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Blood, Vol. 93 No. 1 (January 1), 1999:
pp. 165-175
Biochemical Characterization and Molecular Cloning of a Novel
Endothelial-Specific Sialomucin
Suzanne Marie Morgan,
Ulrike Samulowitz,
Liz Darley,
David L. Simmons, and
Dietmar Vestweber
From the Cell Adhesion Group, Institute of Molecular Medicine, John
Radcliffe Hospital, and the Sir William Dunn School of Pathology,
University of Oxford, Oxford, UK; and the Institute of Cell Biology,
University of Münster, Münster, Germany.
We have generated rat monoclonal antibodies (MoAbs) against cell
surface antigens of the mouse endothelioma cell line bEND.3. Three
antibodies (V.1A7, V.5C7, and V.7C7) were selected, all of which
recognize a 75-kD antigen on bEND.3 cells and bind selectively to
endothelial cells in cryostat sections of mouse tissues. A cDNA for the
antigen was isolated from a bEND.3 pCDM8 expression library by using
transient expression in COS-7 cells and immunoselection with the three
MoAbs. This cDNA coded for a novel, type I membrane protein of 248 amino acids with an extracellular domain rich in threonine and serine
residues (35%). The protein is sensitive to O-sialoglycoprotein
endopeptidase, indicating that it belongs to the class of
sialomucin-like proteins. Therefore, we suggest the name endomucin.
Treatment of isolated endomucin by sialidase and O-glycosidase reduced
the apparent molecular weight to 45 kD and abolished binding of all
three antibodies, indicating that carbohydrates are directly or
indirectly involved in the formation of the antibody epitopes.
Immunohistological analysis of all examined mouse tissues showed that
endomucin is an endothelial antigen found in venous endothelium as well
as in capillaries, but not on arterial endothelium. Interestingly, high
endothelial venules of peripheral and mesenteric lymph nodes as well as
of Peyers's patches were negative for staining with the three MoAbs.
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