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Volumn 49, Issue 5, 2004, Pages 337-343

Salivary micelles: Identification of complexes containing MG2, sIgA, lactoferrin, amylase, glycosylated proline-rich protein and lysozyme

Author keywords

Complexing; Globular Structures; Protein protein interactions; Saliva; Selectivity

Indexed keywords

AMINO ACID; AMYLASE; LACTOFERRIN; LYSOZYME; MAGNESIUM; PEPTIDE; PROLINE RICH PROTEIN; PROLINE-RICH POLYPEPTIDE; SALIVA PROTEIN; SECRETORY IMMUNOGLOBULIN;

EID: 1842539547     PISSN: 00039969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.archoralbio.2003.11.007     Document Type: Article
Times cited : (77)

References (27)
  • 1
    • 0031089153 scopus 로고    scopus 로고
    • Human salivary mucin MG1 selectively forms heterotypic complexes with amylase, proline-rich proteins, statherin, and histatins
    • Iontcheva I., Oppenheim F.G., Troxler R.F. Human salivary mucin MG1 selectively forms heterotypic complexes with amylase, proline-rich proteins, statherin, and histatins. J. Dent. Res. 76:1997;734-743.
    • (1997) J. Dent. Res. , vol.76 , pp. 734-743
    • Iontcheva, I.1    Oppenheim, F.G.2    Troxler, R.F.3
  • 2
    • 0034438593 scopus 로고    scopus 로고
    • Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system
    • Iontcheva I., Oppenheim F.G., Offner G.D., Troxler R.F. Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. J. Dent. Res. 79:2000;732-739.
    • (2000) J. Dent. Res. , vol.79 , pp. 732-739
    • Iontcheva, I.1    Oppenheim, F.G.2    Offner, G.D.3    Troxler, R.F.4
  • 3
    • 0026094266 scopus 로고
    • Interaction of a salivary mucin-secretory immunoglobulin a complex with mucosal pathogens
    • Biesbrock A.R., Reddy M.S., Levine M.J. Interaction of a salivary mucin-secretory immunoglobulin A complex with mucosal pathogens. Infect Immun. 59:1991;3492-3497.
    • (1991) Infect Immun. , vol.59 , pp. 3492-3497
    • Biesbrock, A.R.1    Reddy, M.S.2    Levine, M.J.3
  • 5
    • 0019483790 scopus 로고
    • Association between bacterial agglutinins and immunoglobulin a in human saliva
    • Olsson J., Bratthall D., Carlen A. Association between bacterial agglutinins and immunoglobulin A in human saliva. Acta Odontol Scand. 39:1981;61-66.
    • (1981) Acta Odontol Scand , vol.39 , pp. 61-66
    • Olsson, J.1    Bratthall, D.2    Carlen, A.3
  • 6
    • 0020025351 scopus 로고
    • Interaction of specific and innate factors of immunity: IgA enhances the antimicrobial effect of the lactoperoxidase system against Streptococcus mutans
    • Tenovuo J., Moldoveanu Z., Mestecky J., Pruitt K.M., Rahemtulla B.M. Interaction of specific and innate factors of immunity: IgA enhances the antimicrobial effect of the lactoperoxidase system against Streptococcus mutans. J. Immunol. 128:1982;726-731.
    • (1982) J. Immunol. , vol.128 , pp. 726-731
    • Tenovuo, J.1    Moldoveanu, Z.2    Mestecky, J.3    Pruitt, K.M.4    Rahemtulla, B.M.5
  • 7
    • 0023130986 scopus 로고
    • Differentiation and interaction of secretory immunoglobulin a and a calcium-dependent parotid agglutinin for several bacterial strains
    • Rundegren J., Arnold R.R. Differentiation and interaction of secretory immunoglobulin A and a calcium-dependent parotid agglutinin for several bacterial strains. Infect Immun. 55:1987;288-292.
    • (1987) Infect Immun. , vol.55 , pp. 288-292
    • Rundegren, J.1    Arnold, R.R.2
  • 11
    • 0031264558 scopus 로고    scopus 로고
    • Zeta potentials of human enamel and hydroxyapatite as measured by the Coulter DELSA 440
    • Young A., Smistad G., Karlsen J., Rolla G., Rykke M. Zeta potentials of human enamel and hydroxyapatite as measured by the Coulter DELSA 440. Adv. Dent. Res. 11:1997;560-565.
    • (1997) Adv. Dent. Res. , vol.11 , pp. 560-565
    • Young, A.1    Smistad, G.2    Karlsen, J.3    Rolla, G.4    Rykke, M.5
  • 12
    • 0031242372 scopus 로고    scopus 로고
    • Fractionation of salivary micelle-like structures by gel chromatography
    • Rykke M., Young A., Devold T., Smistad G., Rolla G. Fractionation of salivary micelle-like structures by gel chromatography. Eur J. Oral Sci. 105:1997;495-501.
    • (1997) Eur J. Oral Sci. , vol.105 , pp. 495-501
    • Rykke, M.1    Young, A.2    Devold, T.3    Smistad, G.4    Rolla, G.5
  • 13
    • 0033109252 scopus 로고    scopus 로고
    • Quantitative and qualitative analyses of human salivary micelle-like globules
    • Young A., Rykke M., Rolla G. Quantitative and qualitative analyses of human salivary micelle-like globules. Acta Odontol Scand. 57:1999;105-110.
    • (1999) Acta Odontol Scand , vol.57 , pp. 105-110
    • Young, A.1    Rykke, M.2    Rolla, G.3
  • 14
    • 0033560616 scopus 로고    scopus 로고
    • Isolation of human salivary mucin MG2 by a novel method and characterization of its interactions with oral bacteria
    • Liu B., Rayment S., Oppenheim F.G., Troxler R.F. Isolation of human salivary mucin MG2 by a novel method and characterization of its interactions with oral bacteria. Arch Biochem. Biophys. 364:1999;286-293.
    • (1999) Arch Biochem. Biophys. , vol.364 , pp. 286-293
    • Liu, B.1    Rayment, S.2    Oppenheim, F.G.3    Troxler, R.F.4
  • 15
    • 0028801832 scopus 로고
    • Role of hydrophobic and hydrophilic forces in peptide-protein interaction: New advances
    • Cserhati T., Szogyi M. Role of hydrophobic and hydrophilic forces in peptide-protein interaction: new advances. Peptides. 16:1995;165-173.
    • (1995) Peptides , vol.16 , pp. 165-173
    • Cserhati, T.1    Szogyi, M.2
  • 16
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • Wilson I.A., Stanfield R.L. Antibody-antigen interactions: new structures and new conformational changes. Curr. Opin. Struct. Biol. 4:1994;857-867.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2
  • 17
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S., Thornton J.M. Principles of protein-protein interactions. Proc. Natl. Acad Sci. 93:1996;13-20.
    • (1996) Proc. Natl. Acad Sci. , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 19
    • 0028547354 scopus 로고
    • Evidence for presence of micelle-like protein globules in human saliva
    • Rolla G., Rykke M. Evidence for presence of micelle-like protein globules in human saliva. Colloids Surf. B Biointerfaces. 3:1994;177-182.
    • (1994) Colloids Surf. B Biointerfaces , vol.3 , pp. 177-182
    • Rolla, G.1    Rykke, M.2
  • 20
    • 0001869348 scopus 로고
    • Nonimmunoglobulin defense factors in human saliva
    • Tenovuo JO, editor. Boca Raton: CRC Press Inc.
    • Tenovuo JO. Nonimmunoglobulin defense factors in human saliva. In: Tenovuo JO, editor. Human saliva: clinical chemistry and microbiology, vol. II. Boca Raton: CRC Press Inc.; 1989. p. 55-91.
    • (1989) Human Saliva: Clinical Chemistry and Microbiology , vol.2 , pp. 55-91
    • Tenovuo, J.O.1
  • 21
    • 0036120646 scopus 로고    scopus 로고
    • Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia efficacy and safety
    • Tenovuo J. Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia efficacy and safety. Oral Dis. 8:2002;23-29.
    • (2002) Oral Dis. , vol.8 , pp. 23-29
    • Tenovuo, J.1
  • 22
    • 0034758092 scopus 로고    scopus 로고
    • Human lactoferrin: A novel therapeutic with broad spectrum potential
    • Weinberg E.D. Human lactoferrin: a novel therapeutic with broad spectrum potential. J. Pharm. Pharmacol. 53:2001;1303-1310.
    • (2001) J. Pharm. Pharmacol. , vol.53 , pp. 1303-1310
    • Weinberg, E.D.1
  • 23
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi K., Tomita M., Giehl T.J., Ellison R.T. 3rd Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect Immun. 61:1993;719-728.
    • (1993) Infect Immun. , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison III, R.T.4
  • 24
    • 0031888232 scopus 로고    scopus 로고
    • Oral microbial ecology and the role of salivary immunoglobulin a
    • Marcotte H., Lavoie M.C. Oral microbial ecology and the role of salivary immunoglobulin A. Microbiol. Mol. Biol. Rev. 62:1998;71-109.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 71-109
    • Marcotte, H.1    Lavoie, M.C.2
  • 25
    • 0034141817 scopus 로고    scopus 로고
    • The recombinant N-terminal region of human salivary mucin MG2 (MUC7) contains a binding domain for oral Streptococci and exhibits candidacidal activity
    • Liu B., Rayment S.A., Gyurko C F.G., Offner G.D., Troxler R.F. The recombinant N-terminal region of human salivary mucin MG2 (MUC7) contains a binding domain for oral Streptococci and exhibits candidacidal activity. Biochem. J. 345:2000;557-564.
    • (2000) Biochem. J. , vol.345 , pp. 557-564
    • Liu, B.1    Rayment, S.A.2    Gyurko, C.F.G.3    Offner, G.D.4    Troxler, R.F.5
  • 27
    • 0032878759 scopus 로고    scopus 로고
    • Inhibition of growth and secreted aspartyl proteinase production in Candida albicans by lysozyme
    • Wu T., Samaranayake L.P., Leung W.K., Sullivan P.A. Inhibition of growth and secreted aspartyl proteinase production in Candida albicans by lysozyme. J. Med. Microbiol. 48:1999;721-730.
    • (1999) J. Med. Microbiol. , vol.48 , pp. 721-730
    • Wu, T.1    Samaranayake, L.P.2    Leung, W.K.3    Sullivan, P.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.