Structure and biosynthesis of human salivary mucins

• Autorzy: Zalewska A. , Zwierz K. , Zolkowski K. , Gindzienski A.
• Języki publikacji: EN

Abstrakty

EN

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 havily O-glycosylated tandem repeats located at the central domain of the molecules. MG1 monomers are linked by disulfide bonds located at sparsely glycosylated N- and C-end. MG1 are synthesized by mucous cells and MG2 by the serous cells of human salivary glands.

Słowa kluczowe

EN

glycoprotein; structure; man; mucin; salivary mucin; biosynthesis; salivary gland; saliva

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2000
• Tom: 47
• Numer: 4
• Opis fizyczny: p.1067-1079,fig.,ref.

Twórcy

autor

Zalewska A.

• Medical Academy, A.Mickiewicz 2a, 15-222 Bialystok, Poland

autor

Zwierz K.

autor

Zolkowski K.

autor

Gindzienski A.

Bibliografia

• 1. Nieuw Amerongen, A.V., Bolscher, J.G.M. & Veerman, E.C.I. (1995) Salivary mucins: Pro­tective functions in relation to their diversity. Glycobiology 5, 733-740.
• 7. Wu, A.M., Csako, G. & Herp, A. (1994) Struc­ture, biosynthesis, and function of salivary mucins. Mol. Cell. Biochem. 137, 39-55.
• 8. Thornton, D.J., Khan, N., Mehrotra, R., Howard, M., Veerman, E., Packer, N.H. & Sheehan, J.K. (1999) Salivary mucin MG1 is comprised almost entirely of different glyco- sylated forms of MUC5B gene product. Glycobiology 9, 293-302.
• 9. Nielsen, P.A., Mandel, U., Therkildsen, M.H. & Clausen, H. (1996) Differential expression of human high-molecular-weight salivary mucin (MG1) and low-molecular-weight sali­vary mucin (MG2). J. Dent. Res. 75, 1820-1826.
• 10. Troxler, R.F., Iontcheva, I., Oppenheim, F.G., Nunes, D.P. & Offner, G.D. (1997) Molecular characterization of a major molecular weight mucin from human sublingual gland. Glyco- biology 7, 965-973.
• 11. Milne, R.W. & Dawes, C. (1973) The relative contributions of different salivary glands to the blood group activity of whole saliva in hu­mans. Vox Sang. 25, 298-307.
• 12. Edgerton, M. & Levine, M.J. (1992) Character­ization of acquired denture pellicle from healthy and stomatitis patients. J. Prosthet. Dent. 68, 683-691.
• 13. Desseyn, J.-L., Guyonnet-Duperat, V., Por- chet, N., Aubert, J.-P. & Laine, A. (1997) Hu­man mucin gene MUC5B, the 10.7 kb large central exon encodes various alternate sub­domains resulting in a super-repeat. Struc­tural evidence for a 11p.15.5 gene family. J. Biol. Chem. 272, 3168-3178.
• 14. Van den Steen, Rudd, P.M., Dwek, R. & Opdenakker, G. (1998) Concepts and princi­ples of O-linked glycosylation. Crit. Rev. Biochem. Mol. Biol. 33, 151-208.
• 15. Wickstrom, C., Davies, J.R., Eriksen, G.V., Veermans, E.C. & Carlsted, I. (1998) MUC5B is a major gel-forming, oligomeric mucin from human salivary gland, respiratory tract and endocervix: Identification of glycoforms and C-terminal cleavage. Biochem. J. 334, 685­693.
• 16. Loomis, R.E., Prakobphol, A., Levine, M.J., Reddy, M.S. & Jones, P.C. (1987) Biochemical and biophysical comparison of two mucins from human submandibular-sublingual saliva. Arch. Biochem. Biophys. 258, 452-464.
• 17. Desseyn, J.-L., Aubert, J.-P., VanSeuningen, I., Porchet, N. & Laine, A. (1997) Genomic or­ganization of the 3' region of the human mucin gene MUC5B. J. Biol. Chem. 272, 16873-16883.
• 18. Klein, A., Carnoy, Ch., Wieruszewski, J.-M., Strecker, G., Strang, A.-M., van Halbeck, H., Roussel, Ph. & Lamblin, G. (1992) The broad diversity of neutral and sialylated oligosaccha- rides derived from human salivary mucin. Bio­chemistry 31, 6152-6165.
• 19. Mancuso, D.J., Tuley, E.A., Westfield, L.A., Worral, N.K., Shelton-Inloes, B., Sorace, J.M., Alevy, Y.G. & Sadler, J.E. (1989) Structure of the gene for human von Willebrand factor. J. Biol Chem. 264, 19514-19527.
• 20. Hardy, D.M. & Garbers, D.L. (1995) A sperm membrane protein that binds in a spe­cies-specific manner to the egg extracellular matrix is homologous to von Willebrand fac­tor. J. Biol. Chem. 270, 26025-26028.
• 21. Sheehan, J.K., Boot-Handford, R.P., Chantler, E., Carlstedt, I. & Thornton, D.J. (1991) Evi­dence for shared epitopes within the "naked" domains of human mucus glycoproteins. A study performed using polyclonal antibodies and electron microscopy. Biochem. J. 274, 293-296.
• 22. Antonyraj, K.J., Karunakaran, T. & Raj, P.A. (1998) Bactericidal activity and poly-L-proline II conformation of the tandem repeat se­quence of human salivary glycoprotein (MG2). Arch. Biochem. Biophys. 356, 197-206.
• 23. Bobek, L.A., Tsai, H., Biesbrock, A.R. & Le­vine, M.J. (1993) Molecular cloning, sequence, and specificity of expression of the gene en­coding the low molecular weight human sali­vary mucin (MUC 7). J. Biol. Chem. 268, 20563-20569.
• 24. Mehrotra, R., Thornton, D.J. & Sheehan, J.K. (1998) Isolation and physical characterization of MUC 7 (MG2) mucin from saliva: Evidence for self association. Biochem. J. 334, 415­422.
• 25. Prakobphol, A., Thomsson, K.A., Hansson, G., Rosen, S.D., Singer, M.S., Phillips, N.J., Med- dihradszky, K.F., Burlingame, A.L., Leffler, H. & Fisher, S. (1998) Human low-molecular- weight salivary mucin expresses the sialyl Lewisx determinant and has L-selectin ligand activity. Biochemistry 37, 4916-4927.
• 26. Levine, M.J., Reddy, M.S., Tabak, L.A., Loomis, R.E., Bergey, E.J., Jones, P.C., Co­hen, R.E., Stinson, M.W. & Al-Hashimi, I. (1987) Structural aspects of saliva glyco­proteins. J. Dent. Res. 66, 436-441.
• 27. Slomiany, B.L., Murthy, V.L.N. & Slomiany, A. (1993) Structural features of carbohydrate chains in human salivary mucins. Int. J. Biochem. 25, 259-265.
• 28. Slomiany, B.L., Piotrowski, J., Czajkowski, A. & Slomiany, A. (1993) Control of mucin molec­ular forms expression by salivary protease: Difference with caries. Int. J. Biochem. 25, 681-687.
• 29. Prakobphol, A., Tangemann, K., Rosen, S.D., Hoover, Ch.I., Leffler, H. & Fisher, S.J. (1999) Separate oligosaccharide determinants medi­ate interactions of the low-molecular-weight salivary mucins with neutrophils and bacteria. Biochemistry 38, 6817-6825.
• 30. Li, F., Wilkins, P.P., Crawley, S., Weinstein, J., Cummings, R.D. & McEver, R.P. (1996) Post-translational modifications of recombi­nant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin. J. Biol. Chem. 271, 3255-3264.
• 31. Nehrke, K. & Tabak, L.A. (1997) Biosynthesis of a low-molecular-mass rat submandibular gland mucin glycoprotein in COS 7 cells. Biochem. J. 323, 497-502.
• 32. McCool, D.J., Okada, Y., Forstner, J.F. & Forstner, G.G. (1999) Roles of calreticulin and calnexin during mucin synthesis in LS180 and HT29/A1 human colonic adenocarcinoma cells. Biochem. J. 341, 593-600.
• 33. Kapitonov, D. & Yu, R.K. (1999) Conserved do­mains of glycosyltransferases. Glycobiology 9, 961-978.
• 34. Porowska, H., Paszkiewicz-Gadek, A. & Gin­dzieński, A. (1999) Activity of partially puri­fied UDP-N-acetyl-a-D-galactosamine: Polypep­tide N-acetylgalactosaminyltransferase with different peptide acceptors. Acta Biochim. Polon. 46, 365-360.
• 35. Bennet, E.P., Hassan, H., Mandel, U., Hollin­gsworth, M.A., Akisawa, N., Ikematsu, Y., Merkx, G., vanKellel, A.G., Olofsson, S. & Clausen, H. (1999) Cloning and characteriza­tion of a close homologue of human UDP-N- acetyl-y3-D-galactosamine: Polypeptide N-ace- tylgalactosaminyltransferase-T3, designated GalNAc-T6. J. Biol. Chem. 274, 25362-25370.
• 36. Hagen, K.G.T., Hagen, F.K., Balys, M.M., Beres, T.M., van Wuyckhuyse, B. & Tabak, L.A. (1998) Cloning and expression of a novel, tissue specifically expressed member of the UDP-GalNAc : polypeptide N-acetylgalactosa- minyltransferase family. J. Biol. Chem. 273, 27749-27754.
• 37. Clausen, H. & Bennet, E.P. (1996) A family of UDP-GalNAc : polypeptide N-acetylgalactosa- minyl-transferases control the initiation of mucin-type O-linked glycosylation. Glyco- biology 6, 635-646.
• 38. Paulson, J.C. & Colley, K.J. (1989) Glyco- syltransferases. Structure, localization, and control of cell type-specific glycosylation. J. Biol. Chem. 264, 17615-17618.
• 39. Rottger, S., White, R., Wandall, H.H., Bennet, E.A., Stark, A., Olivio, J., Whitehouse, C., Berger, E.G., Clausen, H. & Nilson, T. (1998) Differential localization of three human GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation occurs through the Golgi apparatus. J. Cell. Sci. 111, 45-60.
• 40. Bennet, E.P., Weghuis, D.D., Merkx, G., van Kessel, A.G., Eiberg, H. & Clausen, H. (1998) Genomic organization and chromosomal local­ization of three members of the UDP-N-acetyl- galactosamine: polypeptide ^-acetylgalactosa­mine transferase family. Glycobiology 8, 547-555.
• 41. Wandall, H.H., Hassan, H., Mirgorodskaya, E., Kristensen, A.K., Roepstorff, P., Bennet, E.P., Nielsen, P.A., Hollingsworth, M.A., Burchell, J., Taylor-Papadamitriou, J. & Clausen, H. (1997) Substrate specificities of three members of the human UDP-N-ace- tyl-a-D-galactosamine:polypeptide ^-acetylga- lactosaminetransferase family. J. Biol. Chem. 272, 23503-23514.
• 42. Mandel, U., Hassan, H., Therkildsen, M.H., Rygaard, J., Jakobsen, M.H., Juhl, B.R., Dabelsteen, E. & Clausen, H. (1999) Expres­sion of polypeptide GalNAc-transferases in stratified epithelia and squamous cell carcino­mas: Immunohistological evaluation using monoclonal antibodies to three members of the GalNAc-transferase family. Glycobiology 9, 43-52.
• 43. Field, M.C. & Wainwright, L.J. (1995) Molecu­lar cloning of eucaryotic glycoprotein and glycolipid glycosyltransferases: A survey. Glycobiology 5, 463-472.
• 44. Beum, P.V., Singh, J., Burdick, M., Hollon- gsworth, M.A. & Cheng, P.W. (1999) Expres­sion of core 2 y31,6-^-acetyl-glucosaminyltrans- ferase in a human pancreatic cancer cell line results in altered expression of MUC1 tu­mor-associated epitopes. J. Biol. Chem. 274, 24641-24648.
• 45. Barran, P., Fellinger, W., Warren, Che, E., Dennis, J.W. & Ziltener, H.J. (1997) Modifica­tion of CD 43 and other lymphocyte O-glyco- proteins by core 2 ^-acetylglucosaminyl trans­ferase. Glycobiology 7, 129-136.
• 46. Granovsky, M., Fode, C., Warren, C.E., Camp­bell, R.M., Marth, J.D., Pierce, M., Fregien, N. & Dennis, J.W. (1995) GlcNAc-transferase V and core GlcNAc-transferase expression in the developing mouse embryo. Glycobiology 5, 797-806.
• 47. Li, F., Wilkins, P.P., Crawley, S., Weinstein, J., Cummings, R.D. & McEver, R.P. (1996) Post-translational modifications of recombi­nant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectins. J. Biol. Chem. 271, 3255-3264.
• 48. Kapadia, A., Feizi, T. & Evans, M.J. (1981) Changes in the expression and polarization of blood group I and i antigens in post-im­plantation embryos and teratocarcinomas of mouse associated with cell differentiation. Exp. Cell Res. 131, 185-195.
• 49. Schachter, H. & Brockhausen, I. (1989) The biosynthesis of branched O-glycans. Symp. Soc. Exp. Biol. 43, 1-26.
• 50. Gooi, H.C., Feizi, T., Kapadia, A., Knowles, B.B., Solter, D. & Evans, M.J. (1981) Stage- specific embryonic antigen involves a 1-3 fuco- sylated type 2 blood group chains. Nature 292, 156-158.
• 51. Lloyd, K.O., Kabat, E.A. & Licerio, E. (1968) Immunochemical studied on blood groups XXXVIII. Structures and activities of oligosac- charides produced by alkaline degradation of blood-group Lewisa substance. Proposed struc­ture of the carbohydrate chains of human blood-group A, B, H, Lea, and Leb substance. Biochemistry 7, 2976-2990.
• 52. Abe, K., McKibbin, J.M. & Hakomori, S.I. (1983) The monoclonal antibody directed to difucosylated type 2 chain (Fuca1-2 Galy31-4- [Fuca1-3] GlcNAc), Y determinant. J. Biol. Chem. 258, 11793-11797.4. Paszkiewicz-Gadek, A., Gindzienski, A. & Porowska, H. (1995) The use of preparative polyacrylamide gel electrophoresis and ele- ctroelution for purification of mucus glyco- proteins. Anal. Biochem. 226, 263-267.
• 53 Van Klinken, B.J.-W., Dekker, J., Buller, H.A. & Einerhand, A.W.C. (1995) Mucin gene struc­ture and expression: Protection vs. adhesion.Am. J. Physiol. (Gastroint. Liver Physiol. 32) 269, G613-G-627.
• 54. Minkiewicz-Radziejewska, I., Gindzienski, A. & Zwierz, K. (2000) Disulfide-bound frag­ments of gastric mucin are 100- and 140-kDa proteins. Biochem. Biophys. Res. Commun. 270, 722-727.