Structural features of carbohydrate chains in human salivary mucins.

  title={Structural features of carbohydrate chains in human salivary mucins.},
  author={B. L. Slomiany and Varahabhotla L.N. Murty and Amalia Slomiany},
  journal={The International journal of biochemistry},
  volume={25 2},
Salivary MUC7 is a major carrier of blood group I type O-linked oligosaccharides serving as the scaffold for sialyl Lewis x.
The data show that MUC7 provides a multivalent scaffold for sialylation, meeting the requirement for high-avidity binding via its glycosylation and mediator of the interaction between immune cells such as salivary neutrophils and oral bacteria.
Structure, biosynthesis, and function of salivary mucins
The glandular secretions of the oral cavity lining the underlying buccal mucosa are highly specialized fluids which provide lubrication, prevent mechanical damage, protect efficiently against viral
Glycomic mapping of O- and N-linked glycans from major rat sublingual mucin
The masking effect of terminal sialylation on the tight binding of rat sublingual mucin to Galβ1→4GlcNAc specific lectins and three oligomannose specific Lectins were clearly demonstrated in this study.
Structure and biosynthesis of human salivary mucins.
Human salivary glands secrete two types of mucins: oligomeric mucin (MG1) with molecular mass above 1 MDa and monomeric mucin (MG2) with molecular mass of 200-250 kDa. Monomers of MG1 and MG2 contain
Mammalian reproductive tract mucins.
Proven functions for the different mucins are largely unknown, although potential functions are addressed in this review and genetic and protein sequence information and expression profiles are summarized.
Comparative structural analysis of the glycosylation of salivary and buccal cell proteins: innate protection against infection by Candida albicans.
Saliva constantly bathes the buccal cells of the epithelial surface of the mouth and it is postulate that the sugars on the salivary glycoproteins provide an innate host immune mechanism against infection by competitively inhibiting pathogen binding to the cell membranes.


In vitro sulfation of sublingual salivary gland mucin: structures of 35S-labeled oligosaccharides.
The enzyme which catalyzes the transfer of sulfate ester group from 3'-phosphoadenosine-5'-phosphosulfate to salivary mucus glycoprotein was located in the detergent extract of the Golgi-rich
Oligosaccharide Structures of the Low-molecular-weight Salivary Mucin from a Normal Individual and one with Cystic Fibrosis
Following alkaline/borotritide cleavage, neutral and sialic acid-containing chains were purified by a combination of gel filtration, paper chromatography, and high-voltage paper electrophoresis.
Effect of ethanol on the in vitro sulfation of salivary mucin.
In vitro sulfation of mucus glycoprotein by sulfotransferase from rat submandibular salivary gland and the effect of ethanol on this enzyme activity was investigated, revealing that the enzyme which catalyzes the transfer of sulfate ester group from 3-phosphoadenosine-5'-phosphosulfate to submandIBular gland mucus Glycoprotein is associated with Golgi-rich membrane fraction.