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Signal Transduction from Leukocyte Integrins

  • Chapter
Cell Adhesion Molecules

Part of the book series: Pezcoller Foundation Symposia ((PFSO,volume 4))

Abstract

The activation of leukocytes at sites of inflamation is a topic of great meidcal importance. Leukocytes normally exist in the circulation unactivated. In response to specific inflammatory signals, they can migrate out of the bloodstream, into the site of inflammation. At the inflammatory site, they express a different phenotype than in the bloos. Neutrophils and monocytes are easily stimulated to release reactive oxygen metabolites which act both as cytocidal agents and as metabolic intermediates (Durum and Oppenheim, 1989); monocytes and macrophages are more highly phagocytic or more competent for antigen presentation (Silverstein, et al., 1989; Unanue and Allen, 1987); lymphocytes are activated to proliferate, synthesize cytokines, or perform effector functions (Durum and Oppenheim, 1989). Inhibition of leukocyte migration into, or activation at, sites of inflammation can dramatically reduce tissue damage and alter survival (Ferguson et al., 1991; Rosen, 1989; Vedder et al., 1988; Vercellotti et al., 1983). Thus, understanding the mechanisms of leukocyte exit from the bloodstream and activation at inflammatory sites is presently a subject of intense effort in several laboratories.

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Abbreviations

DMSO :

Dimethylsulfoxide;

ECM :

Extracellular Matrix;

IAP :

Integrin-associated 50 kD Integral Membrane Protein;

LRI :

Leukocyte-response Integrin;

M r :

Relative molecular mass as estimated from SDS-PAGE;

PMN :

Polymorphonuclear Neutrophil

References

  • Bohnsack, J.F., 1992, CD1 l/CDIS-independent neutrophil adherence to laminin is mediated by the integrin VLA-6. Blood 79:1545–1552.

    PubMed  CAS  Google Scholar 

  • Bohnsack, J.F., Akiyama, S.K., Damsky, C.H., Knape, W.A., and Zimmerman, G.A., 1990a, Human neutrophil adherence to laminin in vitro. Evidence for a distinct neutrophil integrin receptor for laminin. J. Exp. Med. 171:1221–1237.

    Article  PubMed  CAS  Google Scholar 

  • Bohnsack, J.F., Kleinman, H., Takahashi, T., O’Shea, J.J, and Brown, E.J., 1990b, Connective tissue proteins and phagocytic cell function: laminin enhances complement and Fc-mediated phagocytosis by cultured human macrophages. J. Exp. Med. 161:912–923.

    Article  Google Scholar 

  • Bohnsack, J.F., O’Shea, J.J., Takahashi, T., and Brown, E J., 1985, Fibronectin-enhanced phagocytosis of an alternative pathway activator by human culture-derived macrophages is mediated by the C4b/C3b complement receptor (CRI). J. Immunol. 135:2680–2686.

    PubMed  CAS  Google Scholar 

  • Brown, E.J., 1986, The interaction of connective tissue proteins with phagocytic cells. J. Leuk. Biol. 39:579–591.

    CAS  Google Scholar 

  • Brown, E J. and Goodwin, J.L., 1988, Fibronectin receptors of phagocytes: characterization of the arg-gly-asp binding proteins of human monocytes and polymorphonuclear leukocytes. J.Exp.Med. 167:777–793.

    Article  PubMed  CAS  Google Scholar 

  • Brown, E.J., Hooper, L., Ho, T., and Gresham, H., 1990, Integrin-associated protein: A 50-kD plasma membrane antigen physically and functionally associated with integrins. J. Cell Biol. 111:2785–2794.

    Article  PubMed  CAS  Google Scholar 

  • Brown, P. and Juliano, R.L., 1985, Selective inhibition of fibronectin-mediated cell adhesion by monoclonal antibodies to a cell-surface glycoprotein. Science 1448–1450.

    Google Scholar 

  • Carreno, M.P., Gresham, H.D., and Brown, E.J., 1991, Characterization of a novel integrin involved in regulation of phagocytosis. FASEB J. 5:A549 (abstract).

    Google Scholar 

  • Carreno, M.P., Gresham, H.D., and Brown, E.J., 1992, Isolation of a novel integrin involved in regulation of phagocytosis. FASEB J. 6:A1410 (abstract).

    Google Scholar 

  • Chakravarti, S., Tarn, M.F., and Chung, A.E., 1990, The basement membrane glycoprotein entactin promotes cell attachment and binds calcium ions. J. Biol. Chem. 265:10597–10603.

    PubMed  CAS  Google Scholar 

  • Chung, A.E. and Durkin, M.E., 1990, Entactin: Structure and function. Am. J. Respir. Cell Mol. Biol. 3:275–282.

    PubMed  CAS  Google Scholar 

  • Devereux, I., Haeberli, P., and Smithies, O., 1984, A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387–395.

    Article  PubMed  CAS  Google Scholar 

  • Durkin, M.E., Chakravarti, S., Bartos, B.B., Liu, S.H., Friedman, R.L., and Chung, A.E., 1988, Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor. J. Cell Biol. 107:2749–2756.

    Article  PubMed  CAS  Google Scholar 

  • Durum, S.K. and Oppenheim, J.J., 1989, Macrophage-derived mediators: Interleukin 1, tumor necrosis factor, interleukin 6, interferon, and related cytokines, in: “Fundamental Immunology,” WE. Paul, ed., Raven Press, New York, pp. 639–662.

    Google Scholar 

  • Ferguson, T.A., Mizutani, H., and Kupper, T.S., 1991, Two integrin-binding peptides abrogate T cell-mediated immune responses in vivo. Proc. Natl. Acad. Sci. USA 88:8072–8076.

    Article  PubMed  CAS  Google Scholar 

  • Frelinger, A.L.,III, Du, X., Plow, E.F., and Ginsberg, M.H., 1991, Monoclonal antibodies to ligand-occupied conformers of integrin αIIbβ3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. J. Biol. Chem. 266:17106–17111.

    PubMed  CAS  Google Scholar 

  • Gresham, H.D., Adams, S.P., and Brown, E.J., 1992, Ligand binding specificity of the leukocyte response integrin expressed by human neutrophils. J. Biol. Chem. (in press).

    Google Scholar 

  • Gresham, H.D. and Brown, E.J., 1989, Molecular mechanism of fibronectin-stimulated neutrophil phagocytosis. J. Leuk. Biol. 46:310 (abstract).

    Google Scholar 

  • Gresham, H.D. and Brown, E.J., 1990, Fibrinogen gamma chain peptide KQAGDV stimulates neutrophil phagocytosis. Clin. Res. 38:480a (abstract).

    Google Scholar 

  • Gresham, H.D., Goodwin, J.L., Anderson, D.C., and Brown, E.J., 1989, A novel member of the integrin receptor family mediates arg-gly-asp-stimulated neutrophil phagocytosis. J. Cell Biol. 108:1935–1943.

    Article  PubMed  CAS  Google Scholar 

  • Hemler, M.E., Huang, C., and Schwarz, L., 1987, The VLA protein family: Characterization of five distinct cell surface heterodimers each with a common 130,000 molecular weight beta subunit. J. Biol. Chem. 262:3300–3309.

    PubMed  CAS  Google Scholar 

  • Horazdovsky, B.F. and Hogg, R.W., 1987, High-affinity L-arabinose transport operon. Gene product expression and mRNAs. J. Mol. Biol. 197:27–35.

    Article  PubMed  CAS  Google Scholar 

  • Horazdovsky, B.F. and Hogg, R.W., 1989, Genetic reconstitution of the high-affinity L-arabinose transport system. J. Bacteriol. 171:3053–3059.

    PubMed  CAS  Google Scholar 

  • Hynes, R.O., 1992, Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69:11–25.

    Article  PubMed  CAS  Google Scholar 

  • Kozak, M., 1989, The scanning model for translation: An update. J. Cell Biol. 108:229–241.

    Article  PubMed  CAS  Google Scholar 

  • Krissansen, G.W., Elliott, Ml, Lucas, C.M., et al., 1990, Identification of a novel integrin β subunit expressed on cultured monocytes (macrophages): Evidence that one α subunit can associate with multiple β subunits. J. Biol. Chem. 265:823–830.

    PubMed  CAS  Google Scholar 

  • Loike, J.D., Sodeik, B., Cao, L., et al., 1991, CD11c/CD18 on neutrophils recognizes a domain at the N terminus of the Aα chain of fibrinogen. Proc. Natl. Acad. Sci. USA 88:1044–1048.

    Article  PubMed  CAS  Google Scholar 

  • Maxfield, S.R., Moulder, K., Koning, F., et al., 1989, Murine T cells express a cell surface receptor for multiple extracellular matrix proteins. J. Exp. Med. 169:2173–2190.

    Article  PubMed  CAS  Google Scholar 

  • Mecham, R.P. Laminin receptors. Annu. Rev. Cell Biol. 7:71–91.

    Google Scholar 

  • Moulder, K., Roberts, K., Shevach, E.M., and Coligan, J.E., 1991, The mouse vitronectin receptor is a T cell activation antigen. J. Exp. Med. 173:343–347.

    Article  PubMed  CAS  Google Scholar 

  • Nathan, C. and Sanchez, E., 1990, Tumor necrosis factor and CDl 1/CD18 (2) integrins act synergistically to lower cAMP in human neutrophils. J. Cell Biol. 111:2171–2181.

    Article  PubMed  CAS  Google Scholar 

  • Nathan, C., Srimal, S., Farber, C., et al., 1989, Cytokine-induced respiratory burst of human neutrophils: dependence on extracellular matrix proteins and CDl 1/CD18 integrins. J. Cell Biol. 109:1341–1349.

    Article  PubMed  CAS  Google Scholar 

  • Neff, N.T., Lowrey, C., Decker, C., et al., 1982, A monoclonal antibody detaches embryonic skeletal muscle from extracellular matrices. J. Cell Biol. 95:654–666.

    Article  PubMed  CAS  Google Scholar 

  • Noda, M., Ikeda, T., Suzuki, H., et al., 1986, Expression of functional sodium channels from cloned cDNA. Nature 322:826–828.

    Article  PubMed  CAS  Google Scholar 

  • Numa, S. and Noda, M., 1986, Molecular structure of sodium channels. Ann. NY Acad. Sci. 479:338–355.

    Article  PubMed  CAS  Google Scholar 

  • O’Toole, T.E., Loftus, J.C, Du, X., et al., 1990, Affinity modulation of the αIIbβ3 integrin (platelet GPIIb-IIIa) is an intrinsic property of the receptor. Cell Regulation 1:883–893.

    PubMed  Google Scholar 

  • Patel, V.P., Ciechanover, A., Platt, O., and Lodish, H.F., 1985, Mammalian reticulocytes lose adhesion to fibronectin during maturation to erythrocytes. Proc. Natl. Acad. Sci. USA 82:440–444.

    Article  PubMed  CAS  Google Scholar 

  • Patel, V.P. and Lodish, H.F., 1984, Loss of adhesion of murine erythroleukemia cells to fibronectin during erythroid differentiation. Science 224:996–998.

    Article  PubMed  CAS  Google Scholar 

  • Patel, V.P. and Lodish, H.F., 1986, The fibronectin receptor on mammalian erythroid precursor cells: characterization and developmental regulation. J. Cell Biol. 102:449–456.

    Article  PubMed  CAS  Google Scholar 

  • Pearson, W.R. and Lipman, D.J., 1988, Improved tools for biological sequence comparison. Proc. Natl. Acad Sci. USA 85:2444–2448.

    Article  PubMed  CAS  Google Scholar 

  • Pierschbacher, M.D. and Ruoslahti, E., 1984, Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309:30.

    Article  PubMed  CAS  Google Scholar 

  • Pommier, C.G., Inada, S., Fries, L.F., Takahashi, T., Frank, M.M., and Brown, E.J., 1983, Plasma fibronectin enhances phagocytosis of opsonized particles by human peripheral blood monocytes. J. Exp. Med 157:1844–1854.

    Article  PubMed  CAS  Google Scholar 

  • Pommier, C.G., et al., 1984, Differentiation stimuli induce receptors for plasma fibronectin on the human myelomonocytic cell line HL-60. Blood 64:858–866.

    PubMed  CAS  Google Scholar 

  • Pommier, C.G., O’Shea, J.J., et al., 1984, Studies of the fibronectin receptors of human peripheral blood leukocytes. Morphologic and functional characterization. J. Exp. Med 159:137–151.

    Article  PubMed  CAS  Google Scholar 

  • Posnett, D.N., McGrath, H., and Tarn, J.P., 1988, A novel method for producing antipeptide antibodies: production of site-specific antibodies to the T cell antigen receptor β chain. J. Biol. Chem. 263:1719–1725.

    PubMed  CAS  Google Scholar 

  • Pytela, R., Pierschbacher, M.D., and Ruoslahti, E., 1985, Identification and isolation of a 140kd cell surface glycoprotein with properties expected of a fibronectin receptor. Cell 40:191–196.

    Article  PubMed  CAS  Google Scholar 

  • Rosales, C., Gresham, H.D., and Brown, E.J., 1992, Expression of the 50kD integrin associated protein on myeloid cells and erythrocytes. J. Immunol.(in press).

    Google Scholar 

  • Rosen, H., Milon, G., and Gordon, S., 1989, Antibody to the murine type 3 complement receptor inhibits T lymphocyte-dependent recruitment of myelomonocytic cells in vivo. J. Exp. Med 169:535–548.

    Article  PubMed  CAS  Google Scholar 

  • Santoro, S.A. and Lawing, W.J., Jr., 1987, Competition for related but nonidentical binding sites on the glycoprotein IIb-IIIa complex by peptides derived from platelet adhesive proteins. Cell 48:867–873.

    Article  PubMed  CAS  Google Scholar 

  • Savill, J., Dransfield, I., Hogg, N., and Haslett, C., 1990, Vitronectin receptor-mediated phagocytosis of cells undergoing apoptosis. Nature 343:170–173.

    Article  PubMed  CAS  Google Scholar 

  • Scripture, J.B., Voelker, C., Miller, S., et al., 1987, High-affinity L-arabinose transport operon. Nucleotide sequence and analysis of gene products. J. Mol. Biol. 197:37–46.

    Article  PubMed  CAS  Google Scholar 

  • Silverstein, S.C., Greenberg, S., Di Virgilio, F., and Steinberg, T.H., 1989, Phagocytosis, in: “Fundamental Immunology,” W.E. Paul, ed., Raven Press Ltd., New York, pp. 703–720.

    Google Scholar 

  • Singer, I.I., Scott, S., Kawka, D.W., and Kazazis, D.M., 1989, Adhesomes: Specific granules containing receptors for laminin, C3bi/fibrinogen, fibronectin, and vitronectin in human polymorphonuclear leukocytes and monocytes. J. Cell Biol. 109:3169–3182.

    Article  PubMed  CAS  Google Scholar 

  • Tamkun, J.W., Desimone, D.W., Fonda, D., et al., 1986, Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin. Cell 46:271–282.

    Article  PubMed  CAS  Google Scholar 

  • Unanue, E.R. and Allen, P.M., 1987, The basis for the immunoregulatory role of macrophages and other accessory cells. Science 236:551–557.

    Article  PubMed  CAS  Google Scholar 

  • Vedder, N.B., Winn, R.K., Rice, C.L., Chi, E.Y., Arfors, K.-E., and Harlan, J.M. A monoclonal antibody to the adherence-promoting leukocyte glycoprotein, CD 18, reduces organ injury and improves survival from hemorrhagic shock and resuscitation in rabbits. J. Clin. Invest. 81:939–944, 1988.

    Article  PubMed  CAS  Google Scholar 

  • Vedder, N.B., Winn, R.K., Rice, C.L., Chi, E.Y., Arfors, K.-E., and Harlan, J.M., 1990, Inhibition of leukocyte adherence by anti-CD 18 monoclonal antibody attenuates reperfiision injury in the rabbit ear. Proc. Natl. Acad. Sci. USA 87:2643–2646.

    Article  PubMed  CAS  Google Scholar 

  • Vercellotti, G.M., McCarthy, J., Furcht, L.T., Jacob, H.S., and Moldow, C.F., 1983, Inflamed fibronectin: An altered fibronectin enhances neutrophil adhesion. Blood 62:1063–1069.

    PubMed  CAS  Google Scholar 

  • Wright, S.D., Craigmyle, L.S., and Silverstein, S.C., 1983, Fibronectin and serum amyloid P-component stimulate C3b-and C3bi-mediated phagocytosis in cultured human monocytes. J.Exp.Med. 158:1338–1342.

    Article  PubMed  CAS  Google Scholar 

  • Wright, S.D., Licht, M.R., Craigmyle, L.S., and Silverstein, S.C., 1984, Communication between receptors for different ligands on a single cell: Ligation of fibronectin receptors induces a reversible alteration in the fonction of complement receptors on cultured human monocytes. J. Cell Biol. 99:336–339.

    Article  PubMed  CAS  Google Scholar 

  • Wright, S.D. and Meyer, B.C., 1985, Fibronectin receptor of human macrophages recognize the sequence arg-gly-asp-ser. J. Exp. Med. 162:762–767.

    Article  PubMed  CAS  Google Scholar 

  • Wright, S.D., Weitz, J.I., Huang, A.J., Levin, S.M., Silverstein, S C, and Loike, J.D., 1988, Complement receptor type three (CD11b/CD18) of human polymorphonuclear leukocytes recognizes fibrinogen. Proc. Natl. Acad. Sci. USA 85:7734–7738.

    Article  PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Departments of Medicine, Cell Biology and Physiology, and Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri, USA

    Eric J. Brown

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  1. Eric J. Brown
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Editor information

Editors and Affiliations

  1. Dana-Farber Cancer Institute, Boston, Massachusetts, USA

    Martin E. Hemler

  2. Roswell Park Cancer Institute, Buffalo, New York, USA

    Enrico Mihich

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© 1993 Plenum Press, New York

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Brown, E.J. (1993). Signal Transduction from Leukocyte Integrins. In: Hemler, M.E., Mihich, E. (eds) Cell Adhesion Molecules. Pezcoller Foundation Symposia, vol 4. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2830-2_8

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  • DOI: https://doi.org/10.1007/978-1-4615-2830-2_8

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-0-306-44496-8

  • Online ISBN: 978-1-4615-2830-2

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