Abstract
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,physiology
Cadherins
Cell Adhesion
Cell Adhesion Molecules
Cells, Cultured
Cleavage Stage, Ovum/cytology
Dogs
Epithelial Cells
Epithelium/immunology
Epitopes
Fluorescent Antibody Technique
Glycoproteins/immunology,physiology
Mice
Morula/cytology
Peptide Fragments/immunology,physiology
Chemicals
Antibodies, Monoclonal
Antigens, Surface
Cadherins
Cell Adhesion Molecules
Epitopes
Glycoproteins
Peptide Fragments
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Vestweber D
Kemler R
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