Salivary mucin MG1 is comprised almost entirely of different glycosylated forms of the MUC5B gene product

doi:10.1093/glycob/9.3.293

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ORIGINAL ARTICLES

Salivary mucin MG1 is comprised almost entirely of different glycosylated forms of the MUC5B gene product

DJ Thornton, N Khan, R Mehrotra, M Howard, E Veerman, NH Packer and JK Sheehan
Wellcome Trust Centre for Cell-Matrix Research, University of Manchester, School of Biological Sciences, 2.205, Stopford Building, Manchester M13 9PT, UK.

The MG1 population of mucins was isolated from human whole salivas by gel chromatography followed by isopycnic density gradient centrifugation. The reduced and alkylated MG1 mucins, separated by anion exchange chromatography, were of similar size (radius of gyration 55-64 nm) and molecular weight (2.5-2.9 x 10(6) Da). Two differently- charged populations of MG1 subunits were observed which showed different reactivity with monoclonal antibodies to glycan epitopes. Monosaccharide and amino acid compositional analyses indicated that the MG1 subunits had similar glycan structures on the same polypeptide. An antiserum recognizing the MUC5B mucin was reactive across the entire distribution, whereas antisera raised against the MUC2 and MUC5AC mucins showed no reactivity. Western blots of agarose gel electrophoresis of fractions across the anion exchange distribution indicated that the polypeptide underlying the mucins was the product of the MUC5B gene. Amino acid analysis and peptide mapping performed on the fragments produced by trypsin digestion of the two MG1 populations yielded data similar to that obtained for MUC5B mucin subunits prepared from respiratory mucus (Thornton et al., 1997) and confirmed that the MUC5B gene product was the predominant mucin polypeptide present. Isolation of the MG1 mucins from the secretions of the individual salivary glands (palatal, sublingual, and submandibular) indicate that the palatal gland is the source of the highly charged population of the MUC5B mucin.
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				K. Rousseau, S. Kirkham, S. McKane, R. Newton, P. Clegg, and D. J. Thornton Muc5b and Muc5ac are the major oligomeric mucins in equine airway mucus Am J Physiol Lung Cell Mol Physiol, June 1, 2007; 292(6): L1396 - L1404. [Abstract] [Full Text] [PDF]

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				K. A. Thomsson, A. Prakobphol, H. Leffler, M. S. Reddy, M. J. Levine, S. J. Fisher, and G. C. Hansson The salivary mucin MG1 (MUC5B) carries a repertoire of unique oligosaccharides that is large and diverse Glycobiology, January 1, 2002; 12(1): 1 - 14. [Abstract] [Full Text] [PDF]

				D. J. Thornton, J. R. Davies, S. Kirkham, A. Gautrey, N. Khan, P. S. Richardson, and J. K. Sheehan Identification of a nonmucin glycoprotein (gp-340) from a purified respiratory mucin preparation: evidence for an association involving the MUC5B mucin Glycobiology, November 1, 2001; 11(11): 969 - 977. [Abstract] [Full Text] [PDF]

				S.A. Payment, B. Liu, G.D. Offner, F.G. Oppenheim, and R.F. Troxler Immunoquantification of Human Salivary Mucins MG1 and MG2 in Stimulated whole Saliva: Factors Influencing Mucin levels Journal of Dental Research, October 1, 2000; 79(10): 1765 - 1772. [Abstract] [PDF]