Some 30 lectins in combination with glycosidase digestion and
immunohistochemistry with 5 antibodies directed against antigens of the
ABO and Lewis blood group systems were used to analyse the distribution
and synthesis of glycoconjugates in the epithelium of the large airways
in man. Both mucous gland cells and goblet cells were labelled by 12 of
30 lectins and by the antibodies, dependent on the ABO, Lewis, and
secretor status. The corresponding binding patterns of the serous gland
cells differed markedly from those of goblet and mucous gland cells and
in general were not dependent on the ABO, Lewis, and secretor status.
After digestion with neuraminidase and fucosidase, binding of soy bean
agglutinin and peanut agglutinin to goblet and mucous gland cells was
increased. Binding of peanut agglutinin to serous gland cells was
stronger only after the digestion with neuraminidase. Digestion with
O-glycosidase after the use of neuraminidase or fucosidase resulted in
a decrease of peanut agglutinin binding to goblet and mucous gland
cells. The present results show that the secretory products of goblet
and mucous gland cells on the one hand and those of serous cells on the
other differ considerably with respect to their terminal glycosylation.
The glycosyltransferases coded by genes of the ABO and Lewis blood
group and secretor systems are active only in goblet and mucous gland
cells, resulting in the presence of the corresponding antigens.
Precursor substances of blood group antigens types 1, 2, and 3 are
found only in these cell types. In serous gland cells, blood group
systems do not influence the glycosylation of glycoproteins. The
results of the digestion with O-glycosidase indicates the presence of
O-glycosylation in mucous gland and goblet cells, but not in serous
gland cells.