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Lymphocyte Migration Molecules

  • Sirpa Jalkanen
  • Robert Bargatze
  • Markku Jalkanen
  • David Lewinsohn
  • Philip Streeter
  • Ellen Lakey
  • Eugene C. Butcher
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 237)

Abstract

Recirculating lymphocytes leave the blood by selectively binding to specialized high endothelial venules (HEV) in the lymphoid organs of the body1. This binding is mediated by specific lymphocyte surface molecules called homing receptors2. Functionally distinct homing receptors control lymphocyte migration to peripheral lymph nodes, to mucosa-associated lymphatic tissues (appendix, Peyer’s patches) or to inflamed joint tissue (synovium)3,4. Most virgin lymphocytes appear to express all three different types of receptors and can, therefore, migrate throughout the body in search of antigen. Following antigenic activation the lymphocytes go through a nonmigratory phase after which many of them, as memory and effector cells, appear to express a single homing receptor class that controls their migration to particular tissues of the body similar to the site where they first encountered their cognate antigen. Thus, organ-specific homing receptors are thought to play an essential role in determining the characteristics of local immune responses2,5.

Keywords

Sialic Acid Peripheral Lymph Node High Endothelial Venule Lymphocyte Migration Homing Receptor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    J.L. Gowans, and E.J. Knight, The route of recirculation of lymphocytes in the rat, Proc. Roy. Soc. Ser. B. 15 9: 257 (1964).Google Scholar
  2. 2.
    E.C. Butcher, The regulation of lymphocyte traffic, Curr. Top. Microbiol. Immunol. 128: 85 (1986).PubMedCrossRefGoogle Scholar
  3. 3.
    E.C. Butcher, R.G. Scollay, and I.L. Weissman, Organ specificity of lymphocyte migration: Mediation by highly selective lymphocyte interaction with organ-specific determinants on high endothelial venules, Eur. J. Immunol. 10: 556 (1980).PubMedCrossRefGoogle Scholar
  4. 4.
    S. Jalkanen, A.C. Steere, R.I Fox, and E.C. Butcher, A distinct endothelial cell recognition system controlling lymphocyte traffic into inflamed synovium, Science 233: 556 (1986).PubMedCrossRefGoogle Scholar
  5. 5.
    S. Jalkanen, R.A. Reichert, W.M. Gallatin, R.F. Bargatze, I.L. Weissman, and E.C. Butcher, Homing receptors and the control of lymphocyte migration, Immunol. Rev. 91: 39 (1986).PubMedCrossRefGoogle Scholar
  6. 6.
    W.M. Gallatin, I.L. Weissman, and E.C. Butcher, A cell surface molecule involved in organ-specific homing of lymphocytes. Nature 303: 30 (1983).CrossRefGoogle Scholar
  7. 7.
    R.A. Rasmussen, Y-H Chin, J.J. Woodruff, and T.G. Easton, Lymphocyte recognition of lymph node high endothelium. VII. Cell surface proteins involved in adhesion defined by monoclonal anti-HEBFLN (A.11) antibody, J. Immunol. 135: 19 (1985).PubMedGoogle Scholar
  8. 8.
    Y-H. Chin, R.A. Rasmussen, J.J. Woodruff, and T.G. Easton, A monoclonal anti-HEBF antibody with specificity for lymphocyte surface molecules mediating adhesion to Peyer’s patch high endothelium of the rat, J. Immunol. 136: 1 (1986).Google Scholar
  9. 9.
    S. Jalkanen, R. Bargatze, L. Herron, and E.C. Butcher, A lymphoid cell surface glycoprotein involved in endothelial recognition and lymphocyte homing in man, Eur. J. Immunol. 16: 1195 (1986).PubMedCrossRefGoogle Scholar
  10. 10.
    S. Jalkanen, R.F. Bargatze, J. de los Toyos, and E.C. Butcher. Lymphocyte recognition of high endothelium: antibodies to distinct epitopes of an 85–95 kD glycoprotein antigen differ-entially inhibit lymphocyte binding to lymph node, mucosal, or synovial endothelial cells, J. Cell. Biol. 105: 983 (1987).PubMedCrossRefGoogle Scholar
  11. 11.
    S. Jalkanen, R. Bargatze, M. Jalkanen, M. Tammi, and E.C. Butcher, Biochemical properties of glycoproteins involved in lymphocyte recognition of high endothelial venules in man, submitted.Google Scholar
  12. 12.
    M. Siegelman, M. Bond, W.M. Gallatin, T. St. John, H. Smith, V. Fried, and I.L. Weissman, A putative lymphocyte homing receptor is a ubiquitinated branched-chain glycoprotein: Additional cell surface proteins also appear ubiquitinated, Science 231: 823 (1986).PubMedCrossRefGoogle Scholar
  13. 13.
    T. St. John, W.M. Gallatin, M. Siegelman, H.T. Smith, V.A. Fried, and I.L. Weissman, Expression cloning of a lymphocyte homing receptor cDNA: Ubiquitin is the reactive species, Science 231: 845 (1986).PubMedCrossRefGoogle Scholar
  14. 14.
    A. Hershko, Ubiquitin: Roles in protein modification and breakdown, Cell 34: 11 (1983).PubMedCrossRefGoogle Scholar
  15. 15.
    A. Ciechanover, D. Finley, and A. Varshavsky, The ubiquitinmediated proteolytic pathway and mechanisms of energy dependent intracellular protein degradation, J. Cell. Biochem. 24: 27 (1984).PubMedCrossRefGoogle Scholar
  16. 16.
    A. Bachmeir, D. Finley, and A. Varshavsky, In vivo half-life of a protein is a function of its amino-terminal residue, Science 234: 179 (1986).CrossRefGoogle Scholar
  17. 17.
    H.B. Stamper Jr, and J.J. Woodruff, Lymphocyte homing into lymph nodes: In vitro demonstration of the selective affinity of recirculating lymphocytes for high endothelial venules, J. Exp. Med. 144: 828 (1976).PubMedCrossRefGoogle Scholar
  18. 18.
    S. Jalkanen, and E.C. Butcher, In vitro analysis of the homing properties of human lymphocytes: Developmental regulation of functional receptors for high endothelial venules, Blood 66: 577 (1985).PubMedGoogle Scholar
  19. 19.
    J.J. Woodruff, M. Katz, E. Lucas, and H.B. Stamber Jr, An in vitro model of lymphocyte homing.II.Membrane and cytoplasmic events involved in lymphocyte adherence to specialized high-endothelial venules of lymph nodes, J. Immunol. 119: 1603 (1977).PubMedGoogle Scholar
  20. 20.
    D.M. Lewinsohn, R.F. Bargatze, and E.C. Butcher, Leukocyte-endothelial cell recognition: evidence of a common molecular mechanism shared by neutrophils, lymphocytes, and other leukocytes, J. Immunol. 138: 4313 (1987).PubMedGoogle Scholar
  21. 21.
    J.M. Harlan, P.D. Killen, F.M. Senecal, B.R. Schwartz, E.K. Yee, R.F. Taylor, P.G. Beatty, T.H. Price, and H.D. Ochs, The role of neutrophil membrane glycoprotein GP-150 in neutrophil adherence to endothelium in vitro, Blood 69: 338 (1985).Google Scholar
  22. 22.
    K.E. Arfors, C. Lundberg, L. Lindbom, K. Lundberg, P.G. Beatty, A monoclonal antibody to the membrane glycoprotein complex CD18 inhibits polymorphonuclear leukocyte accumulation and plasma leakage in vivo, Blood 69: 338 (1987)PubMedGoogle Scholar
  23. 23.
    L.M. Stoolman, T.S. Tenforde, and S.D. Rosen, Phosphomannosyl receptors may participate in the adhesive interaction between lymphocytes and high endothelial venules, J. Cell Biol. 99: 1535 (1984).PubMedCrossRefGoogle Scholar
  24. 24.
    S.D. Rosen, M.S. Singer, T.A. Yednock, and L.M. Stoolman, Involvement of sialic acid on endothelial cells in organ-specific lymphocyte recirculation, Science 228: 1005 (1985).PubMedCrossRefGoogle Scholar
  25. 25.
    T.A. Yednock, E.C. Butcher, L.M. Stoolman, S.D. Rosen, Lymphocyte homing receptors: relationship between MEL-14 antigen and a carbohydrate-binding receptor, J. Cell. Biol. 104: 725 (1987).PubMedCrossRefGoogle Scholar
  26. 26.
    A.D. Duijvestijn, A. Schreiber, and E.C. Butcher, Interferongamma induces an antigen specific for endothelium involved in lymphocyte homing, PNAS 83: 9114 (1986).PubMedCrossRefGoogle Scholar
  27. 27.
    P. Streeter, E. Lakey, R.F. Bargatze, B.T. Rouse, and E.C. Butcher, A tissue-specific endothelial cell molecule involved in lymphocyte homing to mucosal tissues, submitted.Google Scholar
  28. 28.
    A.D. Duijvestijn, E. Horst, S.T. Pals, B.T. Rouse, A. Steere, L. Picker, C.J.M. Meijer, and E.C. Butcher, High endothelial differentiation in human lymphoid and inflammatory tissue defined by monoclonal antibody HECA-452. Am. J. Path., in press.Google Scholar

Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Sirpa Jalkanen
    • 1
  • Robert Bargatze
    • 2
  • Markku Jalkanen
    • 3
  • David Lewinsohn
    • 2
  • Philip Streeter
    • 2
  • Ellen Lakey
    • 2
  • Eugene C. Butcher
    • 2
  1. 1.Department of Medical MicrobiologyTurku UniversityTurkuFinland
  2. 2.Department of Pathology, Stanford University Medical CenterStanford UniversityStanfordUSA
  3. 3.Department of BiochemistryTurku UniversityTurkuFinland

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