Journal of Dental Research, Vol 66, 442-450, Copyright © 1987 by International & American Associations for Dental Research Online Journals
Genetic and sex-related differences in the structure of submandibular glycoconjugates
B. A. Schulte
Structures of oligosaccharides in submandibular glycoproteins were
evaluated in situ. Sections of fixed paraffin-embedded glands from rats,
mice, hamsters, sheep, and man were stained with a battery of lectins
conjugated to horseradish peroxidase in conjunction with other methods,
such as digestion with sialidase with or without prior saponification
and/or periodate oxidation. Secretory glycoproteins showed a characteristic
lectin binding pattern for each genus. Sialoglycoconjugates were detected
in acinar cell secretions in all genera except the rat but differed with
respect to the linkage of sialic acid to penultimate beta-galactose or
alpha-N-acetylgalactosamine. Species and strains of mice showed minor
differences in the structure of secretory glycoproteins. Sexes differed
similarly in some but not other mouse species. Individual differences were
seen in human glands, where oligosaccharide structure varied in relation to
ABO blood group. In some species, heterogeneity in glycoprotein structure
was observed among morphologically similar cells within a gland.
Differences in the structure of salivary secretions between genera and
between humans of different ABO blood type and secretor status substantiate
biochemical and histochemical findings. The results showing species, sex,
and individual differences in mice and heterogeneity in acinar cells in
several species suggest a greater degree of genetic and perhaps hormonal
influence on the synthesis of salivary glycoproteins than has previously
been recognized.
