Molecular nature of the calcium-dependent cell-cell adhesion system in mouse teratocarcinoma and embryonic cells studied with a monoclonal antibody

Dev Biol. 1984 Jan;101(1):19-27. doi: 10.1016/0012-1606(84)90112-x.


The molecular nature of the Ca2+-dependent cell-cell adhesion system in mouse teratocarcinoma (t-CDS) was studied using a monoclonal antibody recognizing t-CDS. We isolated a hybridoma clone producing a monoclonal antibody (ECCD-1) able to disrupt cell-cell adhesion when added to monolayer cultures of teratocarcinoma cells. This antibody bound to the cells with intact t-CDS, resulting in an inhibition of their aggregation, but did not bind to cells from which t-CDS was removed by trypsin treatment in the absence of Ca2+. The binding of ECCD-1 to cell surfaces required Ca2+ but not other ions. Western blot analysis showed that ECCD-1 recognizes multiple cell surface proteins, the major one of which is a component with a molecular weight of 124,000. The binding of ECCD-1 to these antigens was Ca2+-dependent even in cell-free systems, suggesting that the molecules involved in t-CDS undergo conformational changes by binding with Ca2+, leading to conversion of their molecular structure into an active form. ECCD-1 also reacted with 8-cell stage mouse embryos and with certain types of epithelial cells (excluding fibroblastic cells) in various differentiated tissues collected from mouse fetuses, again affecting their cell-cell adhesion. We also showed that a monoclonal antibody (DE1) raised against gp84 (F. Hyafil et al., 1981, Cell 26, 447-454) recognizes the same antigens as ECCD-1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal
  • Antigens, Surface / immunology
  • Antigens, Surface / physiology*
  • Calcium / physiology*
  • Cell Adhesion Molecules
  • Cell Adhesion*
  • Cell Aggregation
  • Membrane Proteins / immunology
  • Membrane Proteins / physiology*
  • Mice / embryology*
  • Teratoma
  • Tissue Distribution


  • Antibodies, Monoclonal
  • Antigens, Surface
  • Cell Adhesion Molecules
  • Membrane Proteins
  • Calcium