Several mouse monoclonal antibodies recognising different epitopes on human erythrocyte sialoglycoproteins
α and β (syn: glycophorins A and C, respectively) react with human renal endothelium. Those monoclonal
anti-blood group M and anti-blood group N antibodies which recognised the M/N epitopes on sialidase-treated
human erythrocytes also reacted with human renal endothelium whilst those which recognise the M/N epitopes on
native, but not on sialidase-treated human erythrocytes were not reactive with human renal endothelium. These
results provide evidence for the occurrence of α and β molecules in renal endothelium and suggest that α in renal
endothelium is incompletely sialylated.
Two Japanese sisters with consanguineous parents have M —N — En(a —) Wr(a — b — ) S — s — U— red
cells and are therefore apparently homozygous for M^k; the third reported family with members of this genotype. The
serum of the proposita (ORCMK) contained anti-En^aTS, anti-En^a FR and possibly anti-Wr^b, whereas the serum of her
M^kM^k sister contained no atypical antibodies. Total absence of sialoglycoproteins α and δ from red cell membranes
of an M^k homozygote was demonstrated by lactoperoxidase-catalysed radioiodination of accessible tyrosine residues
with subsequent SDS polyacrylamide gel electrophoresis and autoradiography, and by use of a monoclonal antibody
directed at the cytoplasmic portion of α-sialoglycoprotein.
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