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  Identification of a putative cell adhesion domain of uvomorulin

Vestweber, D., & Kemler, R. (1985). Identification of a putative cell adhesion domain of uvomorulin. EMBO Journal, 4(13A), 3393-3398. doi:10.1002/j.1460-2075.1985.tb04095.x.

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Vestweber, D1, Author                 
Kemler, R1, Author           
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1Kemler Group, Friedrich Miescher Laboratory, Max Planck Society, ou_3481124              

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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.

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 Dates: 1985-12
 Publication Status: Issued
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 Rev. Type: -
 Identifiers: DOI: 10.1002/j.1460-2075.1985.tb04095.x
PMID: 2419126
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Title: EMBO Journal
  Other : EMBO J.
Source Genre: Journal
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Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 4 (13A) Sequence Number: - Start / End Page: 3393 - 3398 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061