Identification of a putative cell adhesion domain of uvomorulin.

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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.