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Structural Aspects of Salivary Glycoproteins
M.J. Levine
Department of Oral Biology, 109 Foster Hall, Schools of Dental Medicine and Medicine, State University of New York at Buffalo, Buffalo, New York 14214
M.S. Reddy
Department of Oral Biology, 109 Foster Hall, Schools of Dental Medicine and Medicine, State University of New York at Buffalo, Buffalo, New York 14214
L.A. Tabak
Department of Endodontics, 109 Foster Hall, Schools of Dental Medicine and Medicine, State University of New York at Buffalo, Buffalo, New York 14214
R.E. Loomis
Department of Oral Biology, 109 Foster Hall, Schools of Dental Medicine and Medicine, State University of New York at Buffalo, Buffalo, New York 14214
E.J. Bergey
Department of Oral Biology, 109 Foster Hall, Schools of Dental Medicine and Medicine, State University of New York at Buffalo, Buffalo, New York 14214
P.C. Jones
Department of Oral Biology, 109 Foster Hall, Schools of Dental Medicine and Medicine, State University of New York at Buffalo, Buffalo, New York 14214
R.E. Cohen
Department of Oral Biology, 109 Foster Hall, Schools of Dental Medicine and Medicine, State University of New York at Buffalo, Buffalo, New York 14214
M.W. Stinson
Department of Microbiology, 109 Foster Hall, Schools of Dental Medicine and Medicine, State University of New York at Buffalo, Buffalo, New York 14214
I. Al-Hashimi
Department of Oral Biology, 109 Foster Hall, Schools of Dental Medicine and Medicine, State University of New York at Buffalo, Buffalo, New York 14214
The protective functions of saliva are attributed, in part, to its serous and mucous glycoproteins. We have studied, as representative molecules, the proline-rich glycoprotein (PRG) from human parotid saliva and the high (MGI ) and low (MG2) molecular weight mucins from submandibular-sublingual saliva. PRG (38.9 kDa) contains 40% carbohydrate consisting of 6 triantennary N-linked units and a single peptide chain of 231 amino acids, 75% of which = PRO+GLY+GLN. PRG's secondary structure is comprised of 70% random coil (naked regions) and 30% β-turns (glycosylated domains). MGI (>103 kDa) contains 15% protein (several disulfide linked subunits), 78% carbohydrate (290 units of 4-16 residues), 7% sulfate, and small amounts of covalently linked fatty acids. MG2 (200-250 kDa) contains 30% protein (single peptide chain), 68% carbohydrate (170 units of 2-7 residues), and 2% sulfate. The major carbohydrate units of MG2 are: NeuAc 2, 3Galβ1, 3GalNAc, Galβ1, 3GalNAc, and Fuc1, 2Galβ1, 3GalNAc. MG1 contains hydrophobic domains, as evidenced by its ability to bind fluorescent hydrophobic probes; MG2 does not. Collectively, the biochemical and biophysical comparisons between MGI and MG2 indicate that these two mucins are structurally different. Several functional properties of MG1, MG2, and PRG have been examined, including their presence in two-hour in vivo enamel pellicle, binding to synthetic hydroxyapatite, lubricating properties, and interactions with oral streptococci. The data presented suggest that these glycoproteins may have multiple functions which are predicated, in part, on their carbohydrate units. The potential significance of the structure-function relationships of these glycoproteins to the oral ecology is discussed.
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DOI: 10.1177/00220345870660020901
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