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Volumn 56, Issue 1-2, 1999, Pages 174-178

Spleen antibacterial peptides: High levels of PR-39 and presence of two forms of NK-lysin

Author keywords

Antibacterial peptide; C terminal ladder sequence analysis; Carboxypeptidase P; Carboxypeptidase Y; MALDI mass spectrometry; NK lysin; PR 39

Indexed keywords

ACETIC ACID; AMIDE; ANTIINFECTIVE AGENT; ARGININE; CARBOXYPEPTIDASE C; PEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT; PROLINE; PROLINE CARBOXYPEPTIDASE;

EID: 0033214531     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050016     Document Type: Article
Times cited : (12)

References (23)
  • 1
    • 0026511839 scopus 로고
    • Antibiotic peptides as mediators of innate immunity
    • Zasloff M. (1992) Antibiotic peptides as mediators of innate immunity. Curr. Opin. Immunol. 4: 3-7
    • (1992) Curr. Opin. Immunol. , vol.4 , pp. 3-7
    • Zasloff, M.1
  • 3
    • 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. Immunol. 13: 61-92
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 4
    • 0031821708 scopus 로고    scopus 로고
    • Gene-encoded peptide antibiotics and the concept of innate immunity: Un update review
    • Boman H. G. (1998) Gene-encoded peptide antibiotics and the concept of innate immunity: un update review. Scand. J. Immunol. 48: 15-25
    • (1998) Scand. J. Immunol. , vol.48 , pp. 15-25
    • Boman, H.G.1
  • 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. et al. (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
  • 6
    • 0028092047 scopus 로고
    • Syndeeans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds
    • Gallo R. L., Ono M., Povsic T., Page C., Eriksson E., Klagsbrun M. et al. (1994) Syndeeans, cell surface heparan sulfate proteoglycans, are induced by a proline-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
  • 7
    • 0029061894 scopus 로고
    • NK-lysin, a novel effector peptide of cytotoxic T and NK cells: Structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity
    • Andersson M., Gunne H., Agerberth B., Boman A., Bergman T., Sillard R. et al. (1995) NK-lysin, a novel effector peptide of cytotoxic T and NK cells: structure and cDNA cloning of the porcine form, induction by interleukin 2, antibacterial and antitumour activity. EMBO J. 14: 1615-1625
    • (1995) EMBO J. , vol.14 , pp. 1615-1625
    • Andersson, M.1    Gunne, H.2    Agerberth, B.3    Boman, A.4    Bergman, T.5    Sillard, R.6
  • 8
    • 0031107212 scopus 로고    scopus 로고
    • C-terminal sequence analysis of peptides and proteins using carboxypeptidases and mass spectrometry after derivatization of Lys and Cys residues
    • Bonetto V., Bergman A.-C., Jörnvall H. and Sillard R. (1997) C-terminal sequence analysis of peptides and proteins using carboxypeptidases and mass spectrometry after derivatization of Lys and Cys residues. Anal. Chem. 69: 1315-1319
    • (1997) Anal. Chem. , vol.69 , pp. 1315-1319
    • Bonetto, V.1    Bergman, A.-C.2    Jörnvall, H.3    Sillard, R.4
  • 9
    • 0002931796 scopus 로고    scopus 로고
    • Serine carboxypeptidases: A review
    • Breddam K. (1986) Serine carboxypeptidases: a review. Carlsberg Res. Commun. 51: 83-128 peptides and proteins degraded by carboxypeptidase Y and P. FFBS Lett. 357: 65-69
    • (1986) Carlsberg Res. Commun. , vol.51 , pp. 83-128
    • Breddam, K.1
  • 10
    • 0002931796 scopus 로고    scopus 로고
    • Breddam K. (1986) Serine carboxypeptidases: a review. Carlsberg Res. Commun. 51: 83-128 peptides and proteins degraded by carboxypeptidase Y and P. FFBS Lett. 357: 65-69
    • FFBS Lett. , vol.357 , pp. 65-69
  • 11
    • 0028921824 scopus 로고
    • Simplified high-sensitivity sequencing of a major histocompatibility complex class I-associated immunoreactive peptide using matrix-assisted laser desorption/ionization mass spectrometry
    • Woods A. S., Huang A. Y., Cotter R. J., Pasternack G. R., Pardoll D. M. and Jaffee E. M. (1995) Simplified high-sensitivity sequencing of a major histocompatibility complex class I-associated immunoreactive peptide using matrix-assisted laser desorption/ionization mass spectrometry. Anal. Biochem. 226: 15-25
    • (1995) Anal. Biochem. , vol.226 , pp. 15-25
    • Woods, A.S.1    Huang, A.Y.2    Cotter, R.J.3    Pasternack, G.R.4    Pardoll, D.M.5    Jaffee, E.M.6
  • 12
    • 0029558178 scopus 로고
    • Two alternative processing pathways for a preprohormone: A new bioactive form of secretin
    • Bonetto V., Jörnvall H., Mutt V. and Sillard R. (1995) Two alternative processing pathways for a preprohormone: a new bioactive form of secretin. Proc. Natl. Acad. Sci. USA 92: 11985-11989
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11985-11989
    • Bonetto, V.1    Jörnvall, H.2    Mutt, V.3    Sillard, R.4
  • 13
    • 0020686109 scopus 로고
    • Insect immunity: Attacins a family of antibacterial proteins from Hyalophora cecropia
    • Hultmark D., Engström A., Andersson K., Steiner H., Bennich H. and 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, A.2    Andersson, K.3    Steiner, H.4    Bennich, H.5    Boman, H.G.6
  • 15
    • 0027169823 scopus 로고
    • Protegrins: Leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins
    • Kokryakov V. N., Harwig S. S., Panyutich F. A., Shevchenko A. A., Aleshina G. M., Shamova O. V. et al. (1993) Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett. 327: 231-236
    • (1993) FEBS Lett. , vol.327 , pp. 231-236
    • Kokryakov, V.N.1    Harwig, S.S.2    Panyutich, F.A.3    Shevchenko, A.A.4    Aleshina, G.M.5    Shamova, O.V.6
  • 16
    • 0028930261 scopus 로고
    • Prophenin-l, an exceptionally proline-rich antimicrobial peptide from porcine leukocytes
    • Harwig S. S., Kokryakov V. N., Swiderek K. M., Aleshina G. M., Zhao C. and Lehrer R. I. (1995) Prophenin-l, an exceptionally proline-rich antimicrobial peptide from porcine leukocytes. FEBS Lett. 362: 65-69
    • (1995) FEBS Lett. , vol.362 , pp. 65-69
    • Harwig, S.S.1    Kokryakov, V.N.2    Swiderek, K.M.3    Aleshina, G.M.4    Zhao, C.5    Lehrer, R.I.6
  • 17
    • 0031686776 scopus 로고    scopus 로고
    • Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils
    • Turner J., Cho Y., Dinh N.-N., Waring A. J. and Lehrer R. I. (1998) Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob. Agents Chemother. 42: 2206-2214
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 2206-2214
    • Turner, J.1    Cho, Y.2    Dinh, N.-N.3    Waring, A.J.4    Lehrer, R.I.5
  • 18
    • 0032892736 scopus 로고    scopus 로고
    • Cathelicidin gene expression in porcine tissues: Roles in ontogeny and tissue specificity
    • Wu H., Zhang G., Ross C. R. and Blecha F. (1999) Cathelicidin gene expression in porcine tissues: roles in ontogeny and tissue specificity. Infect. Immun. 67: 439-442
    • (1999) Infect. Immun. , vol.67 , pp. 439-442
    • Wu, H.1    Zhang, G.2    Ross, C.R.3    Blecha, F.4
  • 19
    • 0030976983 scopus 로고    scopus 로고
    • Chemoattractant properties of PR-39, a neutrophil antibacterial peptide
    • Huang H. J., Ross C. R. and Blecha F. (1997) Chemoattractant properties of PR-39, a neutrophil antibacterial peptide. J. Leukoc. Biol. 61: 624-629
    • (1997) J. Leukoc. Biol. , vol.61 , pp. 624-629
    • Huang, H.J.1    Ross, C.R.2    Blecha, F.3
  • 20
    • 0028585933 scopus 로고
    • Identification of a proline-arginine-rich antibacterial peptide from neutrophils that is analogous to PR-39, an antibacterial peptide from the small intestine
    • Shi J., Ross C. R., Chengappa M. M. and Blecha F. (1994) Identification of a proline-arginine-rich antibacterial peptide from neutrophils that is analogous to PR-39, an antibacterial peptide from the small intestine. J. Leukoc. Biol. 56: 807-811
    • (1994) J. Leukoc. Biol. , vol.56 , pp. 807-811
    • Shi, J.1    Ross, C.R.2    Chengappa, M.M.3    Blecha, F.4
  • 21
    • 0028908524 scopus 로고
    • An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B
    • Andersson M., Curstedt T., Jörnvall H. and Johansson J. (1995) An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B. FEBS Lett. 362: 328-332
    • (1995) FEBS Lett. , vol.362 , pp. 328-332
    • Andersson, M.1    Curstedt, T.2    Jörnvall, H.3    Johansson, J.4
  • 22
    • 0028073698 scopus 로고
    • Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeha histolytica: Isolation, primary structure, and pore formation in bacterial cytoplasmic membranes
    • Leippe M., Andrä J., Nickel R., Tannich E. and Müller-Eberhard H. J. (1994) Amoebapores, a family of membranolytic peptides from cytoplasmic granules of Entamoeha histolytica: isolation, primary structure, and pore formation in bacterial cytoplasmic membranes. Mol. Microbiol. 14: 895-904
    • (1994) Mol. Microbiol. , vol.14 , pp. 895-904
    • Leippe, M.1    Andrä, J.2    Nickel, R.3    Tannich, E.4    Müller-Eberhard, H.J.5
  • 23
    • 0345291179 scopus 로고    scopus 로고
    • Amoebapore homologs of Caenorhabditis elegans
    • Banyai L. and Patthy L. (1998) Amoebapore homologs of Caenorhabditis elegans. Biochim. Biophys. Acta 1429: 259-264
    • (1998) Biochim. Biophys. Acta , vol.1429 , pp. 259-264
    • Banyai, L.1    Patthy, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.