Identification of a putative cell adhesion domain of uvomorulin

EMBO J. 1985 Dec 16;4(13A):3393-8. doi: 10.1002/j.1460-2075.1985.tb04095.x.


A rat monoclonal antibody (DECMA-1) selected against the murine cell adhesion molecule uvomorulin blocks both the aggregation of mouse embryonal carcinoma cells and the compaction of pre-implantation embryos. However, decompacted embryos eventually become recompacted in the presence of DECMA-1 and form blastocysts composed of both trophectoderm and inner cell mass. DECMA-1 also disrupts confluent monolayers of Madin-Darby canine kidney (MDCK) epithelial cells. DECMA-1 recognizes uvomorulin in extracts from mouse and dog tissues. Protease digestion of mouse and dog uvomorulin generated core fragments including one of 26 kd which reacted with DECMA-1. The same 26-kd fragment is recognized by anti-uvomorulin monoclonal antibodies which have been obtained from other laboratories and which dissociate MDCK cell monolayers and block the formation of the epithelial occluding barrier. This 26-kd fragment therefore seems to be involved in the adhesive function of uvomorulin.

MeSH terms

  • Animals
  • Antibodies, Monoclonal
  • Antibody Specificity
  • Antigens, Surface / immunology
  • Antigens, Surface / physiology*
  • Cadherins
  • Cell Adhesion Molecules
  • Cell Adhesion*
  • Cells, Cultured
  • Cleavage Stage, Ovum / cytology*
  • Dogs
  • Epithelial Cells
  • Epithelium / immunology
  • Epitopes
  • Fluorescent Antibody Technique
  • Glycoproteins / immunology
  • Glycoproteins / physiology*
  • Mice
  • Morula / cytology*
  • Peptide Fragments / immunology
  • Peptide Fragments / physiology


  • Antibodies, Monoclonal
  • Antigens, Surface
  • Cadherins
  • Cell Adhesion Molecules
  • Epitopes
  • Glycoproteins
  • Peptide Fragments