메뉴 건너뛰기




Volumn 9, Issue 10, 2010, Pages 5413-5421

Mass spectrometric identification of key proteolytic cleavage sites in statherin affecting mineral homeostasis and bacterial binding domains

Author keywords

enzymatic; fragmentation; oral; saliva; statherin

Indexed keywords

ARGININE; GLYCINE; PHENYLALANINE; STATHERIN; TYROSINE; ZINC CHLORIDE;

EID: 77957359728     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr100653r     Document Type: Article
Times cited : (25)

References (40)
  • 1
    • 0015721165 scopus 로고
    • The isolation from human parotid saliva of a tyrosine-rich acidic peptide which exhibits high affinity for hydroxyapatite surfaces
    • Hay, D. I. The isolation from human parotid saliva of a tyrosine-rich acidic peptide which exhibits high affinity for hydroxyapatite surfaces Arch. Oral Biol. 1973, 18 (12) 1531-41
    • (1973) Arch. Oral Biol. , vol.18 , Issue.12 , pp. 1531-1541
    • Hay, D.I.1
  • 2
    • 0017348985 scopus 로고
    • Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva
    • Schlesinger, D. H.; Hay, D. I. Complete covalent structure of statherin, a tyrosine-rich acidic peptide which inhibits calcium phosphate precipitation from human parotid saliva J. Biol. Chem. 1977, 252 (5) 1689-95
    • (1977) J. Biol. Chem. , vol.252 , Issue.5 , pp. 1689-1695
    • Schlesinger, D.H.1    Hay, D.I.2
  • 4
    • 33846028206 scopus 로고    scopus 로고
    • HPLC-MS characterization of cyclo-statherin Q-37, a specific cyclization product of human salivary statherin generated by transglutaminase 2
    • Cabras, T.; Inzitari, R.; Fanali, C.; Scarano, E.; Patamia, M.; Sanna, M. T.; Pisano, E.; Giardina, B.; Castagnola, M.; Messana, I. HPLC-MS characterization of cyclo-statherin Q-37, a specific cyclization product of human salivary statherin generated by transglutaminase 2 J. Sep. Sci. 2006, 29 (17) 2600-8
    • (2006) J. Sep. Sci. , vol.29 , Issue.17 , pp. 2600-2608
    • Cabras, T.1    Inzitari, R.2    Fanali, C.3    Scarano, E.4    Patamia, M.5    Sanna, M.T.6    Pisano, E.7    Giardina, B.8    Castagnola, M.9    Messana, I.10
  • 5
    • 1842592027 scopus 로고    scopus 로고
    • Statherin is an in vivo pellicle constituent: Identification and immuno-quantification
    • DOI 10.1016/j.archoralbio.2004.01.002, PII S0003996904000093
    • Li, J.; Helmerhorst, E. J.; Yao, Y.; Nunn, M. E.; Troxler, R. F.; Oppenheim, F. G. Statherin is an in vivo pellicle constituent: identification and immuno-quantification Arch. Oral Biol. 2004, 49 (5) 379-85 (Pubitemid 38431023)
    • (2004) Archives of Oral Biology , vol.49 , Issue.5 , pp. 379-385
    • Li, J.1    Helmerhorst, E.J.2    Yao, Y.3    Nunn, M.E.4    Troxler, R.F.5    Oppenheim, F.G.6
  • 7
    • 0018571582 scopus 로고
    • Phosphoprotein-inhibitors of calcium phosphate precipitation from salivary secretions
    • Hay, D. I.; Moreno, E. C.; Schlesinger, D. H. Phosphoprotein-inhibitors of calcium phosphate precipitation from salivary secretions Inorg. Perspec. Biol. Med. 1979, 2, 271-85
    • (1979) Inorg. Perspec. Biol. Med. , vol.2 , pp. 271-285
    • Hay, D.I.1    Moreno, E.C.2    Schlesinger, D.H.3
  • 9
    • 33750817561 scopus 로고    scopus 로고
    • Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals
    • Goobes, G.; Goobes, R.; Schueler-Furman, O.; Baker, D.; Stayton, P. S.; Drobny, G. P. Folding of the C-terminal bacterial binding domain in statherin upon adsorption onto hydroxyapatite crystals Proc. Natl. Acad. Sci. U.S.A. 2006, 103 (44) 16083-8
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , Issue.44 , pp. 16083-16088
    • Goobes, G.1    Goobes, R.2    Schueler-Furman, O.3    Baker, D.4    Stayton, P.S.5    Drobny, G.P.6
  • 10
    • 0031923274 scopus 로고    scopus 로고
    • Binding of Porphyromonas gingivalis fimbriae to proline-rich glycoproteins in parotid saliva via a domain shared by major salivary components
    • Amano, A.; Shizukuishi, S.; Horie, H.; Kimura, S.; Morisaki, I.; Hamada, S. Binding of Porphyromonas gingivalis fimbriae to proline-rich glycoproteins in parotid saliva via a domain shared by major salivary components Infect. Immun. 1998, 66 (5), 2072-7
    • (1998) Infect. Immun. , vol.66 , Issue.5 , pp. 2072-2077
    • Amano, A.1    Shizukuishi, S.2    Horie, H.3    Kimura, S.4    Morisaki, I.5    Hamada, S.6
  • 11
    • 0032899829 scopus 로고    scopus 로고
    • Strains of Actinomyces naeslundii and Actinomyces viscosus exhibit structurally variant fimbrial subunit proteins and bind to different peptide motifs in salivary proteins
    • Li, T.; Johansson, I.; Hay, D. I.; Stromberg, N. Strains of Actinomyces naeslundii and Actinomyces viscosus exhibit structurally variant fimbrial subunit proteins and bind to different peptide motifs in salivary proteins Infect. Immun. 1999, 67 (5) 2053-9
    • (1999) Infect. Immun. , vol.67 , Issue.5 , pp. 2053-2059
    • Li, T.1    Johansson, I.2    Hay, D.I.3    Stromberg, N.4
  • 12
    • 0842283894 scopus 로고    scopus 로고
    • Salivary statherin peptide-binding epitopes of commensal and potentially infectious Actinomyces spp. delineated by a hybrid peptide construct
    • Niemi, L. D.; Johansson, I. Salivary statherin peptide-binding epitopes of commensal and potentially infectious Actinomyces spp. delineated by a hybrid peptide construct Infect. Immun. 2004, 72 (2) 782-7
    • (2004) Infect. Immun. , vol.72 , Issue.2 , pp. 782-787
    • Niemi, L.D.1    Johansson, I.2
  • 13
    • 4344623485 scopus 로고    scopus 로고
    • Active domains of salivary statherin on apatitic surfaces for binding to Fusobacterium nucleatum cells
    • Sekine, S.; Kataoka, K.; Tanaka, M.; Nagata, H.; Kawakami, T.; Akaji, K.; Aimoto, S.; Shizukuishi, S. Active domains of salivary statherin on apatitic surfaces for binding to Fusobacterium nucleatum cells Microbiology 2004, 150 (Pt 7) 2373-9
    • (2004) Microbiology , vol.150 , Issue.PART 7 , pp. 2373-2379
    • Sekine, S.1    Kataoka, K.2    Tanaka, M.3    Nagata, H.4    Kawakami, T.5    Akaji, K.6    Aimoto, S.7    Shizukuishi, S.8
  • 14
    • 70350022242 scopus 로고    scopus 로고
    • Identification of salivary components that induce transition of hyphae to yeast in Candida albicans
    • Leito, J. T.; Ligtenberg, A. J.; Nazmi, K.; Veerman, E. C. Identification of salivary components that induce transition of hyphae to yeast in Candida albicans FEMS Yeast Res. 2009, 9 (7) 1102-10
    • (2009) FEMS Yeast Res. , vol.9 , Issue.7 , pp. 1102-1110
    • Leito, J.T.1    Ligtenberg, A.J.2    Nazmi, K.3    Veerman, E.C.4
  • 15
    • 0030291942 scopus 로고    scopus 로고
    • Solid-phase synthesis and characterization of human salivary statherin: A tyrosine-rich phosphoprotein inhibitor of calcium phosphate precipitation
    • Gururaja, T. L.; Levine, M. J. Solid-phase synthesis and characterization of human salivary statherin: a tyrosine-rich phosphoprotein inhibitor of calcium phosphate precipitation Pept. Res. 1996, 9 (6) 283-9
    • (1996) Pept. Res. , vol.9 , Issue.6 , pp. 283-289
    • Gururaja, T.L.1    Levine, M.J.2
  • 17
    • 50649088005 scopus 로고    scopus 로고
    • Identification of Lys-Pro-Gln as a novel cleavage site specificity of saliva-associated proteases
    • Helmerhorst, E. J.; Sun, X.; Salih, E.; Oppenheim, F. G. Identification of Lys-Pro-Gln as a novel cleavage site specificity of saliva-associated proteases J. Biol. Chem. 2008, 283 (29) 19957-66
    • (2008) J. Biol. Chem. , vol.283 , Issue.29 , pp. 19957-19966
    • Helmerhorst, E.J.1    Sun, X.2    Salih, E.3    Oppenheim, F.G.4
  • 18
    • 0034805369 scopus 로고    scopus 로고
    • A new method for the isolation of histatins 1, 3, and 5 from parotid secretion using zinc precipitation
    • Flora, B.; Gusman, H.; Helmerhorst, E. J.; Troxler, R. F.; Oppenheim, F. G. A new method for the isolation of histatins 1, 3, and 5 from parotid secretion using zinc precipitation Protein Expr. Purif. 2001, 23 (1) 198-206
    • (2001) Protein Expr. Purif. , vol.23 , Issue.1 , pp. 198-206
    • Flora, B.1    Gusman, H.2    Helmerhorst, E.J.3    Troxler, R.F.4    Oppenheim, F.G.5
  • 19
    • 0017572695 scopus 로고
    • Histidine-rich-polypeptides in Macaque parotid saliva are not nuclear histones
    • Baum, B. J.; Bird, J. L.; Longton, R. W. Histidine-rich-polypeptides in Macaque parotid saliva are not nuclear histones Arch. Oral Biol. 1977, 22 (7) 455-6
    • (1977) Arch. Oral Biol. , vol.22 , Issue.7 , pp. 455-456
    • Baum, B.J.1    Bird, J.L.2    Longton, R.W.3
  • 20
    • 61449147898 scopus 로고    scopus 로고
    • Concentration and fate of histatins and acidic proline-rich proteins in the oral environment
    • Campese, M.; Sun, X.; Bosch, J. A.; Oppenheim, F. G.; Helmerhorst, E. J. Concentration and fate of histatins and acidic proline-rich proteins in the oral environment Arch. Oral Biol. 2009, 54 (4) 345-53
    • (2009) Arch. Oral Biol. , vol.54 , Issue.4 , pp. 345-353
    • Campese, M.1    Sun, X.2    Bosch, J.A.3    Oppenheim, F.G.4    Helmerhorst, E.J.5
  • 21
    • 78651153791 scopus 로고
    • Disc Electrophoresis. Ii. Method and Application to Human Serum Proteins
    • Davis, B. J. Disc Electrophoresis. Ii. Method And Application To Human Serum Proteins Ann. N.Y. Acad. Sci. 1964, 121, 404-27
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 22
    • 0020441762 scopus 로고
    • Phosphoproteins in the parotid saliva from the subhuman primate Macaca fascicularis. Isolation and characterization of a proline-rich phosphoglycoprotein and the complete covalent structure of a proline-rich phosphopeptide
    • Oppenheim, F. G.; Offner, G. D.; Troxler, R. F. Phosphoproteins in the parotid saliva from the subhuman primate Macaca fascicularis. Isolation and characterization of a proline-rich phosphoglycoprotein and the complete covalent structure of a proline-rich phosphopeptide J. Biol. Chem. 1982, 257 (16) 9271-82
    • (1982) J. Biol. Chem. , vol.257 , Issue.16 , pp. 9271-9282
    • Oppenheim, F.G.1    Offner, G.D.2    Troxler, R.F.3
  • 23
    • 0020480152 scopus 로고
    • Structure of the carbohydrate chains of the proline-rich glycoprotein from human parotid saliva
    • Reddy, M. S.; Levine, M. J.; Tabak, L. A. Structure of the carbohydrate chains of the proline-rich glycoprotein from human parotid saliva Biochem. Biophys. Res. Commun. 1982, 104 (3) 882-8
    • (1982) Biochem. Biophys. Res. Commun. , vol.104 , Issue.3 , pp. 882-888
    • Reddy, M.S.1    Levine, M.J.2    Tabak, L.A.3
  • 24
    • 0027292301 scopus 로고
    • Salivary alpha-amylase: Role in dental plaque and caries formation
    • Scannapieco, F. A.; Torres, G.; Levine, M. J. Salivary alpha-amylase: role in dental plaque and caries formation Crit. Rev. Oral Biol. Med. 1993, 4 (3-4) 301-7
    • (1993) Crit. Rev. Oral Biol. Med. , vol.4 , Issue.3-4 , pp. 301-307
    • Scannapieco, F.A.1    Torres, G.2    Levine, M.J.3
  • 25
    • 0017699712 scopus 로고
    • Polyacrylamide gel electrophoresis of human salivary histidine-rich- polypeptides
    • Baum, B. J.; Bird, J. L.; Longton, R. W. Polyacrylamide gel electrophoresis of human salivary histidine-rich-polypeptides J. Dent. Res. 1977, 56 (9) 1115-8
    • (1977) J. Dent. Res. , vol.56 , Issue.9 , pp. 1115-1118
    • Baum, B.J.1    Bird, J.L.2    Longton, R.W.3
  • 26
    • 78651163419 scopus 로고
    • Disc Electrophoresis. I. Background and Theory
    • Ornstein, L. Disc Electrophoresis. I. Background And Theory Ann. N.Y. Acad. Sci. 1964, 121, 321-49
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 321-349
    • Ornstein, L.1
  • 27
    • 0028537955 scopus 로고
    • Human salivary acidic proline-rich protein polymorphisms and biosynthesis studied by high-performance liquid chromatography
    • Hay, D. I.; Ahern, J. M.; Schluckebier, S. K.; Schlesinger, D. H. Human salivary acidic proline-rich protein polymorphisms and biosynthesis studied by high-performance liquid chromatography J. Dent. Res. 1994, 73 (11) 1717-26
    • (1994) J. Dent. Res. , vol.73 , Issue.11 , pp. 1717-1726
    • Hay, D.I.1    Ahern, J.M.2    Schluckebier, S.K.3    Schlesinger, D.H.4
  • 28
    • 0022623229 scopus 로고
    • The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion
    • Oppenheim, F. G.; Yang, Y. C.; Diamond, R. D.; Hyslop, D.; Offner, G. D.; Troxler, R. F. The primary structure and functional characterization of the neutral histidine-rich polypeptide from human parotid secretion J. Biol. Chem. 1986, 261 (3) 1177-82
    • (1986) J. Biol. Chem. , vol.261 , Issue.3 , pp. 1177-1182
    • Oppenheim, F.G.1    Yang, Y.C.2    Diamond, R.D.3    Hyslop, D.4    Offner, G.D.5    Troxler, R.F.6
  • 30
    • 33750618079 scopus 로고    scopus 로고
    • Oral fluid proteolytic effects on histatin 5 structure and function
    • Helmerhorst, E. J.; Alagl, A. S.; Siqueira, W. L.; Oppenheim, F. G. Oral fluid proteolytic effects on histatin 5 structure and function Arch. Oral Biol. 2006, 51 (12) 1061-70
    • (2006) Arch. Oral Biol. , vol.51 , Issue.12 , pp. 1061-1070
    • Helmerhorst, E.J.1    Alagl, A.S.2    Siqueira, W.L.3    Oppenheim, F.G.4
  • 34
    • 34250814573 scopus 로고    scopus 로고
    • Identification of protein components in in vivo human acquired enamel pellicle using LC-ESI-MS/MS
    • Siqueira, W. L.; Zhang, W.; Helmerhorst, E. J.; Gygi, S. P.; Oppenheim, F. G. Identification of protein components in in vivo human acquired enamel pellicle using LC-ESI-MS/MS J. Proteome Res. 2007, 6 (6) 2152-60
    • (2007) J. Proteome Res. , vol.6 , Issue.6 , pp. 2152-2160
    • Siqueira, W.L.1    Zhang, W.2    Helmerhorst, E.J.3    Gygi, S.P.4    Oppenheim, F.G.5
  • 36
    • 70349366462 scopus 로고    scopus 로고
    • Activity-based mass spectrometric characterization of proteases and inhibitors in human saliva
    • Sun, X.; Salih, E.; Oppenheim, F. G.; Helmerhorst, E. J. Activity-based mass spectrometric characterization of proteases and inhibitors in human saliva Proteomics: Clin. Appl. 2009, 3 (7) 810-820
    • (2009) Proteomics: Clin. Appl. , vol.3 , Issue.7 , pp. 810-820
    • Sun, X.1    Salih, E.2    Oppenheim, F.G.3    Helmerhorst, E.J.4
  • 37
    • 0026688607 scopus 로고
    • Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization
    • Raj, P. A.; Johnsson, M.; Levine, M. J.; Nancollas, G. H. Salivary statherin. Dependence on sequence, charge, hydrogen bonding potency, and helical conformation for adsorption to hydroxyapatite and inhibition of mineralization J. Biol. Chem. 1992, 267 (9) 5968-76
    • (1992) J. Biol. Chem. , vol.267 , Issue.9 , pp. 5968-5976
    • Raj, P.A.1    Johnsson, M.2    Levine, M.J.3    Nancollas, G.H.4
  • 38
    • 0025886803 scopus 로고
    • Delineation of a segment of adsorbed salivary acidic proline-rich proteins which promotes adhesion of Streptococcus gordonii to apatitic surfaces
    • Gibbons, R. J.; Hay, D. I.; Schlesinger, D. H. Delineation of a segment of adsorbed salivary acidic proline-rich proteins which promotes adhesion of Streptococcus gordonii to apatitic surfaces Infect. Immun. 1991, 59 (9) 2948-54
    • (1991) Infect. Immun. , vol.59 , Issue.9 , pp. 2948-2954
    • Gibbons, R.J.1    Hay, D.I.2    Schlesinger, D.H.3
  • 39
    • 77957369476 scopus 로고    scopus 로고
    • Histatin 1 resists oral proteolytic environment when adsorbed to hydroxyapatite
    • McDonald, E.; Goldberg, H. A.; Siqueira, W. L. Histatin 1 resists oral proteolytic environment when adsorbed to hydroxyapatite. J. Dent. Res. 2010, 89, (Spec Iss A): Abstract 357
    • (2010) J. Dent. Res. , vol.89 , pp. 357
    • McDonald, E.1    Goldberg, H.A.2    Siqueira, W.L.3
  • 40
    • 0021206721 scopus 로고
    • Adsorption of molecules of biological interest onto hydroxyapatite
    • Moreno, E. C.; Kresak, M.; Hay, D. I. Adsorption of molecules of biological interest onto hydroxyapatite Calcif. Tissue Int. 1984, 36 (1) 48-59
    • (1984) Calcif. Tissue Int. , vol.36 , Issue.1 , pp. 48-59
    • Moreno, E.C.1    Kresak, M.2    Hay, D.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.