메뉴 건너뛰기




Volumn 237, Issue 1, 1996, Pages 86-92

Biochemical and antibacterial analysis of human wound and blister fluid

Author keywords

Autoimmune disorders; Defensins; FALL 39; Lysozyme; Thymosin

Indexed keywords

DEFENSIN; LYSOZYME;

EID: 0029971227     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0086n.x     Document Type: Article
Times cited : (197)

References (28)
  • 1
    • 0028906062 scopus 로고
    • Pharmacologic enhancement of wound healing
    • Pierce, G. F. & Mustoe, T. A. (1995) Pharmacologic enhancement of wound healing, Annu. Rev. Med. 46, 467-481.
    • (1995) Annu. Rev. Med. , vol.46 , pp. 467-481
    • Pierce, G.F.1    Mustoe, T.A.2
  • 2
    • 0027990415 scopus 로고
    • Wound repair in the context of extracellular matrix
    • Gailit, J. & Clark, R. A. F. (1994) Wound repair in the context of extracellular matrix, Curr. Opin. Cell Biol. 6, 717-725.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 717-725
    • Gailit, J.1    Clark, R.A.F.2
  • 3
    • 0027399332 scopus 로고
    • The skin immune system: Progress in cutaneous biology
    • Bos, J. D. & Kapsenberg, M. L. (1993) The skin immune system: progress in cutaneous biology, Immunol. Today 14, 75-78.
    • (1993) Immunol. Today , vol.14 , pp. 75-78
    • Bos, J.D.1    Kapsenberg, M.L.2
  • 5
    • 0026349223 scopus 로고
    • Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides
    • Agerberth, B., Lee, J.-Y., Bergman, T., Carlquist, M., Boman, H. G., Mutt, V. & Jörnvall, H. (1991) Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides, Eur. J. Biochem. 202, 849-854.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 849-854
    • Agerberth, B.1    Lee, J.-Y.2    Bergman, T.3    Carlquist, M.4    Boman, H.G.5    Mutt, V.6    Jörnvall, H.7
  • 6
    • 0028092047 scopus 로고
    • Syndecans, cell surface heparan sulfate proteoglycans, are induced by a prolin-rich antimicrobial peptide from wounds
    • Gallo, R. L., Ono, M., Povsic, T., Page, C., Eriksson, E., Klagsbrun, M. & Bernfield, M. (1994) Syndecans, cell surface heparan sulfate proteoglycans, are induced by a prolin-rich antimicrobial peptide from wounds, Proc. Natl Acad. Sci. USA 91, 11035-11039.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11035-11039
    • Gallo, R.L.1    Ono, M.2    Povsic, T.3    Page, C.4    Eriksson, E.5    Klagsbrun, M.6    Bernfield, M.7
  • 7
  • 8
    • 0027932950 scopus 로고
    • Internal amino acid sequences via in situ cyanogen bromide cleavage
    • Bergman, T. (1994) Internal amino acid sequences via in situ cyanogen bromide cleavage, J. Protein Chem. 13, 456-457.
    • (1994) J. Protein Chem. , vol.13 , pp. 456-457
    • Bergman, T.1
  • 9
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. & Jagow, G. V. (1987) Tricine-sodium dodecyl sulfate-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    Jagow, G.V.2
  • 10
    • 0019551730 scopus 로고
    • Western blotting: Electrophoretic transfer of proteins from sodium dodecyl sulphate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, V. N. (1981) Western blotting: electrophoretic transfer of proteins from sodium dodecyl sulphate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A, Anal. Biochem. 112, 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, V.N.1
  • 12
    • 0020686109 scopus 로고
    • Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia
    • Hultmark, D., Engström, Å., Andersson, K., Steiner, H., Bennich, H. & Boman, H. G. (1983) Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia, EMBO J. 2, 571-576.
    • (1983) EMBO J. , vol.2 , pp. 571-576
    • Hultmark, D.1    Engström, Å.2    Andersson, K.3    Steiner, H.4    Bennich, H.5    Boman, H.G.6
  • 13
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: Partial purification and some properties
    • Vogel, H. J. & Bonner, D. M. (1956) Acetylornithinase of Escherichia coli: partial purification and some properties, J. Biol. Chem. 218, 97-106.
    • (1956) J. Biol. Chem. , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 14
    • 0029007198 scopus 로고
    • hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules
    • Cowland, J. B., Johnsen, A. H. & Borregaard, N. (1995) hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules, FEBS Lett. 368, 173-176.
    • (1995) FEBS Lett. , vol.368 , pp. 173-176
    • Cowland, J.B.1    Johnsen, A.H.2    Borregaard, N.3
  • 15
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman, H. G. (1995) Peptide antibiotics and their role in innate immunity, Annu. Rev. Immun. 13, 61-92.
    • (1995) Annu. Rev. Immun. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 17
    • 0028453839 scopus 로고
    • Actin assembly in response to extracellular signals: Role of capping proteins, thymosin β-4 and profilin
    • Carlier, M.-F. & Pantaloni, D. (1994) Actin assembly in response to extracellular signals: role of capping proteins, thymosin β-4 and profilin, Semin. Cell Biol. 5, 183-191.
    • (1994) Semin. Cell Biol. , vol.5 , pp. 183-191
    • Carlier, M.-F.1    Pantaloni, D.2
  • 18
    • 0028964136 scopus 로고
    • Defensins in granules and non-phagocytic cells
    • Selsted, M. E. & Ouellette, A. J. (1995) Defensins in granules and non-phagocytic cells, Trends Cell Biol. 5, 114-119.
    • (1995) Trends Cell Biol. , vol.5 , pp. 114-119
    • Selsted, M.E.1    Ouellette, A.J.2
  • 19
    • 0029892512 scopus 로고    scopus 로고
    • Current concepts about neutrophil granule physiology
    • Borregard, N. (1996) Current concepts about neutrophil granule physiology, Curr. Opin. Hematol. 3, 11-18.
    • (1996) Curr. Opin. Hematol. , vol.3 , pp. 11-18
    • Borregard, N.1
  • 20
    • 0028718634 scopus 로고
    • Bactericidal permeability-increasing protein in host defence against Gram-negative bacteria and endotoxin
    • Elsbach, P. (1994) Bactericidal permeability-increasing protein in host defence against Gram-negative bacteria and endotoxin, Ciba Symp. 186, 176-189.
    • (1994) Ciba Symp. , vol.186 , pp. 176-189
    • Elsbach, P.1
  • 21
    • 0021767932 scopus 로고
    • The antibacterial effect of attacins from the silk moth Hyalophora cecropia is directed against the outer membrane of Escherichia coli
    • Engström, P., Carlsson, A., Engström, Å., Tao, Z.-j. & Bennich, H. (1984) The antibacterial effect of attacins from the silk moth Hyalophora cecropia is directed against the outer membrane of Escherichia coli, EMBO J. 3, 3347-3351.
    • (1984) EMBO J. , vol.3 , pp. 3347-3351
    • Engström, P.1    Carlsson, A.2    Engström, Å.3    Tao, Z.-J.4    Bennich, H.5
  • 23
    • 9244253417 scopus 로고
    • Antibacterial activity of human neutrophil defensins: Modulation factors
    • Lehrer, R. I., Szklarek, D., Ganz, T. & Selsted, M. E. (1994) Antibacterial activity of human neutrophil defensins: modulation factors, J. Clin. Invest. 93, 553-561.
    • (1994) J. Clin. Invest. , vol.93 , pp. 553-561
    • Lehrer, R.I.1    Szklarek, D.2    Ganz, T.3    Selsted, M.E.4
  • 25
    • 0002369211 scopus 로고
    • Autoimmunity and autoimmune diseases
    • (Paul, W. E., ed.) 3rd edn, Raven Press, New York
    • Schwartz, R. S. (1993)Autoimmunity and autoimmune diseases, Fundamental immunology (Paul, W. E., ed.) 3rd edn, pp. 1082-1083, Raven Press, New York.
    • (1993) Fundamental Immunology , pp. 1082-1083
    • Schwartz, R.S.1
  • 26
    • 0028973014 scopus 로고
    • 1-Antitrypsin is degraded and non-functional in chronic wounds but intact and functional in acute wounds: The inhibitor protects fibronectin from degradation by chronic wound fluid enzymes
    • 1-Antitrypsin is degraded and non-functional in chronic wounds but intact and functional in acute wounds: The inhibitor protects fibronectin from degradation by chronic wound fluid enzymes, J. Invest. Dermatol. 105, 572-577.
    • (1995) J. Invest. Dermatol. , vol.105 , pp. 572-577
    • Rao, C.N.1    Ladin, D.A.2    Liu, Y.Y.3    Chilikuri, K.4    Hou, Z.Z.5    Woodley, D.T.6
  • 28
    • 0028344132 scopus 로고
    • 92-kD Gelatinase is produced by eosinophils at the site of the blister formation in Bullous pemphigoid and cleaves the extracellular domain of recombinant 180-kD Bullous pemphigoid autoantigen
    • Ståhle-Bäckdahl, M., Inoue, M., Giudice, G. J. & Parks, W. C. (1994) 92-kD Gelatinase is produced by eosinophils at the site of the blister formation in Bullous pemphigoid and cleaves the extracellular domain of recombinant 180-kD Bullous pemphigoid autoantigen, J. Clin. Invest. 93, 2022-2030.
    • (1994) J. Clin. Invest. , vol.93 , pp. 2022-2030
    • Ståhle-Bäckdahl, M.1    Inoue, M.2    Giudice, G.J.3    Parks, W.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.