메뉴 건너뛰기




Volumn 358, Issue 1, 2007, Pages 277-284

Pro-oxidant activity of histatin 5 related Cu(II)-model peptide probed by mass spectrometry

Author keywords

"ATCUN" motif; ESI IT MS spectrometry; Histatin 5; Metals; Reactive oxygen species (ROS)

Indexed keywords

ASCORBIC ACID; COPPER ION; HISTATIN 5; NICKEL; REACTIVE OXYGEN METABOLITE;

EID: 34248372445     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.04.121     Document Type: Article
Times cited : (41)

References (29)
  • 1
    • 0027215164 scopus 로고
    • Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family
    • Sabatini L.M., Ota T., and Azen E.A. Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family. Mol. Biol. Evol. 10 (1993) 497-511
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 497-511
    • Sabatini, L.M.1    Ota, T.2    Azen, E.A.3
  • 4
    • 0023888810 scopus 로고
    • Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans
    • Oppenheim F.G., Xu T., McMillian F.M., Levitz S.M., Diamond R.D., Offner G.D., and Troxler R.F. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J. Biol. Chem. 263 (1988) 7472-7477
    • (1988) J. Biol. Chem. , vol.263 , pp. 7472-7477
    • Oppenheim, F.G.1    Xu, T.2    McMillian, F.M.3    Levitz, S.M.4    Diamond, R.D.5    Offner, G.D.6    Troxler, R.F.7
  • 5
    • 0017952427 scopus 로고
    • Biochemical effects of micronazole on fungi. II. Inhibition of ergosterol biosynthesis in Candida albicans
    • van den Bossche H., Willemsens G., Cools W., Lauwers W.F., and Le Jeune L. Biochemical effects of micronazole on fungi. II. Inhibition of ergosterol biosynthesis in Candida albicans. Chem. Biol. Interact. 21 (1978) 59-78
    • (1978) Chem. Biol. Interact. , vol.21 , pp. 59-78
    • van den Bossche, H.1    Willemsens, G.2    Cools, W.3    Lauwers, W.F.4    Le Jeune, L.5
  • 7
    • 0035807815 scopus 로고    scopus 로고
    • The human salivary peptide histatin 5 exerts its antifungal activity through the formation of reactive oxygen species
    • Helmerhorst E.J., Troxler R.F., and Oppenheim F.G. The human salivary peptide histatin 5 exerts its antifungal activity through the formation of reactive oxygen species. Proc. Natl. Acad. Sci. USA 98 (2001) 14637-14642
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14637-14642
    • Helmerhorst, E.J.1    Troxler, R.F.2    Oppenheim, F.G.3
  • 8
    • 0042208078 scopus 로고    scopus 로고
    • Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5
    • Li X.S., Reddy M.S., Baev D., and Edgerton M. Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5. J. Biol. Chem. 278 (2003) 28553-28661
    • (2003) J. Biol. Chem. , vol.278 , pp. 28553-28661
    • Li, X.S.1    Reddy, M.S.2    Baev, D.3    Edgerton, M.4
  • 9
    • 11244278605 scopus 로고    scopus 로고
    • The TRK1 potassium transporter is the critical effector for killing of Candida albicans by the cationic protein, Histatin 5
    • Baev D., Rivetta A., Vylkova S., Sun J.N., Zeng G.F., Slayman C.L., and Edgerton M. The TRK1 potassium transporter is the critical effector for killing of Candida albicans by the cationic protein, Histatin 5. J. Biol. Chem. 279 (2004) 55060-55072
    • (2004) J. Biol. Chem. , vol.279 , pp. 55060-55072
    • Baev, D.1    Rivetta, A.2    Vylkova, S.3    Sun, J.N.4    Zeng, G.F.5    Slayman, C.L.6    Edgerton, M.7
  • 11
    • 0033609529 scopus 로고    scopus 로고
    • 2+ ions selectively induce antimicrobial salivary peptide histatin 5 to fuse negatively charged vesicles. Identification and characterization of a zinc binding motif present in the functional domain
    • 2+ ions selectively induce antimicrobial salivary peptide histatin 5 to fuse negatively charged vesicles. Identification and characterization of a zinc binding motif present in the functional domain. Biochemistry 38 (1999) 9626-9633
    • (1999) Biochemistry , vol.38 , pp. 9626-9633
    • Melino, S.1    Rufini, S.2    Sette, M.3    Morero, R.4    Grottesi, A.5    Paci, M.6    Petruzzelli, R.7
  • 13
    • 0020837254 scopus 로고
    • DNA- and protein-scission activities of ascorbate in the presence of copper ion and a copper-peptide complex
    • Chiou S.H. DNA- and protein-scission activities of ascorbate in the presence of copper ion and a copper-peptide complex. J. Biochem. Tokyo 94 (1983) 1259-1267
    • (1983) J. Biochem. Tokyo , vol.94 , pp. 1259-1267
    • Chiou, S.H.1
  • 14
    • 0039911097 scopus 로고
    • Interaction of one mole of copper with the alpha amino group of bovine serum albumin
    • Peters Jr. T. Interaction of one mole of copper with the alpha amino group of bovine serum albumin. Biochim. Biophys. Acta 39 (1960) 546-547
    • (1960) Biochim. Biophys. Acta , vol.39 , pp. 546-547
    • Peters Jr., T.1
  • 15
    • 0032010153 scopus 로고    scopus 로고
    • Universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra
    • Zhang Z., and Marshall A.G.A. Universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra. J. Am. Soc. Mass Spectrom. 9 (1998) 225-233
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , pp. 225-233
    • Zhang, Z.1    Marshall, A.G.A.2
  • 16
    • 0019981504 scopus 로고
    • Nickel(II) transport in human blood serum. Studies of nickel(II) binding to human albumin and to native-sequence peptide, and ternary-complex formation with l-histidine
    • Glennon J.D., and Sarkar B. Nickel(II) transport in human blood serum. Studies of nickel(II) binding to human albumin and to native-sequence peptide, and ternary-complex formation with l-histidine. Biochem. J. 203 (1982) 15-23
    • (1982) Biochem. J. , vol.203 , pp. 15-23
    • Glennon, J.D.1    Sarkar, B.2
  • 17
    • 0019972224 scopus 로고
    • The non-specificity of dog serum albumin and the N-terminal model peptide glycylglycyl-l-tyrosine n-methylamide for nickel is due to the lack of histidine in the third position
    • Glennon J.D., and Sarkar B. The non-specificity of dog serum albumin and the N-terminal model peptide glycylglycyl-l-tyrosine n-methylamide for nickel is due to the lack of histidine in the third position. Biochem J. 203 (1982) 25-31
    • (1982) Biochem J. , vol.203 , pp. 25-31
    • Glennon, J.D.1    Sarkar, B.2
  • 18
    • 0033794888 scopus 로고    scopus 로고
    • Evaluation of the metal binding properties of the histidine-rich antimicrobial peptides histatin 3 and 5 by electrospray ionization mass spectrometry
    • Brewer D., and Lajoie G. Evaluation of the metal binding properties of the histidine-rich antimicrobial peptides histatin 3 and 5 by electrospray ionization mass spectrometry. Rapid Commun. Mass Spectrom. 14 (2000) 1736-1745
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1736-1745
    • Brewer, D.1    Lajoie, G.2
  • 19
    • 0347992031 scopus 로고    scopus 로고
    • Human salivary histatin 5 fungicidal action does not induce programmed cell death pathways in Candida albicans
    • Wunder D., Dong J., Baev D., and Edgerton M. Human salivary histatin 5 fungicidal action does not induce programmed cell death pathways in Candida albicans. Antimicrob. Agents Chemother. 48 (2004) 110-115
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 110-115
    • Wunder, D.1    Dong, J.2    Baev, D.3    Edgerton, M.4
  • 20
    • 1842739598 scopus 로고    scopus 로고
    • Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrix
    • Cobine P.A., Ojeda L.D., Rigby K.M., and Winge D.R. Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrix. J. Biol. Chem. 279 (2004) 14447-14455
    • (2004) J. Biol. Chem. , vol.279 , pp. 14447-14455
    • Cobine, P.A.1    Ojeda, L.D.2    Rigby, K.M.3    Winge, D.R.4
  • 21
    • 0036098268 scopus 로고    scopus 로고
    • Cu(II)-catalyzed oxidation of beta-amyloid peptide targets His13 and His 14 over His 6: detection of 2-Oxo-histidine by HPLC-MS/MS
    • Schoneich C., and Williams T.D. Cu(II)-catalyzed oxidation of beta-amyloid peptide targets His13 and His 14 over His 6: detection of 2-Oxo-histidine by HPLC-MS/MS. Chem. Res. Toxicol. 15 (2002) 717-722
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 717-722
    • Schoneich, C.1    Williams, T.D.2
  • 22
    • 0037353826 scopus 로고    scopus 로고
    • Development of a methodology based on metal-catalyzed oxidation reactions and mass spectrometry to determine the metal binding sites in copper metalloproteins
    • Lim J., and Vachet R. Development of a methodology based on metal-catalyzed oxidation reactions and mass spectrometry to determine the metal binding sites in copper metalloproteins. Anal. Chem. 75 (2003) 1164-1172
    • (2003) Anal. Chem. , vol.75 , pp. 1164-1172
    • Lim, J.1    Vachet, R.2
  • 23
    • 33750011594 scopus 로고    scopus 로고
    • Characterization of the metal binding site of human prolactin by site-specific metal-catalyzed oxidation
    • Sadineni V., Galeva N.A., and Schoneich C. Characterization of the metal binding site of human prolactin by site-specific metal-catalyzed oxidation. Anal. Biochem. 358 (2006) 208-215
    • (2006) Anal. Biochem. , vol.358 , pp. 208-215
    • Sadineni, V.1    Galeva, N.A.2    Schoneich, C.3
  • 24
    • 0026795211 scopus 로고
    • Sequence-specific oxidative cleavage of DNA by a designed metalloprotein, Ni(II)GGH(Hin139-190)
    • Mack D.P., and Dervan P.B. Sequence-specific oxidative cleavage of DNA by a designed metalloprotein, Ni(II)GGH(Hin139-190). Biochemistry 31 (1992) 9399-9405
    • (1992) Biochemistry , vol.31 , pp. 9399-9405
    • Mack, D.P.1    Dervan, P.B.2
  • 25
    • 0032167555 scopus 로고    scopus 로고
    • Selective recognition and cleavage of RNA loop structures by Ni(II). Xaa-Gly-His metallopeptides
    • Brittain I.J., Huang X., and Long E.C. Selective recognition and cleavage of RNA loop structures by Ni(II). Xaa-Gly-His metallopeptides. Biochemistry 37 (1998) 12113-12120
    • (1998) Biochemistry , vol.37 , pp. 12113-12120
    • Brittain, I.J.1    Huang, X.2    Long, E.C.3
  • 26
    • 20444459812 scopus 로고    scopus 로고
    • DNA cleavage by copper-ATCUN complexes. Factors influencing cleavage mechanism and linearization of dsDNA
    • Yan J., and Cowan J.A. DNA cleavage by copper-ATCUN complexes. Factors influencing cleavage mechanism and linearization of dsDNA. J. Am. Chem. Soc. 127 (2005) 8408-8415
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8408-8415
    • Yan, J.1    Cowan, J.A.2
  • 27
    • 0028098076 scopus 로고
    • Light activated cleavage of DNA by cobalt-bleomycin
    • Nightingale K.P., and Fox K.R. Light activated cleavage of DNA by cobalt-bleomycin. Eur. J. Biochem. 220 (1994) 173-181
    • (1994) Eur. J. Biochem. , vol.220 , pp. 173-181
    • Nightingale, K.P.1    Fox, K.R.2
  • 28
    • 0030877009 scopus 로고    scopus 로고
    • Mediation of oxidative damage by nickel(II) and copper(II) complexes with the N-terminal sequence of human protamine HP2
    • Bal W., Lukszo J., and Kasprzak K.S. Mediation of oxidative damage by nickel(II) and copper(II) complexes with the N-terminal sequence of human protamine HP2. Chem. Res. Toxicol. 10 (1997) 915-921
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 915-921
    • Bal, W.1    Lukszo, J.2    Kasprzak, K.S.3
  • 29
    • 0034863640 scopus 로고    scopus 로고
    • Copper stimulates human oral fibroblasts in vitro: a role in the pathogenesis of oral submucous fibrosis
    • Trivedy C., Meghji S., Warnakulasurija K.A.A.S., Johnson N.W., and Harris M.J. Copper stimulates human oral fibroblasts in vitro: a role in the pathogenesis of oral submucous fibrosis. Oral. Pathol. Med. 30 (2001) 465-470
    • (2001) Oral. Pathol. Med. , vol.30 , pp. 465-470
    • Trivedy, C.1    Meghji, S.2    Warnakulasurija, K.A.A.S.3    Johnson, N.W.4    Harris, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.