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The N-domain of the biliary glycoprotein (BGP) adhesion molecule mediates
homotypic binding: domain interactions and epitope analysis of BGPc
AM Teixeira, J Fawcett, DL Simmons and SM Watt
ICRF Medical Oncology Unit, St Bartholomew's Hospital, London, UK.
The biliary glycoproteins (BGPs) represent a group of at least eight
differentially spliced molecules belonging to the carcinoembryonic antigen
(CEA) subgroup of the CEA family. These molecules are recognized by the
CD66 monoclonal antibodies (MoAbs) and function as homotypic and
heterotypic adhesion molecules. The extracellular region of the BGPc splice
variant comprises an N-terminal IgV-like domain and three IgC2-set domains
(A1, B1, and A2). Using soluble recombinant BGP domain variants, we
demonstrate in this report that the N-terminal domain mediates homotypic
adhesion. Furthermore, this adhesion is both temperature- and
cation-dependent. The soluble domain variants of BGP are ideal molecules
for epitope mapping. Using these constructs, we have mapped 11 MoAbs that
react with the CEA family to different domains of BGPc and have shown that
the CD66 MoAbs, YTH71.3.2 and CLBgran 10 (M38), recognize epitopes in the
N-terminal domain.
Volume 84,
Issue 1,
pp. 211-219,
07/01/1994
Copyright © 1994 by The American Society of Hematology

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