Abstract
Mucins, the major components of salivary mucus, are large glycoproteins abundantly modified with O-glycans. Mucins present on the surface of oral tissues contribute greatly to the maintenance of oral hygiene by selectively adhering to the surfaces of microbes via mucin O-glycans. However, due to the complex physicochemical properties of mucins, there have been relatively few detailed analyses of the mechanisms controlling the expression of mucin genes and the glycosyltransferase genes involved in glycosylation. Analysis performed using supported molecular matrix electrophoresis, a methodology developed for mucin analysis, and knockout mice without the polycomb group protein Bmi-1 revealed that Bmi-1 regulates mucin levels in the submandibular gland by suppressing the expression of the mucin Smgc gene, and that Bmi-1 also regulates mucin O-glycosylation via suppression of the glycosyltransferase Gcnt3 gene in the submandibular gland.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Chromatin Immunoprecipitation
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Electrophoresis
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Gene Expression Regulation / genetics*
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Glycosylation
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Immunohistochemistry
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Male
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Mass Spectrometry
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Mice
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Mice, Inbred C57BL
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Mice, Knockout
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Mucins / analysis
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Mucins / genetics
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Mucins / metabolism*
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N-Acetylglucosaminyltransferases / genetics
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N-Acetylglucosaminyltransferases / metabolism
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Polycomb Repressive Complex 1 / genetics
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Polycomb Repressive Complex 1 / metabolism*
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Polysaccharides / analysis*
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Polysaccharides / chemistry
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Proto-Oncogene Proteins / genetics
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Proto-Oncogene Proteins / metabolism*
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Real-Time Polymerase Chain Reaction
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Submandibular Gland / enzymology
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Submandibular Gland / metabolism*
Substances
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Bmi1 protein, mouse
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Mucins
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Polysaccharides
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Proto-Oncogene Proteins
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Smgc protein, mouse
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Polycomb Repressive Complex 1
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N-Acetylglucosaminyltransferases
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beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3