The Histochemical Journal

, Volume 26, Issue 7, pp 582–586 | Cite as

Immunohistochemical localization of a β-d-galactoside-binding lectin at the human maternofetal interface

  • B. H. Bevan
  • D. C. Kilpatrick
  • W. A. Liston
  • J. Hirabayashi
  • K. Kasai
Papers

Summary

The 14 kD S-type lectin from human placenta may have a role in regulating the maternal immune response to fetal antigens. In this study, an immunoperoxidase technique was used to determine the distribution of the lectin at the human maternofetal interface. Tissue obtained during the first trimester of pregnancy and at term was used. The lectin was not detectable in either the villous syncytiotrophoblast or the underlying cytotrophoblast in first-trimester tissue, although some cells of the cytotrophoblast columns were reactive. It was also not detectable in villous or extravillous trophoblast populations at term. In contrast, strong reactivity was found in decidual stromal cells throughout gestation, and endometrial stromal cells were also positive. The lectin is, therefore, not a component of the immunosuppressive factors associated with syncytiotrophoblast membranes, but may have a role in either the decidual control of trophoblast migration or some functions unrelated to pregnancy, or both.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Braunstein, G. D. (1992) Editors formulation. Sem. Reprod. Endocrinol. 10, 180–2.Google Scholar
  2. Butterworth, B. H., Greer, I. A., Liston, W. A., Haddad, N. G. & Johnston, T. A. (1991) Immunocytochemical localisation of neutrophil elastase in term placenta decidua and myometrium in pregnancy-induced hypertension. Br. J. Obstet. Gynaecol. 98, 929–33.Google Scholar
  3. Catt, J. W. & Harrison, F. L. (1985) Selective association of an endogenous lectin with connective tissues. J. Cell Sci. 73, 347–59.Google Scholar
  4. Catt, J. W., Harrison, F. L. & Carleton, J. S. (1987) Distribution of an endogenous β-galactoside specific lectin during foetal and neonatal rabbit developmental. J. Cell Sci. 87, 623–33.Google Scholar
  5. Dalchau, R., Kirkley, J. & Fabre, J. W. (1980) Monoclonal antibody to a human leucocyte-specific membrane glycoprotein probably homologus to the leucocyte-common (L-C) antigen of the rat. Eur. J. Immunol. 10, 737–74.Google Scholar
  6. Harrison, F. L. (1991) Soluble β-galactoside-binding lectins in vertebrates. In: Lectin Reviews, (edited by Kilpatrick, D. C., VanDriessche, E. & Bog-Hansen, T. C.) Vol 1, pp. 17–39. St Louis: Sigma Chemical Co.Google Scholar
  7. Hirabayashi, J. & Kasai, K. (1984) Human placenta galactoside-binding lectin. Biochem. Biophys. Res. Commun. 122, 938–44.Google Scholar
  8. Hirabayashi, J. & Kasai, K. (1988) Complete amino acid sequence of a β-galactoside-binding lectin from human placenta. J. Biochem. (Tokyo) 104, 1–4.Google Scholar
  9. Kajikawa, T., Nakajima, Y., Hirabayashi, J., Kasai, K. & Yamazaki, M. (1986) Release of cytotoxin by macrophages on treatment with human placental lectin. Life Sci. 39, 1177–81.Google Scholar
  10. Kaneko, M., Hirabayashi, J., Oda, Y. & Kasai, K. (1990) β-D-Galactoside-binding lectin of human umbilical cord: purification characterization, and distribution. Lectins Biol. Biochem. Clin. Biochem. 7, 77–82.Google Scholar
  11. Lalmanach-Girard, A. C., Thibault, G., Lacord, M., Degenne, D. & Bardos, P. (1992) Lipid and protein components of the syncytiotrophoblast plasma membrane inhibit lymphocyte proliferation by two distinct pathways. Immunol. Lett. 32, 131–8.Google Scholar
  12. Levi, G., Tarrab-Hazdai, R. & Teichberg, V. I. (1983) Prevention and therapy with electrolectin of experimental autoimmune myasthenia gravis in rabbits. Eur. J. Immunol. 13, 500–7.Google Scholar
  13. Offner, H., Celnik, B., Bringman, T. S., Casentini-Borocz, D., Nedwin, G. E. & Vandenbark, A. A. (1990) Recombinant human β-galactoside binding lectin suppresses clinical and histological signs of experimental autoimmune encephalomyelitis. J. Neuroimmunol. 28, 177–84.Google Scholar
  14. Sharon, N. & Lis, H. (1989) Lectins as cell recognition molecules. Science 246, 227–34.Google Scholar
  15. Sternberger, L. A. & Joseph, S. A. (1979) The unlabeled antibody method: contrasting color staining of paired pituitary hormones without antibody removal. J. Histochem. Cytochem. 27, 1424–9.Google Scholar
  16. Thibault, G., Degenne, D., Girard, A. C., Guillaumin, J. M., Lacord, M. & Bardos, P. (1991) The inhibitory effect of human syncytiotrophoblast plasma membrane vesicles on in vitro lymphocyte proliferation is associated with reduced interleukin 2 receptor expression. Cell. Immunol. 138, 165–74.Google Scholar
  17. Wasano, K., Hirakawa, Y. & Yamamoto, T. (1990) Immuno-histochemical localization of 14 kDa β-galactoside-binding lectin in various organs of rat. Cell Tissue Res. 259, 43–9.Google Scholar
  18. Wells, V. & Mallucci, L. (1991) Identification of an autocrine negative growth factor; mouse β-galactoside-binding protein is a cytostatic factor and cell growth regulator. Cell 64, 91–7.Google Scholar

Copyright information

© Chapman & Hall 1994

Authors and Affiliations

  • B. H. Bevan
    • 1
  • D. C. Kilpatrick
    • 2
  • W. A. Liston
    • 3
  • J. Hirabayashi
    • 4
  • K. Kasai
    • 4
  1. 1.Department of AnatomyMedical SchoolEdinburghUK
  2. 2.Department of Transfusion MedicineEdinburghUK
  3. 3.Simpson Memorial Maternity Pavilion, Royal InfirmaryEdinburghUK
  4. 4.Department of Biological Chemistry, Faculty of Pharmaceutical SciencesTeiko UniversityKanagawaJapan

Personalised recommendations