A cell surface glycoprotein involved in the compaction of embryonal carcinoma cells and cleavage stage embryos

Cell. 1980 Oct;21(3):927-34. doi: 10.1016/0092-8674(80)90456-0.

Abstract

Fab fragments of rabbit anti-embryonal carcinoma cells IgG dramatically perturb cell-cell interactions between embryonal carcinoma cells and between early mouse embryo blastomeres. These antibodies prevent compaction of preimplantation embryos (or trigger their decompaction) and have similar effects on embryonal carcinoma cells. They probably act through the masking of specific molecules (Fab targets) involved in the mechanisms of recognition between cells during compaction. Fab target molecules have been extracted from embryonal carcinoma cell membranes and purified using their property to inhibit the effects mediated by anti-embryonal carcinoma Fab. The solubilization of the Fab targets could be achieved using both detergent extraction and trypsin treatment of membranes. In the latter case, a glycoprotein of 84,000 daltons could be purified which has all the properties expected from the Fab target and accounts for most of the Fab-inhibiting activity of embryonal carcinoma cell membranes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibody Specificity
  • Antigens, Surface / physiology
  • Blastocyst / physiology*
  • Cell Communication*
  • Cell Line
  • Epitopes*
  • Glycoproteins / physiology*
  • Immunoglobulin Fab Fragments / physiology*
  • Membrane Proteins / physiology*
  • Mice
  • Teratoma

Substances

  • Antigens, Surface
  • Epitopes
  • Glycoproteins
  • Immunoglobulin Fab Fragments
  • Membrane Proteins