Sakurai T., Okumura K., and Yagita H. Identification of collagen and laminin receptor integrins on murine T lymphocytes. Eur. J. Immunol. 24 (1994) 2000-2005
    • (1994) Eur. J. Immunol. , vol.24 , pp. 2000-2005
    • Miyake, S.1    Sakurai, T.2    Okumura, K.3    Yagita, H.4
  • 50
    • 0031180570 scopus 로고    scopus 로고
    • Distribution of receptors of collagen and globular domains of C1q in human lung fibroblasts
    • Narayanan A.S., Lurton J., and Raghu G. Distribution of receptors of collagen and globular domains of C1q in human lung fibroblasts. Am. J. Respir. Cell Mol. Biol. 17 (1997) 84-90
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.17 , pp. 84-90
    • Narayanan, A.S.1    Lurton, J.2    Raghu, G.3
  • 51
    • 0033558378 scopus 로고    scopus 로고
    • C1qRP is a heavily O-glycosylated cell surface protein involved in the regulation of phagocytic activity
    • Nepomuceno R.R., Ruiz S., Park M., and Tenner A.J. C1qRP is a heavily O-glycosylated cell surface protein involved in the regulation of phagocytic activity. J. Immunol. 162 (1999) 3583-3589
    • (1999) J. Immunol. , vol.162 , pp. 3583-3589
    • Nepomuceno, R.R.1    Ruiz, S.2    Park, M.3    Tenner, A.J.4
  • 52
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interaction: is GPVI the central receptor?
    • Nieswandt B., and Watson S.P. Platelet-collagen interaction: is GPVI the central receptor?. Blood 102 (2003) 449-461
    • (2003) Blood , vol.102 , pp. 449-461
    • Nieswandt, B.1    Watson, S.P.2
  • 53
    • 0022536502 scopus 로고
    • Deficiency of platelet membrane glycoprotein Ia associated with a decreased platelet adhesion to subendothelium: a defect in platelet spreading
    • Nieuwenhuis H.K., Sakariassen K.S., Houdijk W.P., Nievelstein P.F., and Sixma J.J. Deficiency of platelet membrane glycoprotein Ia associated with a decreased platelet adhesion to subendothelium: a defect in platelet spreading. Blood 68 (1986) 692-695
    • (1986) Blood , vol.68 , pp. 692-695
    • Nieuwenhuis, H.K.1    Sakariassen, K.S.2    Houdijk, W.P.3    Nievelstein, P.F.4    Sixma, J.J.5
  • 55
    • 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 C.A., deCathelineau A., Hoffmann P.R., Bratton D., Ghebrehiwet B., Fadok V.A., and Henson P.M. C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J. Exp. Med. 194 (2001) 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
  • 56
    • 0025166117 scopus 로고
    • Platelet C1q receptor interactions with collagen- and C1q-coated surfaces
    • Peerschke E.I., and Ghebrehiwet B. Platelet C1q receptor interactions with collagen- and C1q-coated surfaces. J. Immunol. 145 (1990) 2984-2988
    • (1990) J. Immunol. , vol.145 , pp. 2984-2988
    • Peerschke, E.I.1    Ghebrehiwet, B.2
  • 57
    • 0027999287 scopus 로고
    • Platelet membrane receptors for the complement component C1q
    • Peerschke E.I., and Ghebrehiwet B. Platelet membrane receptors for the complement component C1q. Semin. Hematol. 31 (1994) 320-328
    • (1994) Semin. Hematol. , vol.31 , pp. 320-328
    • Peerschke, E.I.1    Ghebrehiwet, B.2
  • 58
    • 0030718543 scopus 로고    scopus 로고
    • Impaired mast cell-dependent natural immunity in complement C3-deficient mice
    • Prodeus A.P., Zhou X., Maurer M., Galli S.J., and Carroll M.C. Impaired mast cell-dependent natural immunity in complement C3-deficient mice. Nature 390 (1997) 172-175
    • (1997) Nature , vol.390 , pp. 172-175
    • Prodeus, A.P.1    Zhou, X.2    Maurer, M.3    Galli, S.J.4    Carroll, M.C.5
  • 59
    • 0034326626 scopus 로고    scopus 로고
    • Potent costimulation of effector T lymphocytes by human collagen type I
    • Rao W.H., Hales J.M., and Camp R.D. Potent costimulation of effector T lymphocytes by human collagen type I. J. Immunol. 165 (2000) 4935-4940
    • (2000) J. Immunol. , vol.165 , pp. 4935-4940
    • Rao, W.H.1    Hales, J.M.2    Camp, R.D.3
  • 60
    • 0035284909 scopus 로고    scopus 로고
    • Differential effects of CD18, CD29, and CD49 integrin subunit inhibition on neutrophil migration in pulmonary inflammation
    • Ridger V.C., Wagner B.E., Wallace W.A., and Hellewell P.G. Differential effects of CD18, CD29, and CD49 integrin subunit inhibition on neutrophil migration in pulmonary inflammation. J. Immunol. 166 (2001) 3484-3490
    • (2001) J. Immunol. , vol.166 , pp. 3484-3490
    • Ridger, V.C.1    Wagner, B.E.2    Wallace, W.A.3    Hellewell, P.G.4
  • 62
    • 0022922723 scopus 로고
    • Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen
    • Santoro S.A. Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen. Cell 46 (1986) 913-920
    • (1986) Cell , vol.46 , pp. 913-920
    • Santoro, S.A.1
  • 63
    • 0028979497 scopus 로고
    • The alpha 2 beta 1 integrin: a collagen receptor on platelets and other cells
    • Santoro S.A., and Zutter M.M. The alpha 2 beta 1 integrin: a collagen receptor on platelets and other cells. Thromb. Haemost. 74 (1995) 813-821
    • (1995) Thromb. Haemost. , vol.74 , pp. 813-821
    • Santoro, S.A.1    Zutter, M.M.2
  • 64
    • 0026253404 scopus 로고
    • Distinct determinants on collagen support alpha 2 beta 1 integrin-mediated platelet adhesion and platelet activation
    • Santoro S.A., Walsh J.J., Staatz W.D., and Baranski K.J. Distinct determinants on collagen support alpha 2 beta 1 integrin-mediated platelet adhesion and platelet activation. Cell Regul. 2 (1991) 905-913
    • (1991) Cell Regul. , vol.2 , pp. 905-913
    • Santoro, S.A.1    Walsh, J.J.2    Staatz, W.D.3    Baranski, K.J.4
  • 66
    • 0031459567 scopus 로고    scopus 로고
    • The C1q and collectin binding site within C1q receptor (cell surface calreticulin)
    • Stuart G.R., Lynch N.J., Day A.J., Schwaeble W.J., and Sim R.B. The C1q and collectin binding site within C1q receptor (cell surface calreticulin). Immunopharmacology 38 (1997) 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
  • 67
    • 0035881267 scopus 로고    scopus 로고
    • Protective roles of mast cells against enterobacterial infection are mediated by Toll-like receptor 4
    • Supajatura V., Ushio H., Nakao A., Okumura K., Ra C., and Ogawa H. Protective roles of mast cells against enterobacterial infection are mediated by Toll-like receptor 4. J. Immunol. 167 (2001) 2250-2256
    • (2001) J. Immunol. , vol.167 , pp. 2250-2256
    • Supajatura, V.1    Ushio, H.2    Nakao, A.3    Okumura, K.4    Ra, C.5    Ogawa, H.6
  • 68
    • 0036105543 scopus 로고    scopus 로고
    • Differential responses of mast cell Toll-like receptors 2 and 4 in allergy and innate immunity
    • Supajatura V., Ushio H., Nakao A., Akira S., Okumura K., Ra C., and Ogawa H. Differential responses of mast cell Toll-like receptors 2 and 4 in allergy and innate immunity. J. Clin. Invest. 109 (2002) 1351-1359
    • (2002) J. Clin. Invest. , vol.109 , pp. 1351-1359
    • Supajatura, V.1    Ushio, H.2    Nakao, A.3    Akira, S.4    Okumura, K.5    Ra, C.6    Ogawa, H.7
  • 69
    • 0031692665 scopus 로고    scopus 로고
    • C1q receptors: regulating specific functions of phagocytic cells
    • Tenner A.J. C1q receptors: regulating specific functions of phagocytic cells. Immunobiology 199 (1998) 250-264
    • (1998) Immunobiology , vol.199 , pp. 250-264
    • Tenner, A.J.1
  • 70
    • 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 A.J., Robinson S.L., and Ezekowitz R.A. 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 (1995) 485-493
    • (1995) Immunity , vol.3 , pp. 485-493
    • Tenner, A.J.1    Robinson, S.L.2    Ezekowitz, R.A.3
  • 71
    • 0030764155 scopus 로고    scopus 로고
    • A novel association of Fc receptor gamma-chain with glycoprotein VI and their co-expression as a collagen receptor in human platelets
    • Tsuji M., Ezumi Y., Arai M., and Takayama H. A novel association of Fc receptor gamma-chain with glycoprotein VI and their co-expression as a collagen receptor in human platelets. J. Biol. Chem. 272 (1997) 23528-23531
    • (1997) J. Biol. Chem. , vol.272 , pp. 23528-23531
    • Tsuji, M.1    Ezumi, Y.2    Arai, M.3    Takayama, H.4
  • 73
    • 0037020239 scopus 로고    scopus 로고
    • Polymerization of type I and III collagens is dependent on fibronectin and enhanced by integrins alpha 11beta 1 and alpha 2beta 1
    • Velling T., Risteli J., Wennerberg K., Mosher D.F., and Johansson S. Polymerization of type I and III collagens is dependent on fibronectin and enhanced by integrins alpha 11beta 1 and alpha 2beta 1. J. Biol. Chem. 277 (2002) 37377-37381
    • (2002) J. Biol. Chem. , vol.277 , pp. 37377-37381
    • Velling, T.1    Risteli, J.2    Wennerberg, K.3    Mosher, D.F.4    Johansson, S.5
  • 74
    • 0034161512 scopus 로고    scopus 로고
    • Integrin alpha(2)beta(1) (VLA-2) is a principal receptor used by neutrophils for locomotion in extravascular tissue
    • Werr J., Johansson J., Eriksson E.E., Hedqvist P., Ruoslahti E., and Lindbom L. Integrin alpha(2)beta(1) (VLA-2) is a principal receptor used by neutrophils for locomotion in extravascular tissue. Blood 95 (2000) 1804-1809
    • (2000) Blood , vol.95 , pp. 1804-1809
    • Werr, J.1    Johansson, J.2    Eriksson, E.E.3    Hedqvist, P.4    Ruoslahti, E.5    Lindbom, L.6
  • 76
    • 30144445753 scopus 로고    scopus 로고
    • Function of α2β1 integrin
    • Gullberg D. (Ed), Landis Bioscience, Georgetown
    • Zutter M.M., and Santoro S.A. Function of α2β1 integrin. In: Gullberg D. (Ed). Domains in Integrins (2003), Landis Bioscience, Georgetown 41-58
    • (2003) Domains in Integrins , pp. 41-58
    • Zutter, M.M.1    Santoro, S.A.2


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