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. 1976 Jun;24(3):435–440.

Immunological studies of human placentae. Lectin binding to villous stroma and to trophoblastic basement membrane.

P M Johnson, W P Faulk
PMCID: PMC1538524  PMID: 181190

Abstract

It has been demonstrated immunohistologically using cryostat sections that the lectins PHA and Con A bind to human placentae. Both lectins stain trophoblastic basement membrane (TBM), perivascular tissue and stroma. No staining of trophoblasts was observed. It has been shown by blocking experiments that the lectin binding sites on placental TBM are glycoproteins, whereas experiments involving pretreatment of placental sections with anti-collagen antisera or highly purified bacterial collagenase have indicated that lectin binding to stromal and perivascular structures is collagen-associated. The possible relation of TBM lectin-binding sites to immune response gene products is briefly discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arbeit R. D., Sachs D. H., Amos D. B., Dickler H. B. Human lymphocyte alloantigen(s) similar to murine Ir region-associated (Ia) antigens. J Immunol. 1975 Oct;115(4):1173–1175. [PubMed] [Google Scholar]
  2. Beer A. E., Billingham R. E., Yang S. L. Further evidence concerning the autoantigenic status of the trophoblast. J Exp Med. 1972 May 1;135(5):1177–1184. doi: 10.1084/jem.135.5.1177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bornstein P., Piez K. A. The nature of the intramolecular cross-links in collagen. The separation and characterization of peptides from the cross-link region of rat skin collagen. Biochemistry. 1966 Nov;5(11):3460–3473. doi: 10.1021/bi00875a012. [DOI] [PubMed] [Google Scholar]
  4. Bradbury S., Billington W. D., Kirby D. R., Williams E. A. Surface mucin of human trophoblast. Am J Obstet Gynecol. 1969 Jun 1;104(3):416–418. doi: 10.1016/s0002-9378(16)34195-3. [DOI] [PubMed] [Google Scholar]
  5. Curzen P. The antigenicity of the human placenta. Proc R Soc Med. 1970 Jan;63(1):65–66. [PMC free article] [PubMed] [Google Scholar]
  6. Faulk W. P., Conochie L. B., Temple A., Papamichail M. Immunobiology of membrane-bound collagen on mouse fibroblasts. Nature. 1975 Jul 10;256(5513):123–125. doi: 10.1038/256123a0. [DOI] [PubMed] [Google Scholar]
  7. Faulk W. P., Hijmans W. Recent developments in immunofluorescence. Prog Allergy. 1972;16:9–39. doi: 10.1159/000393067. [DOI] [PubMed] [Google Scholar]
  8. Faulk W. P., Jeannet M., Creighton W. D., Carbonara A. Immunological studies of the human placenta. Characterization of immunoglobulins on trophoblastic basement membranes. J Clin Invest. 1974 Nov;54(5):1011–1019. doi: 10.1172/JCI107844. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. GOLDSTEIN I. J., HOLLERMAN C. E., SMITH E. E. PROTEIN-CARBOHYDRATE INTERACTION. II. INHIBITION STUDIES ON THE INTERACTION OF CONCANAVALIN A WITH POLYSACCHARIDES. Biochemistry. 1965 May;4:876–883. doi: 10.1021/bi00881a013. [DOI] [PubMed] [Google Scholar]
  10. Gaugas J. M. Glycoproteins in pregnancy serum which interact with concanavalin A and may suppress lymphocyte transformation. Transplantation. 1974 Dec;18(6):538–541. [PubMed] [Google Scholar]
  11. Inbar M., Sachs L. Interaction of the carbohydrate-binding protein concanavalin A with normal and transformed cells. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1418–1425. doi: 10.1073/pnas.63.4.1418. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Johnson P. M., Trenchev P., Faulk W. P. Immunological studies of human placentae. Binding of complexed immunoglobulin by stromal endothelial cells. Clin Exp Immunol. 1975 Oct;22(1):133–138. [PMC free article] [PubMed] [Google Scholar]
  13. Loke Y. W., Joysey V. C., Borland R. HL-A antigens on human trophoblast cells. Nature. 1971 Aug 6;232(5310):403–405. doi: 10.1038/232403a0. [DOI] [PubMed] [Google Scholar]
  14. McCormick J. N., Faulk W. P., Fox H., Fudenberg H. H. Immunohistological and elution studies of the human placenta. J Exp Med. 1971 Jan 1;133(1):1–18. doi: 10.1084/jem.133.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Nicolson G. L. The interactions of lectins with animal cell surfaces. Int Rev Cytol. 1974;39:89–190. doi: 10.1016/s0074-7696(08)60939-0. [DOI] [PubMed] [Google Scholar]
  16. Pflumm M. N., Wang J. L., Edelman G. M. Conformational changes in concanavalin A. J Biol Chem. 1971 Jul 10;246(13):4369–4370. [PubMed] [Google Scholar]
  17. Poulik M. D., Ferrone S., Pellegrino M. A., Sevier D. E., Oh S. K., Reisfeld R. A. Association of HL-A antigens and beta 2-microglobulin: concepts and questions. Transplant Rev. 1974;21(0):106–125. doi: 10.1111/j.1600-065x.1974.tb01548.x. [DOI] [PubMed] [Google Scholar]
  18. Sharon N., Lis H. Lectins: cell-agglutinating and sugar-specific proteins. Science. 1972 Sep 15;177(4053):949–959. doi: 10.1126/science.177.4053.949. [DOI] [PubMed] [Google Scholar]
  19. Shreffler D. C., David C. S. The H-2 major histocompatibility complex and the I immune response region: genetic variation, function, and organization. Adv Immunol. 1975;20:125–195. doi: 10.1016/s0065-2776(08)60208-4. [DOI] [PubMed] [Google Scholar]
  20. Winchester R. J., Wernet P., Kunkel H. G., Dupont B., Jersild C., Fu S. M. Recognition by pregnancy serums of non-HL-A alloantigens selectively expressed on B lymphocytes. J Exp Med. 1975 Apr 1;141(4):924–929. [PMC free article] [PubMed] [Google Scholar]

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