메뉴 건너뛰기




Volumn 368, Issue 2, 2002, Pages 611-620

Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss

Author keywords

Anti bacterial protein; Epithelium; Mucosal immunity; Nucleosome

Indexed keywords

AMINO ACIDS; BACTERIA; CELLS; CHROMATOGRAPHIC ANALYSIS; ION EXCHANGE; IONIZATION; SKIN; YEAST;

EID: 2242429813     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020980     Document Type: Article
Times cited : (161)

References (44)
  • 1
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. (2002) Antimicrobial peptides of multicellular organisms. Nature (London) 415, 389-396
    • (2002) Nature (London) , vol.415 , pp. 389-396
    • Zasloff, M.1
  • 3
    • 0032567666 scopus 로고    scopus 로고
    • Expression of antimicrobial peptides has an antitumour effect in human cells
    • Winder, D., Gunzburg, W. H., Erfle, V. and Salmons, B. (1998) Expression of antimicrobial peptides has an antitumour effect in human cells. Biochem. Biophys. Res. Commun. 242, 608-612
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 608-612
    • Winder, D.1    Gunzburg, W.H.2    Erfle, V.3    Salmons, B.4
  • 5
    • 58149206315 scopus 로고
    • Temperature and teleost immune mechanisms
    • Bly, J. E. and Clem, L. W. (1992) Temperature and teleost immune mechanisms. Fish Shellfish Immunol. 2, 159-171
    • (1992) Fish Shellfish Immunol. , vol.2 , pp. 159-171
    • Bly, J.E.1    Clem, L.W.2
  • 6
    • 0028694311 scopus 로고
    • Antimicrobial peptides as agents of mucosal immunity
    • (Marsh, J. and Goode, J. A., eds.), John Wiley & Sons, London
    • Bevins, C. L. (1994) Antimicrobial peptides as agents of mucosal immunity. In Antimicrobial Peptides, Ciba Foundation Symposium (Marsh, J. and Goode, J. A., eds.), pp. 250-260, John Wiley & Sons, London
    • (1994) Antimicrobial Peptides, Ciba Foundation Symposium , pp. 250-260
    • Bevins, C.L.1
  • 7
    • 0031753591 scopus 로고    scopus 로고
    • Experimental infection of Rana esculenta with Aeromonas hydrophila: A molecular mechanism for the control of the normal flora
    • Simmaco, M., Mangoni, M. L., Boman, A., Barra, D. and Boman, H. G. (1998) Experimental infection of Rana esculenta with Aeromonas hydrophila: A molecular mechanism for the control of the normal flora. Scand. J. Immunol. 48, 357-363
    • (1998) Scand. J. Immunol. , vol.48 , pp. 357-363
    • Simmaco, M.1    Mangoni, M.L.2    Boman, A.3    Barra, D.4    Boman, H.G.5
  • 8
    • 77956721412 scopus 로고    scopus 로고
    • The nonspecific immune system: Humoral defense
    • (Iwama, G. and Nakanishi, T., eds.), Academic Press, San Diego
    • Yano, T. (1996) The nonspecific immune system: Humoral defense. In The Fish Immune System: Organism, Pathogen and Environment, vol. 15 (Iwama, G. and Nakanishi, T., eds.), pp. 105-157, Academic Press, San Diego
    • (1996) The Fish Immune System: Organism, Pathogen and Environment , vol.15 , pp. 105-157
    • Yano, T.1
  • 9
    • 0034870985 scopus 로고    scopus 로고
    • Lectins in fish skin: Do they play a role in host-monogenean interactions?
    • Buchmann, K. (2001) Lectins in fish skin: Do they play a role in host-monogenean interactions? J. Helminthol. 75, 227-231
    • (2001) J. Helminthol. , vol.75 , pp. 227-231
    • Buchmann, K.1
  • 10
    • 84985161685 scopus 로고
    • Skin mucus protease from rainbow trout, Salmo gairdneri Richardson, and its biological significance
    • Hjelmeland, K., Christie, M. and Raa, J. (1983) Skin mucus protease from rainbow trout, Salmo gairdneri Richardson, and its biological significance. J. Fish Biol. 23, 13-22
    • (1983) J. Fish Biol. , vol.23 , pp. 13-22
    • Hjelmeland, K.1    Christie, M.2    Raa, J.3
  • 11
    • 0031449192 scopus 로고    scopus 로고
    • Characterization and expression of c-type lysozyme cDNA from Japanese flounder (Paralichthys olivaceus)
    • Hikima, J., Hirono, I. and Aoki, T. (1997) Characterization and expression of c-type lysozyme cDNA from Japanese flounder (Paralichthys olivaceus). Mol. Mar. Biol. Biotechnol. 6, 339-344
    • (1997) Mol. Mar. Biol. Biotechnol. , vol.6 , pp. 339-344
    • Hikima, J.1    Hirono, I.2    Aoki, T.3
  • 13
    • 0029947232 scopus 로고    scopus 로고
    • A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from Moses sole Pardachirus marmoratus
    • Oren, Z. and Shai, Y. (1996) A class of highly potent antibacterial peptides derived from pardaxin, a pore-forming peptide isolated from Moses sole Pardachirus marmoratus. Eur. J. Biochem. 237, 303-310
    • (1996) Eur. J. Biochem. , vol.237 , pp. 303-310
    • Oren, Z.1    Shai, Y.2
  • 14
    • 0030957967 scopus 로고    scopus 로고
    • Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder
    • Cole, A. M., Weis, P. and Diamond, G. (1997) Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. J. Biol. Chem. 272, 12008-12013
    • (1997) J. Biol. Chem. , vol.272 , pp. 12008-12013
    • Cole, A.M.1    Weis, P.2    Diamond, G.3
  • 15
    • 0032561422 scopus 로고    scopus 로고
    • Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus
    • Park, I. Y., Park, C. B., Kim, M. S. and Kim, S. C. (1998) Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus. FEBS Lett. 437, 258-262
    • (1998) FEBS Lett. , vol.437 , pp. 258-262
    • Park, I.Y.1    Park, C.B.2    Kim, M.S.3    Kim, S.C.4
  • 16
    • 0035038578 scopus 로고    scopus 로고
    • Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin
    • Patrzykat, A., Zhang, L., Mendoza, V., Iwama, G. and Hancock, R. (2001) Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin. Antimicrob. Agents Chemother. 45, 1337-1342
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 1337-1342
    • Patrzykat, A.1    Zhang, L.2    Mendoza, V.3    Iwama, G.4    Hancock, R.5
  • 20
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M. and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 24
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. and Gibson, T. J. (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 25
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal, M. and Mueller, P. (1972) Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. U.S.A. 69, 3561-3566
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 26
    • 0021699091 scopus 로고
    • Organization and nucleotide sequence of rainbow trout histone H2A and H3 genes
    • Connor, W., States, J. C., Mezquita, J. and Dixon, G. H. (1984) Organization and nucleotide sequence of rainbow trout histone H2A and H3 genes. J. Mol. Evol. 20, 236-250
    • (1984) J. Mol. Evol. , vol.20 , pp. 236-250
    • Connor, W.1    States, J.C.2    Mezquita, J.3    Dixon, G.H.4
  • 27
    • 0000220470 scopus 로고
    • Bactericidal action of histone
    • Hirsch, J. G. (1958) Bactericidal action of histone. J. Exp. Med. 108, 925-944
    • (1958) J. Exp. Med. , vol.108 , pp. 925-944
    • Hirsch, J.G.1
  • 29
    • 0031838588 scopus 로고    scopus 로고
    • Antimicrobial activity in the skin of the channel catfish Ictalurus punctatus: Characterization of broad-spectrum histone-like antimicrobial proteins
    • Robinette, D., Wada, S., Arroll, T., Levy, M. G., Miller, W. L. and Noga, E. J. (1998) Antimicrobial activity in the skin of the channel catfish Ictalurus punctatus: Characterization of broad-spectrum histone-like antimicrobial proteins. Cell Mol. Life Sci. 54, 467-475
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 467-475
    • Robinette, D.1    Wada, S.2    Arroll, T.3    Levy, M.G.4    Miller, W.L.5    Noga, E.J.6
  • 30
    • 0025836653 scopus 로고
    • Nucleosome positioning is determined by the (H3-H4)2 tetramer
    • Dong, F. and van Holde, K. E. (1991) Nucleosome positioning is determined by the (H3-H4)2 tetramer. Proc. Natl. Acad. Sci. U.S.A. 88, 10596-10600
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10596-10600
    • Dong, F.1    Van Holde, K.E.2
  • 31
    • 0026357951 scopus 로고
    • H1 histones contribute to candidacidal activities of human epidermal extract
    • Kashima, M. (1991) H1 histones contribute to candidacidal activities of human epidermal extract. J. Dermatol. 18, 695-706
    • (1991) J. Dermatol. , vol.18 , pp. 695-706
    • Kashima, M.1
  • 32
    • 0036514179 scopus 로고    scopus 로고
    • Cathepsin D produces antimicrobial peptide parasin I from histone H2A in the skin mucosa of fish
    • Cho, J. H., Park, I. Y., Kim, H. S., Lee, W. T., Kim, M. S. and Kim, S. C. (2002) Cathepsin D produces antimicrobial peptide parasin I from histone H2A in the skin mucosa of fish. FASEB J. 16, 429-431
    • (2002) FASEB J. , vol.16 , pp. 429-431
    • Cho, J.H.1    Park, I.Y.2    Kim, H.S.3    Lee, W.T.4    Kim, M.S.5    Kim, S.C.6
  • 33
    • 0030068934 scopus 로고    scopus 로고
    • A novel antimicrobial peptide from Bufo bufo gargarizans
    • Park, C. B., Kim, M. S. and Kim, S. C. (1996) A novel antimicrobial peptide from Bufo bufo gargarizans. Biochem. Biophys. Res. Commun. 218, 408-413
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 408-413
    • Park, C.B.1    Kim, M.S.2    Kim, S.C.3
  • 34
    • 0034714386 scopus 로고    scopus 로고
    • Isolation and characterization of novel glycoproteins from fish epidermal mucus: Correlation between their pore-forming properties and their antibacterial activities
    • Ebran, N., Julien, S., Orange, N., Auperin, B. and Molle, G. (2000) Isolation and characterization of novel glycoproteins from fish epidermal mucus: Correlation between their pore-forming properties and their antibacterial activities. Biochim. Biophys. Acta 1467, 271-280
    • (2000) Biochim. Biophys. Acta , vol.1467 , pp. 271-280
    • Ebran, N.1    Julien, S.2    Orange, N.3    Auperin, B.4    Molle, G.5
  • 35
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park, C. B., Kim, H. S. and Kim, S. C. (1998) Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 244, 253-257
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 36
    • 0035853022 scopus 로고    scopus 로고
    • The antibacterial peptide pyrrhocoricin inhibits the ATPase actions ol DnaK and prevents chaperone-assisted protein folding
    • Kragol, G., Lovas, S., Varadi, G., Condie, B. A., Hoffmann, R. and Otvos, Jr, L. (2001) The antibacterial peptide pyrrhocoricin inhibits the ATPase actions ol DnaK and prevents chaperone-assisted protein folding. Biochemistry 40, 3016-3026
    • (2001) Biochemistry , vol.40 , pp. 3016-3026
    • Kragol, G.1    Lovas, S.2    Varadi, G.3    Condie, B.A.4    Hoffmann, R.5    Otvos L., Jr.6
  • 37
    • 0034713831 scopus 로고    scopus 로고
    • Action of antimicrobial peptides: Two-state model
    • Huang, H. W. (2000) Action of antimicrobial peptides: Two-state model. Biochemistry 39, 8347-8352
    • (2000) Biochemistry , vol.39 , pp. 8347-8352
    • Huang, H.W.1
  • 38
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and non-selective membrane-lytic peptides
    • Shai, Y. (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462, 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 39
    • 0032956513 scopus 로고    scopus 로고
    • Pore-forming properties and antibacterial activity of proteins extracted from epidermal mucus of fish
    • Ebran, N., Julien, S., Orange, N., Saglio, P., Lemaitre, C. and Molle, G. (1999) Pore-forming properties and antibacterial activity of proteins extracted from epidermal mucus of fish. Comp. Biochem. Physiol. A 122, 181-189
    • (1999) Comp. Biochem. Physiol. A , vol.122 , pp. 181-189
    • Ebran, N.1    Julien, S.2    Orange, N.3    Saglio, P.4    Lemaitre, C.5    Molle, G.6
  • 41
    • 0030757152 scopus 로고    scopus 로고
    • Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analogue
    • Matsuzaki, K., Yoneyama, S., Fujii, N., Miyajima, K., Yamada, K.-I., Kirino, Y. and Anzai, K. (1997) Membrane permeabilization mechanisms of a cyclic antimicrobial peptide, tachyplesin I, and its linear analogue. Biochemistry 36, 9799-9806
    • (1997) Biochemistry , vol.36 , pp. 9799-9806
    • Matsuzaki, K.1    Yoneyama, S.2    Fujii, N.3    Miyajima, K.4    Yamada, K.-I.5    Kirino, Y.6    Anzai, K.7
  • 42
    • 0033198883 scopus 로고    scopus 로고
    • Purification and characterization of a cysteine-rich 11.5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas
    • Relf, J. M., Chisholm, J. R. S., Kemp, G. D. and Smith, V. J. (1999) Purification and characterization of a cysteine-rich 11.5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas. Eur. J. Biochem. 264, 350-357
    • (1999) Eur. J. Biochem. , vol.264 , pp. 350-357
    • Relf, J.M.1    Chisholm, J.R.S.2    Kemp, G.D.3    Smith, V.J.4
  • 43
    • 0035745998 scopus 로고    scopus 로고
    • Functional mapping of ultraviolet photosensitivity during metamorphic transitions in a salmonid fish, Oncorhynchus mykiss
    • Deutschlander, M. E., Greaves, D. K., Haimberger, T. J. and Hawryshyn, C. W. (2001) Functional mapping of ultraviolet photosensitivity during metamorphic transitions in a salmonid fish, Oncorhynchus mykiss. J. Exp. Biol. 204, 2401-2413
    • (2001) J. Exp. Biol. , vol.204 , pp. 2401-2413
    • Deutschlander, M.E.1    Greaves, D.K.2    Haimberger, T.J.3    Hawryshyn, C.W.4
  • 44
    • 0021101252 scopus 로고
    • The primary structure and expression of four cloned human histone genes
    • Zhong, R., Roeder, R. G. and Heintz, N. (1983) The primary structure and expression of four cloned human histone genes. Nucleic Acids Res. 11, 7409-7425
    • (1983) Nucleic Acids Res. , vol.11 , pp. 7409-7425
    • Zhong, R.1    Roeder, R.G.2    Heintz, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.