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Volumn 17, Issue 6, 2011, Pages 577-583

Influences of hyaluronic acid on the anticandidal activities of lysozyme and the peroxidase system

Author keywords

Anticandidal activity; Hyaluronic acid; Lysozyme; Peroxidase

Indexed keywords

HYALURONIC ACID; LYSOZYME; PEROXIDASE;

EID: 79960700891     PISSN: 1354523X     EISSN: 16010825     Source Type: Journal    
DOI: 10.1111/j.1601-0825.2011.01807.x     Document Type: Article
Times cited : (41)

References (37)
  • 1
    • 34447121482 scopus 로고    scopus 로고
    • Hyaluronan
    • Almond A (2007). Hyaluronan. Cell Mol Life Sci 64: 1591-1596.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 1591-1596
    • Almond, A.1
  • 2
    • 0016817563 scopus 로고
    • Inhibition of leucocytic lysosomal enzymes by glycosaminoglycans in vitro
    • Avila JL, Convit J (1975). Inhibition of leucocytic lysosomal enzymes by glycosaminoglycans in vitro. Biochem J 152: 57-64.
    • (1975) Biochem J , vol.152 , pp. 57-64
    • Avila, J.L.1    Convit, J.2
  • 3
    • 16844372948 scopus 로고
    • The non-Newtonian behaviour of human saliva. AIChE symposium series on biorheology No 181
    • Balmer RT, Hirsch SR (1978). The non-Newtonian behaviour of human saliva. AIChE symposium series on biorheology No 181 74: 125-129.
    • (1978) , vol.74 , pp. 125-129
    • Balmer, R.T.1    Hirsch, S.R.2
  • 4
    • 0017813122 scopus 로고
    • Quantitative study of the interaction of salivary acidic proline-rich proteins with hydroxyapatite
    • Bennick A, Cannon M (1978). Quantitative study of the interaction of salivary acidic proline-rich proteins with hydroxyapatite. Caries Res 12: 159-169.
    • (1978) Caries Res , vol.12 , pp. 159-169
    • Bennick, A.1    Cannon, M.2
  • 5
    • 0032899955 scopus 로고    scopus 로고
    • Functions of hyaluronan in wound repair
    • Chen WY, Abatangelo G (1999). Functions of hyaluronan in wound repair. Wound Repair Regen 7: 79-89.
    • (1999) Wound Repair Regen , vol.7 , pp. 79-89
    • Chen, W.Y.1    Abatangelo, G.2
  • 6
    • 34548414633 scopus 로고    scopus 로고
    • Rheological properties of synovial fluids
    • Fam H, Bryant JT, Kontopoulou M (2007). Rheological properties of synovial fluids. Biorheology 44: 59-74.
    • (2007) Biorheology , vol.44 , pp. 59-74
    • Fam, H.1    Bryant, J.T.2    Kontopoulou, M.3
  • 7
    • 0025615119 scopus 로고
    • Depolymerization of synovial fluid hyaluronic acid (HA) by the complete myeloperoxidase (MPO) system may involve the formation of a HA-MPO ionic complex
    • Green SP, Baker MS, Lowther DA (1990). Depolymerization of synovial fluid hyaluronic acid (HA) by the complete myeloperoxidase (MPO) system may involve the formation of a HA-MPO ionic complex. J Rheumatol 17: 1670-1675.
    • (1990) J Rheumatol , vol.17 , pp. 1670-1675
    • Green, S.P.1    Baker, M.S.2    Lowther, D.A.3
  • 8
    • 66749144093 scopus 로고    scopus 로고
    • Salivary levels of hyaluronic acid in female patients with dry mouth compared with age-matched controls: a pilot study
    • Higuchi Y, Ansai T, Awano S et al (2009). Salivary levels of hyaluronic acid in female patients with dry mouth compared with age-matched controls: a pilot study. Biomed Res 30: 63-68.
    • (2009) Biomed Res , vol.30 , pp. 63-68
    • Higuchi, Y.1    Ansai, T.2    Awano, S.3
  • 10
    • 0023473729 scopus 로고
    • Hyaluronic acid and hyaluronidase activity in gingival exudate from sites of acute ulcerative gingivitis in man
    • Last KS, Embery G (1987). Hyaluronic acid and hyaluronidase activity in gingival exudate from sites of acute ulcerative gingivitis in man. Arch Oral Biol 32: 811-815.
    • (1987) Arch Oral Biol , vol.32 , pp. 811-815
    • Last, K.S.1    Embery, G.2
  • 11
    • 77955552738 scopus 로고    scopus 로고
    • The effects of peroxidase on the enzymatic and candidacidal activities of lysozyme
    • Lee JY, Kim YY, Chang JY, Park MS, Kho HS (2010). The effects of peroxidase on the enzymatic and candidacidal activities of lysozyme. Arch Oral Biol 55: 607-612.
    • (2010) Arch Oral Biol , vol.55 , pp. 607-612
    • Lee, J.Y.1    Kim, Y.Y.2    Chang, J.Y.3    Park, M.S.4    Kho, H.S.5
  • 12
    • 0014559279 scopus 로고
    • Antifungal effects of peroxidase systems
    • Lehrer RI (1969). Antifungal effects of peroxidase systems. J Bacteriol 99: 361-365.
    • (1969) J Bacteriol , vol.99 , pp. 361-365
    • Lehrer, R.I.1
  • 14
    • 0026828233 scopus 로고
    • Lysozyme enhances the inhibitory effects of the peroxidase system on glucose metabolism of Streptococcus mutans
    • Lenander-Lumikari M, Mansson-Rahemtulla B, Rahemtulla F (1992). Lysozyme enhances the inhibitory effects of the peroxidase system on glucose metabolism of Streptococcus mutans. J Dent Res 71: 484-490.
    • (1992) J Dent Res , vol.71 , pp. 484-490
    • Lenander-Lumikari, M.1    Mansson-Rahemtulla, B.2    Rahemtulla, F.3
  • 15
    • 0027313501 scopus 로고
    • Development of artificial salivas
    • Levine MJ (1993). Development of artificial salivas. Crit Rev Oral Biol Med 4: 279-286.
    • (1993) Crit Rev Oral Biol Med , vol.4 , pp. 279-286
    • Levine, M.J.1
  • 17
    • 0019953274 scopus 로고
    • Fungitoxicity of muramidase. Ultrastructural damage to Candida albicans
    • Marquis G, Montplaisir S, Garzon S, Strykowski H, Auger P (1982). Fungitoxicity of muramidase. Ultrastructural damage to Candida albicans. Lab Invest 46: 627-636.
    • (1982) Lab Invest , vol.46 , pp. 627-636
    • Marquis, G.1    Montplaisir, S.2    Garzon, S.3    Strykowski, H.4    Auger, P.5
  • 18
    • 0026100932 scopus 로고
    • Cell walls of normal and lysozyme-damaged blastoconidia of Candida albicans: localization of surface factor 4 antigen and vicinal-glycol staining
    • Marquis G, Garzon S, Strykowski H, Auger P (1991). Cell walls of normal and lysozyme-damaged blastoconidia of Candida albicans: localization of surface factor 4 antigen and vicinal-glycol staining. Infect Immun 59: 1312-1318.
    • (1991) Infect Immun , vol.59 , pp. 1312-1318
    • Marquis, G.1    Garzon, S.2    Strykowski, H.3    Auger, P.4
  • 19
    • 0031543494 scopus 로고    scopus 로고
    • Dependence of salt concentration on glycosaminoglycan - lysozyme interactions in cartilage
    • Moss JM, Van Damme MP, Murphy WH, Preston BN (1997). Dependence of salt concentration on glycosaminoglycan - lysozyme interactions in cartilage. Arch Biochem Biophys 348: 49-55.
    • (1997) Arch Biochem Biophys , vol.348 , pp. 49-55
    • Moss, J.M.1    Van Damme, M.P.2    Murphy, W.H.3    Preston, B.N.4
  • 20
    • 5444267588 scopus 로고    scopus 로고
    • Dry eye: diagnosis and current treatment strategies
    • O'Brien PD, Collum LM (2004). Dry eye: diagnosis and current treatment strategies. Curr Allergy Asthma Rep 4: 314-319.
    • (2004) Curr Allergy Asthma Rep , vol.4 , pp. 314-319
    • O'Brien, P.D.1    Collum, L.M.2
  • 21
    • 77950504881 scopus 로고    scopus 로고
    • Rheological properties of hyaluronic acid and its effects on salivary enzymes and candida
    • Park MS, Chang JY, Kang JH, Park KP, Kho HS (2010). Rheological properties of hyaluronic acid and its effects on salivary enzymes and candida. Oral Dis 16: 382-387.
    • (2010) Oral Dis , vol.16 , pp. 382-387
    • Park, M.S.1    Chang, J.Y.2    Kang, J.H.3    Park, K.P.4    Kho, H.S.5
  • 22
    • 0001084885 scopus 로고
    • Purification and analysis of human saliva lysozyme
    • Petit JF, Jolles P (1963). Purification and analysis of human saliva lysozyme. Nature 200: 168-169.
    • (1963) Nature , vol.200 , pp. 168-169
    • Petit, J.F.1    Jolles, P.2
  • 23
    • 0030186170 scopus 로고    scopus 로고
    • Hyaluronan (hyaluronic acid) in human saliva
    • Pogrel MA, Lowe MA, Stern R (1996). Hyaluronan (hyaluronic acid) in human saliva. Arch Oral Biol 41: 667-671.
    • (1996) Arch Oral Biol , vol.41 , pp. 667-671
    • Pogrel, M.A.1    Lowe, M.A.2    Stern, R.3
  • 24
    • 0142093129 scopus 로고    scopus 로고
    • Hyaluronan (hyaluronic acid) and its regulation in human saliva by hyaluronidase and its inhibitors
    • Pogrel MA, Low MA, Stern R (2003). Hyaluronan (hyaluronic acid) and its regulation in human saliva by hyaluronidase and its inhibitors. J Oral Sci 45: 85-91.
    • (2003) J Oral Sci , vol.45 , pp. 85-91
    • Pogrel, M.A.1    Low, M.A.2    Stern, R.3
  • 26
    • 0032088677 scopus 로고    scopus 로고
    • Efficacy of a synthetic polymer saliva substitute in reducing oral complaints of patients suffering from irradiation-induced xerostomia
    • Regelink G, Vissink A, Reintsema H, Nauta JM (1998). Efficacy of a synthetic polymer saliva substitute in reducing oral complaints of patients suffering from irradiation-induced xerostomia. Quintessence Int 29: 383-388.
    • (1998) Quintessence Int , vol.29 , pp. 383-388
    • Regelink, G.1    Vissink, A.2    Reintsema, H.3    Nauta, J.M.4
  • 27
    • 34249661233 scopus 로고    scopus 로고
    • Potential role of high molecular weight hyaluronan in the anti-Candida activity of human oral epithelial cells
    • Sakai A, Akifusa S, Itano N et al (2007). Potential role of high molecular weight hyaluronan in the anti-Candida activity of human oral epithelial cells. Med Mycol 45: 73-79.
    • (2007) Med Mycol , vol.45 , pp. 73-79
    • Sakai, A.1    Akifusa, S.2    Itano, N.3
  • 28
    • 0034783753 scopus 로고    scopus 로고
    • Potential role for a carbohydrate moiety in anti-Candida activity of human epithelial cells
    • Steele C, Leigh J, Swoboda R, Ozenci H, Fidel PL Jr (2001). Potential role for a carbohydrate moiety in anti-Candida activity of human epithelial cells. Infect Immun 69: 7091-7099.
    • (2001) Infect Immun , vol.69 , pp. 7091-7099
    • Steele, C.1    Leigh, J.2    Swoboda, R.3    Ozenci, H.4    Fidel Jr., P.L.5
  • 29
    • 0036120646 scopus 로고    scopus 로고
    • Clinical applications of antimicrobial host proteins, lactoperoxidase, lysozyme and lactoferrin in xerostomia: efficacy and safety
    • Tenovuo J (2002). Clinical applications of antimicrobial host proteins, lactoperoxidase, lysozyme and lactoferrin in xerostomia: efficacy and safety. Oral Dis 8: 23-29.
    • (2002) Oral Dis , vol.8 , pp. 23-29
    • Tenovuo, J.1
  • 31
    • 0026043448 scopus 로고
    • Binding of hyaluronan to lysozyme at various pHs and salt concentrations
    • Van Damme MP, Moss JM, Murphy WH, Preston BN (1991). Binding of hyaluronan to lysozyme at various pHs and salt concentrations. Biochem Int 24: 605-613.
    • (1991) Biochem Int , vol.24 , pp. 605-613
    • Van Damme, M.P.1    Moss, J.M.2    Murphy, W.H.3    Preston, B.N.4
  • 32
    • 0028223569 scopus 로고
    • Binding properties of glycosaminoglycans to lysozyme - effect of salt and molecular weight
    • Van Damme MP, Moss JM, Murphy WH, Preston BN (1994). Binding properties of glycosaminoglycans to lysozyme - effect of salt and molecular weight. Arch Biochem Biophys 310: 16-24.
    • (1994) Arch Biochem Biophys , vol.310 , pp. 16-24
    • Van Damme, M.P.1    Moss, J.M.2    Murphy, W.H.3    Preston, B.N.4
  • 33
    • 0021353997 scopus 로고
    • Rheological properties of saliva substitutes containing mucin, carboxymethylcellulose or polyethylenoxide
    • Vissink A, Waterman HA, 's-Gravenmade EJ, Panders AK, Vermey A (1984). Rheological properties of saliva substitutes containing mucin, carboxymethylcellulose or polyethylenoxide. J Oral Pathol 13: 22-28.
    • (1984) J Oral Pathol , vol.13 , pp. 22-28
    • Vissink, A.1    Waterman, H.A.2    's-Gravenmade, E.J.3    Panders, A.K.4    Vermey, A.5
  • 34
    • 0023431174 scopus 로고
    • Effect of the application of a mucin-based saliva substitute on the oral microflora of xerostomic patients
    • Weerkamp AH, Wagner K, Vissink A, 's-Gravenmade EJ (1987). Effect of the application of a mucin-based saliva substitute on the oral microflora of xerostomic patients. J Oral Pathol 16: 474-478.
    • (1987) J Oral Pathol , vol.16 , pp. 474-478
    • Weerkamp, A.H.1    Wagner, K.2    Vissink, A.3    's-Gravenmade, E.J.4
  • 35
    • 68349144161 scopus 로고    scopus 로고
    • Effect of lactoperoxidase on the antimicrobial effectiveness of the thiocyanate hydrogen peroxide combination in a quantitative suspension test
    • Welk A, Meller Ch, Schubert R, Schwahn Ch, Kramer A, Below H (2009). Effect of lactoperoxidase on the antimicrobial effectiveness of the thiocyanate hydrogen peroxide combination in a quantitative suspension test. BMC Microbiol 9: 134.
    • (2009) BMC Microbiol , vol.9 , pp. 134
    • Welk, A.1    Meller, C.2    Schubert, R.3    Schwahn, C.4    Kramer, A.5    Below, H.6
  • 36
    • 0020603168 scopus 로고
    • Candidacidal activity of myeloperoxidase: mechanisms of inhibitory influence of soluble cell wall mannan
    • Wright CD, Bowie JU, Gray GR, Nelson RD (1983). Candidacidal activity of myeloperoxidase: mechanisms of inhibitory influence of soluble cell wall mannan. Infect Immun 42: 76-80.
    • (1983) Infect Immun , vol.42 , pp. 76-80
    • Wright, C.D.1    Bowie, J.U.2    Gray, G.R.3    Nelson, R.D.4
  • 37
    • 0032878759 scopus 로고    scopus 로고
    • Inhibition of growth and secreted aspartyl proteinase production in Candida albicans by lysozyme
    • Wu T, Samaranayake LP, Leung WK, Sullivan PA (1999). Inhibition of growth and secreted aspartyl proteinase production in Candida albicans by lysozyme. J Med Microbiol 48: 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.