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CD66 identifies the biliary glycoprotein (BGP) adhesion molecule: cloning,
expression, and adhesion functions of the BGPc splice variant
SM Watt, J Fawcett, SJ Murdoch, AM Teixeira, SE Gschmeissner, NM Hajibagheri and DL Simmons
MRC Molecular Haematology Unit, Institute of Molecular Medicine, Oxford,
UK.
Within the hematopoietic lineage, the monoclonal antibody (MoAb) CD66
reacts with cells of the granulocyte lineage, but not with the majority of
progenitor cells from human bone marrow. Our previous studies have shown
that CD66 binds specifically to at least three carcinoembryonic antigen
(CEA) superfamily members, ie, CEA itself, nonspecific cross- reacting
antigen (NCA), and CGM1, but not to CGM6 (NCA-95). In this report, we show
that CD66 will also identify the biliary glycoproteins (BGP). A full-length
cDNA for the BGPc molecule (a cytoplasmic splice variant of BGPa) was
isolated by expression cloning using the CD66 MoAbs. This protein has an
identical extracellular and transmembrane sequence to BGPa with one
N-terminal IgV like domain, three IgC-like extracellular domains (A1, B1,
and A2), plus a transmembrane domain, but the cytoplasmic domain is spliced
by 53 nucleotides. Reverse transcriptase-polymerase chain reaction
experiments show that this splice variant can be detected in colonic
carcinoma cell lines, in primary colonic adenocarcinomas, and in myeloid
and B-cell lines to varying degrees. Quantitative analyses of BGPc RNA
expression by RNase protection indicate that abundant levels occur only in
the colonic, but not in the hematopoietic, cell lines tested. Studies
presented here show that BGPc mediates homotypic adhesion and suggest that
the cytoplasmic splicing does not alter the initial homotypic adhesion
properties of BGPa.
Volume 84,
Issue 1,
pp. 200-210,
07/01/1994
Copyright © 1994 by The American Society of Hematology
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