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Volumn 13, Issue 6, 1997, Pages 494-499

Enteric defensins

Author keywords

[No Author keywords available]

Indexed keywords

DEFENSIN; PEPTIDE;

EID: 0030730524     PISSN: 02671379     EISSN: None     Source Type: Journal    
DOI: 10.1097/00001574-199711000-00010     Document Type: Short Survey
Times cited : (4)

References (71)
  • 1
    • 0004210742 scopus 로고
    • Opening remarks
    • Edited by Marsh J, Goode JA. Chichester: John Wiley & Sons Ltd.
    • Boman HG: Opening remarks. In Antimicrobial Peptides. Edited by Marsh J, Goode JA. Chichester: John Wiley & Sons Ltd.; 1994:1-4.
    • (1994) Antimicrobial Peptides , pp. 1-4
    • Boman, H.G.1
  • 2
    • 0025818448 scopus 로고
    • Antibacterial peptides: Key components needed in immunity
    • Boman HG: Antibacterial peptides: key components needed in immunity. Cell 1991, 65:205-207.
    • (1991) Cell , vol.65 , pp. 205-207
    • Boman, H.G.1
  • 3
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman HG: Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 1995, 13:61-92.
    • (1995) Annu Rev Immunol , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 4
    • 0029097115 scopus 로고
    • Structure, function, and membrane integration of defensins
    • White SH, Wimley WC, Selsted ME: Structure, function, and membrane integration of defensins. Curr Opin Struct Biol 1995, 5:521-527.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 521-527
    • White, S.H.1    Wimley, W.C.2    Selsted, M.E.3
  • 5
    • 0028964136 scopus 로고
    • Defensins in granules of phagocytic and non-phagocytic cells
    • Selsted ME, Ouellette AJ: Defensins in granules of phagocytic and non-phagocytic cells. Trends in Cell Biology 1995, 5:114-119.
    • (1995) Trends in Cell Biology , vol.5 , pp. 114-119
    • Selsted, M.E.1    Ouellette, A.J.2
  • 7
    • 0029051685 scopus 로고
    • Defensins and other endogenous peptide antibiotics of vertebrates
    • Martin E, Ganz T, Lehrer RI: Defensins and other endogenous peptide antibiotics of vertebrates. J Leukoc Biol 1995, 58:128-136.
    • (1995) J Leukoc Biol , vol.58 , pp. 128-136
    • Martin, E.1    Ganz, T.2    Lehrer, R.I.3
  • 9
    • 0020562530 scopus 로고
    • Antibacterial activity of microbicidal cationic proteins 1 and 2, natural peptide antibiotics of rabbit lung macrophages
    • Lehrer RI, Selsted ME, Szklarek D, Fleischmann J: Antibacterial activity of microbicidal cationic proteins 1 and 2, natural peptide antibiotics of rabbit lung macrophages. Infect Immun 1983, 42:10-14.
    • (1983) Infect Immun , vol.42 , pp. 10-14
    • Lehrer, R.I.1    Selsted, M.E.2    Szklarek, D.3    Fleischmann, J.4
  • 10
    • 0021032178 scopus 로고
    • Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages
    • Selsted ME, Brown DM, Delange RJ, Lehrer RI: Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages. J Biol Chem 1983, 258:14485-14489.
    • (1983) J Biol Chem , vol.258 , pp. 14485-14489
    • Selsted, M.E.1    Brown, D.M.2    Delange, R.J.3    Lehrer, R.I.4
  • 11
    • 0025959114 scopus 로고
    • Defensins: Endogenous antibiotic peptides of animal cells
    • Lehrer RI, Ganz T, Selsted ME: Defensins: endogenous antibiotic peptides of animal cells. Cell 1991, 64:229-230.
    • (1991) Cell , vol.64 , pp. 229-230
    • Lehrer, R.I.1    Ganz, T.2    Selsted, M.E.3
  • 13
    • 0029819784 scopus 로고    scopus 로고
    • Paneth cell defensins: Endogenous peptide components of intestinal host defense
    • Ouellette AJ, Selsted ME: Paneth cell defensins: endogenous peptide components of intestinal host defense. FASEB J 1996, 10:1280-1289.
    • (1996) FASEB J , vol.10 , pp. 1280-1289
    • Ouellette, A.J.1    Selsted, M.E.2
  • 14
    • 0030778218 scopus 로고    scopus 로고
    • Antimicrobial protection of the testis: Secretion of defensins of the cryptdin family
    • in press
    • Grandjean V, Vincent S, Martin L, Rassoulzadegan M, Cuzin F: Antimicrobial protection of the testis: secretion of defensins of the cryptdin family. Biol Reprod 1997, in press. The authors demonstrate that Paneth cell α-defensins are present in Sertoli cells and Leydig cells of the mouse testis. Studies in 15P-1 cells, a mouse Sertoli cell line, showed that α-defensin expression was inducible both by coculture with germ cells and by administration of nerve growth factor.
    • (1997) Biol Reprod
    • Grandjean, V.1    Vincent, S.2    Martin, L.3    Rassoulzadegan, M.4    Cuzin, F.5
  • 15
    • 0031028671 scopus 로고    scopus 로고
    • Detection of human defensin 5 in reproductive tissues
    • Svinarich DM, Wolf NA, Gomez R, Gonik B, Romero R: Detection of human defensin 5 in reproductive tissues. Am J Obstet Gynecol 1997, 176:470-475. This study shows that transcripts corresponding to human Paneth cell α-defensin HD-5 are detectable in endocervix, endometrium, chorion, and a cell line derived from endometrium. DNA sequence analysis of cloned amplified sequences identified potential allelic variants of HD-5.
    • (1997) Am J Obstet Gynecol , vol.176 , pp. 470-475
    • Svinarich, D.M.1    Wolf, N.A.2    Gomez, R.3    Gonik, B.4    Romero, R.5
  • 16
    • 0028902757 scopus 로고
    • Epithelial antibiotics induced at sites of inflammation
    • Schonwetter BS, Stolzenberg ED, Zasloff MA: Epithelial antibiotics induced at sites of inflammation. Science 1995, 267:1645-1648.
    • (1995) Science , vol.267 , pp. 1645-1648
    • Schonwetter, B.S.1    Stolzenberg, E.D.2    Zasloff, M.A.3
  • 17
    • 0025811874 scopus 로고
    • Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: Peptide isolation and cloning of a cDNA
    • Diamond G, Zasloff M, Eck H, Brasseur M, Maloy WL, Bevins CL: Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA. Proc Natl Acad Sci U S A 1991, 88:3952-3956.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3952-3956
    • Diamond, G.1    Zasloff, M.2    Eck, H.3    Brasseur, M.4    Maloy, W.L.5    Bevins, C.L.6
  • 18
    • 0027514011 scopus 로고
    • Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils
    • Selsted ME, Tang YQ, Morris WL, McGuire PA, Novotny MJ, Smith W, Henschen AH, Cullor JS. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. J Biol Chem 1993, 268:6641-6648.
    • (1993) J Biol Chem , vol.268 , pp. 6641-6648
    • Selsted, M.E.1    Tang, Y.Q.2    Morris, W.L.3    McGuire, P.A.4    Novotny, M.J.5    Smith, W.6    Henschen, A.H.7    Cullor, J.S.8
  • 20
    • 0030569343 scopus 로고    scopus 로고
    • Widespread expression of beta-defensin hBD-1 in human secretory glands and epithelial cells
    • Zhao CQ, Wang I, Lehrer RI: Widespread expression of beta-defensin hBD-1 in human secretory glands and epithelial cells. FEBS Lett 1996, 396:319-322.
    • (1996) FEBS Lett , vol.396 , pp. 319-322
    • Zhao, C.Q.1    Wang, I.2    Lehrer, R.I.3
  • 22
    • 0030949875 scopus 로고    scopus 로고
    • Human β-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis
    • Goldman MJ, Anderson GM, Stolzenberg ED, Kari UP, Zasloff M, Wilson JM: Human β-defensin-1 is a salt-sensitive antibiotic in lung that is inactivated in cystic fibrosis. Cell 1997, 88:553-560.
    • (1997) Cell , vol.88 , pp. 553-560
    • Goldman, M.J.1    Anderson, G.M.2    Stolzenberg, E.D.3    Kari, U.P.4    Zasloff, M.5    Wilson, J.M.6
  • 23
    • 0028825285 scopus 로고
    • Solution structure of bovine neutrophil β-defensin-12: The peptide fold of the β-defensins is identical to that of the classical defensins
    • Zimmermann GR, Legault P, Selsted ME. Pardi A: Solution structure of bovine neutrophil β-defensin-12: the peptide fold of the β-defensins is identical to that of the classical defensins. Biochemistry 1995, 34:13663-13671.
    • (1995) Biochemistry , vol.34 , pp. 13663-13671
    • Zimmermann, G.R.1    Legault, P.2    Selsted, M.E.3    Pardi, A.4
  • 24
    • 0027981211 scopus 로고
    • Structure and dynamics of the neutrophil defensins NP-2, NP-5, and HNP-1: NMR studies of amide hydrogen exchange kinetics
    • Skalicky JJ, Selsted ME, Pardi A: Structure and dynamics of the neutrophil defensins NP-2, NP-5, and HNP-1: NMR studies of amide hydrogen exchange kinetics. Proteins 1994, 20:52-67.
    • (1994) Proteins , vol.20 , pp. 52-67
    • Skalicky, J.J.1    Selsted, M.E.2    Pardi, A.3
  • 25
    • 0026468973 scopus 로고
    • NMR studies of defensin antimicrobial peptides: 2. Three-dimensional structures of rabbit NP-2 and human HNP-1
    • Pardi A, Zhang XL, Selsted ME, Skalicky JJ, Yip PF: NMR studies of defensin antimicrobial peptides: 2. Three-dimensional structures of rabbit NP-2 and human HNP-1. Biochemistry 1992, 31:11357-11364.
    • (1992) Biochemistry , vol.31 , pp. 11357-11364
    • Pardi, A.1    Zhang, X.L.2    Selsted, M.E.3    Skalicky, J.J.4    Yip, P.F.5
  • 26
    • 0026490907 scopus 로고
    • NMR studies of defensin antimicrobial peptides: 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1
    • Zhang XL, Selsted ME, Pardi A: NMR studies of defensin antimicrobial peptides: 1. Resonance assignment and secondary structure determination of rabbit NP-2 and human HNP-1. Biochemistry 1992, 31:11348-11356.
    • (1992) Biochemistry , vol.31 , pp. 11348-11356
    • Zhang, X.L.1    Selsted, M.E.2    Pardi, A.3
  • 27
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: Evidence for formation of multimeric pores
    • Wimley WC, Selsted ME, White SH: Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores. Protein Science 1994, 3:1362-1373.
    • (1994) Protein Science , vol.3 , pp. 1362-1373
    • Wimley, W.C.1    Selsted, M.E.2    White, S.H.3
  • 28
    • 0029811094 scopus 로고    scopus 로고
    • Interactions of monomeric rabbit neutrophil defensins with bilayers: Comparison with dimeric human defensin HNP-2
    • Hristova K, Selsted ME, White SH: Interactions of monomeric rabbit neutrophil defensins with bilayers: comparison with dimeric human defensin HNP-2. Biochemistry 1996, 35:11888-11894. In these experiments on model membranes, rabbit neutrophil α-defensin NP-1, a monomeric peptide, was shown to permeabilize the membrane by generating large, transient defects in phospholipid bilayers. The mechanism is in contrast to that of dimeric HNP-2, which induces the formation of large, stable multimeric pores.
    • (1996) Biochemistry , vol.35 , pp. 11888-11894
    • Hristova, K.1    Selsted, M.E.2    White, S.H.3
  • 29
    • 0016333713 scopus 로고
    • Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine: IV. Paneth cells
    • Cheng H: Origin, differentiation and renewal of the four main epithelial cell types in the mouse small intestine: IV. Paneth cells. Am J Anat 1974, 141:521-535.
    • (1974) Am J Anat , vol.141 , pp. 521-535
    • Cheng, H.1
  • 30
    • 0014634629 scopus 로고
    • Renewal of Paneth cells in the small intestine of the mouse
    • Cheng H, Merzel J, Leblond CP: Renewal of Paneth cells in the small intestine of the mouse. Am J Anat 1969, 126:507-525.
    • (1969) Am J Anat , vol.126 , pp. 507-525
    • Cheng, H.1    Merzel, J.2    Leblond, C.P.3
  • 31
    • 0016794772 scopus 로고
    • The Paneth cell: A source of intestinal lysozyme
    • Peeters T, Vantrappen G: The Paneth cell: a source of intestinal lysozyme. Gut 1975, 16:553-558.
    • (1975) Gut , vol.16 , pp. 553-558
    • Peeters, T.1    Vantrappen, G.2
  • 32
    • 0015749193 scopus 로고
    • Lysozyme in Paneth cell secretions
    • Geyer G: Lysozyme in Paneth cell secretions. Acta Histochemica 1973, 45:126-132.
    • (1973) Acta Histochemica , vol.45 , pp. 126-132
    • Geyer, G.1
  • 33
    • 0027372308 scopus 로고
    • Enhancing factor, a Paneth cell specific protein from mouse small intestines: Predicted amino acid sequence from RT-PCR amplified cDNA and its expression
    • Mulherkar R, Rao RS, Wagle AS, Patti V, Deo MG: Enhancing factor, a Paneth cell specific protein from mouse small intestines: predicted amino acid sequence from RT-PCR amplified cDNA and its expression. Biochem Biophys Res Comm 1993, 195:1254-1263.
    • (1993) Biochem Biophys Res Comm , vol.195 , pp. 1254-1263
    • Mulherkar, R.1    Rao, R.S.2    Wagle, A.S.3    Patti, V.4    Deo, M.G.5
  • 34
    • 0026660392 scopus 로고
    • Enteric defensins: Antibiotic peptide components of intestinal host defense
    • Selsted ME, Miller SI, Henschen AH, Ouellette AJ: Enteric defensins: antibiotic peptide components of intestinal host defense. J Cell Biol 1992, 118:929-936.
    • (1992) J Cell Biol , vol.118 , pp. 929-936
    • Selsted, M.E.1    Miller, S.I.2    Henschen, A.H.3    Ouellette, A.J.4
  • 35
    • 0030914439 scopus 로고    scopus 로고
    • Localization of human intestinal defensin 5 in Paneth cell granules
    • Porter EM, Liu L, Oren A, Anton PA, Ganz T: Localization of human intestinal defensin 5 in Paneth cell granules. Infect Immun 1997, 65:2389-2395. The authors produced a polyclonal anliserum to recombinant HD-5 expressed in an insect cell-baculovirus system. The antibody provided definitive evidence that human Paneth cell α-defensin HD-5 is a constituent of Paneth cell granules.
    • (1997) Infect Immun , vol.65 , pp. 2389-2395
    • Porter, E.M.1    Liu, L.2    Oren, A.3    Anton, P.A.4    Ganz, T.5
  • 36
    • 0028907433 scopus 로고
    • Carbamylcholine- and catecholamine-induced intracellular calcium dynamics of epithelial cells in mouse ileal crypts
    • Satoh Y, Habara Y, Ono K, Kanno T: Carbamylcholine- and catecholamine-induced intracellular calcium dynamics of epithelial cells in mouse ileal crypts. Gastroenterology 1995, 108:1345-1356.
    • (1995) Gastroenterology , vol.108 , pp. 1345-1356
    • Satoh, Y.1    Habara, Y.2    Ono, K.3    Kanno, T.4
  • 37
    • 0024414474 scopus 로고
    • Effects of cholecystokinin and carbamylcholine on Paneth cell secretion in mice: A comparison with pancreatic acinar cells
    • Satoh Y, Ishikawa K, Oomori Y, Yamano M, Ono K: Effects of cholecystokinin and carbamylcholine on Paneth cell secretion in mice: a comparison with pancreatic acinar cells. Anat Rec 1989, 225:124-132.
    • (1989) Anat Rec , vol.225 , pp. 124-132
    • Satoh, Y.1    Ishikawa, K.2    Oomori, Y.3    Yamano, M.4    Ono, K.5
  • 38
    • 0026638027 scopus 로고
    • Bethanechol and a G-protein activator, NaF/AlCl3, induce secretory response in Paneth cells of mouse intestine
    • Satoh Y, Ishikawa K, Oomori Y, Takeda S, Ono K: Bethanechol and a G-protein activator, NaF/AlCl3, induce secretory response in Paneth cells of mouse intestine. Cell Tiss Res 1992, 269:213-220.
    • (1992) Cell Tiss Res , vol.269 , pp. 213-220
    • Satoh, Y.1    Ishikawa, K.2    Oomori, Y.3    Takeda, S.4    Ono, K.5
  • 42
    • 0030029451 scopus 로고    scopus 로고
    • Human enteric defensins: Gene structure and developmental expression
    • Mallow EB, Harris A, Salzman N, Russell JP, Deberardinis RJ, Ruchelli E, Bevins CL: Human enteric defensins: gene structure and developmental expression. J Biol Chem 1996, 271:4038-4045. These studies demonstrate that human Paneth cell defensins can be detected as early as 13.5 weeks gestation in differentiating Paneth cells in the developing small intestine. In the fetus, the overall intestinal content of α-defensin messenger RNA is 40- to 250-fold lower than the adult level.
    • (1996) J Biol Chem , vol.271 , pp. 4038-4045
    • Mallow, E.B.1    Harris, A.2    Salzman, N.3    Russell, J.P.4    Deberardinis, R.J.5    Ruchelli, E.6    Bevins, C.L.7
  • 43
    • 0027390031 scopus 로고
    • Defensin-6 mRNA in human Paneth cells: Implications for antimicrobial peptides in host defense of the human bowel
    • Jones DE, Bevins CL: Defensin-6 mRNA in human Paneth cells: implications for antimicrobial peptides in host defense of the human bowel. FEBS Lett 1993, 315:187-192.
    • (1993) FEBS Lett , vol.315 , pp. 187-192
    • Jones, D.E.1    Bevins, C.L.2
  • 44
    • 0024521812 scopus 로고
    • Developmental regulation of cryptdin, a corticostatin/defensin precursor mRNA in mouse small intestinal crypt epithelium
    • Ouellette AJ, Greco RM, James M, Frederick D, Naftilan J, Fallon JT: Developmental regulation of cryptdin, a corticostatin/defensin precursor mRNA in mouse small intestinal crypt epithelium. J Cell Biol 1989, 108:1687-1695.
    • (1989) J Cell Biol , vol.108 , pp. 1687-1695
    • Ouellette, A.J.1    Greco, R.M.2    James, M.3    Frederick, D.4    Naftilan, J.5    Fallon, J.T.6
  • 45
    • 0031014756 scopus 로고    scopus 로고
    • Cryptdin gene expression in developing mouse small intestine
    • Darmoul D, Brown D, Selsted ME, Ouellette AJ: Cryptdin gene expression in developing mouse small intestine. Am J Physiol 1997, 272:G197-G206. These studies show that certain cryptdin genes are expressed in the differentiating intestinal epithelium prior to the appearance of recognizable Paneth cells. The peptide was detected by immunofluorescence in apparent cytoplasmic granules and on the surface of the intestinal mucosa.
    • (1997) Am J Physiol , vol.272
    • Darmoul, D.1    Brown, D.2    Selsted, M.E.3    Ouellette, A.J.4
  • 46
    • 0030027096 scopus 로고    scopus 로고
    • Human enteric defensin genes: Chromosomal map position and a model for possible evolutionary relationships
    • Bevins CL, Jones DE, Dutra A, Schaffzin J, Muenke M: Human enteric defensin genes: chromosomal map position and a model for possible evolutionary relationships. Genomics 1996, 31:95-106. The authors show that the human Paneth cell α-defensin genes map to the same cytogenetic region of chromosome 8 as the myeloid defensin genes. A model is presented for the evolutionary history of the human defensin gene family.
    • (1996) Genomics , vol.31 , pp. 95-106
    • Bevins, C.L.1    Jones, D.E.2    Dutra, A.3    Schaffzin, J.4    Muenke, M.5
  • 47
    • 0028195081 scopus 로고
    • Structure and diversity of the murine cryptdin gene family
    • Huttner KM, Selsted ME, Ouellette AJ: Structure and diversity of the murine cryptdin gene family. Genomics 1994, 19:448-453.
    • (1994) Genomics , vol.19 , pp. 448-453
    • Huttner, K.M.1    Selsted, M.E.2    Ouellette, A.J.3
  • 49
    • 0028898423 scopus 로고
    • The pro region of human neutrophil defensin contains a motif that is essential for normal subcellular sorting
    • Liu L, Ganz T: The pro region of human neutrophil defensin contains a motif that is essential for normal subcellular sorting. Blood 1995, 85:1095-1103.
    • (1995) Blood , vol.85 , pp. 1095-1103
    • Liu, L.1    Ganz, T.2
  • 50
    • 0026652575 scopus 로고
    • Cationic defensins arise from charge-neutralized propeptides: A mechanism for avoiding leukocyte autocytotoxicity?
    • Michaelson D, Rayner J, Couto M, Ganz T: Cationic defensins arise from charge-neutralized propeptides: a mechanism for avoiding leukocyte autocytotoxicity? J Leukoc Biol 1992, 51:634-639.
    • (1992) J Leukoc Biol , vol.51 , pp. 634-639
    • Michaelson, D.1    Rayner, J.2    Couto, M.3    Ganz, T.4
  • 51
    • 0026535104 scopus 로고
    • Posttranslational processing of defensins in immature human myeloid cells
    • Valore EV, Ganz T: Posttranslational processing of defensins in immature human myeloid cells. Blood 1992, 79:1538-1544.
    • (1992) Blood , vol.79 , pp. 1538-1544
    • Valore, E.V.1    Ganz, T.2
  • 52
    • 0029978338 scopus 로고    scopus 로고
    • Intramolecular inhibition of human defensin HNP-1 by its propiece
    • Valore EV, Martin E. Harwig SSL, Ganz T: Intramolecular inhibition of human defensin HNP-1 by its propiece. J Clin Invest 1996, 97:1624-1629. These studies show that the prosegment of the HNP-1 precursor is capable of inhibiting the antimicrobial and cell-permeabilizing activities of the HNP-1 peptide in a dose-dependent fashion. The findings suggest that prosegments may attenuate the cytotoxic effects of α-defensins during processing.
    • (1996) J Clin Invest , vol.97 , pp. 1624-1629
    • Valore, E.V.1    Martin, E.2    Harwig, S.S.L.3    Ganz, T.4
  • 53
    • 0026712324 scopus 로고
    • Cryptdins: Antimicrobial defensins of the murine small intestine
    • Eisenhauer PB, Harwig SS, Lehrer RI: Cryptdins: antimicrobial defensins of the murine small intestine. Infect Immun 1992, 60:3556-3565.
    • (1992) Infect Immun , vol.60 , pp. 3556-3565
    • Eisenhauer, P.B.1    Harwig, S.S.2    Lehrer, R.I.3
  • 54
    • 0027945728 scopus 로고
    • Killing of Giardia lamblia by cryptdins and cationic neutrophil peptides
    • Aley SB, Zimmerman M, Hetsko M, Selsted ME, Gillin FD: Killing of Giardia lamblia by cryptdins and cationic neutrophil peptides. Infect Immun 1994, 62:5397-5403.
    • (1994) Infect Immun , vol.62 , pp. 5397-5403
    • Aley, S.B.1    Zimmerman, M.2    Hetsko, M.3    Selsted, M.E.4    Gillin, F.D.5
  • 55
    • 0030913746 scopus 로고    scopus 로고
    • Broad-spectrum antimicrobial activity of human intestinal defensin 5
    • Porter EM, Van Dam E, Valore EV, Ganz T: Broad-spectrum antimicrobial activity of human intestinal defensin 5. Infect Immun 1997, 65:2396-2401. This study shows that a recombinant form of HD-5 has broad-spectrum antimicrobial activity, the first report of such measurements for human Paneth cell α-defensin peptides.
    • (1997) Infect Immun , vol.65 , pp. 2396-2401
    • Porter, E.M.1    Van Dam, E.2    Valore, E.V.3    Ganz, T.4
  • 57
    • 0026534359 scopus 로고
    • Structure of the guinea pig neutrophil cationic peptide gene
    • Nagaoka I, Someya A, Iwabuchi K, Yamashita T: Structure of the guinea pig neutrophil cationic peptide gene. FEBS Lett 1992, 303:31-35.
    • (1992) FEBS Lett , vol.303 , pp. 31-35
    • Nagaoka, I.1    Someya, A.2    Iwabuchi, K.3    Yamashita, T.4
  • 58
    • 0024396994 scopus 로고
    • The structure of the rabbit macrophage defensin genes and their organspecific expression
    • Ganz T, Rayner JR, Valore EV, Tumolo A, Talmadge K, Fuller F: The structure of the rabbit macrophage defensin genes and their organspecific expression. J Immunol 1989, 143:1358-1365.
    • (1989) J Immunol , vol.143 , pp. 1358-1365
    • Ganz, T.1    Rayner, J.R.2    Valore, E.V.3    Tumolo, A.4    Talmadge, K.5    Fuller, F.6
  • 60
    • 0028130174 scopus 로고
    • A family of defensin-like genes codes for diverse cysteine-rich peptides in mouse Paneth cells
    • Huttner KM, Ouellette AJ: A family of defensin-like genes codes for diverse cysteine-rich peptides in mouse Paneth cells. Genomics 1994, 24:99-109.
    • (1994) Genomics , vol.24 , pp. 99-109
    • Huttner, K.M.1    Ouellette, A.J.2
  • 61
    • 0027378632 scopus 로고
    • In vitro cDNA amplification from individual intestinal crypts: A novel approach to the study of differential gene expression along the cryptvillus axis
    • Cano-Gauci DF, Lualdi JC, Ouellette AJ, Brady G, Iscove NN, Buick RN: In vitro cDNA amplification from individual intestinal crypts: a novel approach to the study of differential gene expression along the cryptvillus axis. Exp Cell Res 1993, 208:344-349.
    • (1993) Exp Cell Res , vol.208 , pp. 344-349
    • Cano-Gauci, D.F.1    Lualdi, J.C.2    Ouellette, A.J.3    Brady, G.4    Iscove, N.N.5    Buick, R.N.6
  • 62
    • 0026457997 scopus 로고
    • Paneth cells of the human small intestine express an antimicrobial peptide gene
    • Jones DE, Bevins CL: Paneth cells of the human small intestine express an antimicrobial peptide gene. J Biol Chem 1992, 267:23216-23225.
    • (1992) J Biol Chem , vol.267 , pp. 23216-23225
    • Jones, D.E.1    Bevins, C.L.2
  • 63
    • 0029738094 scopus 로고    scopus 로고
    • Positional specificity of defensin gene expression reveals Paneth cell heterogeneity in mouse small intestine
    • Darmoul D, Ouellette AJ: Positional specificity of defensin gene expression reveals Paneth cell heterogeneity in mouse small intestine. Am J Physiol 1996, 271:G68-G74.
    • (1996) Am J Physiol , vol.271
    • Darmoul, D.1    Ouellette, A.J.2
  • 64
    • 0025281425 scopus 로고
    • A novel mouse gene family coding for cationic, cysteine-rcch peptides: Regulation in small intestine and cells of myeloid origin
    • Ouellette AJ, Lualdi JC: A novel mouse gene family coding for cationic, cysteine-rcch peptides: regulation in small intestine and cells of myeloid origin. J Biol Chem 1990, 265:9831-9837.
    • (1990) J Biol Chem , vol.265 , pp. 9831-9837
    • Ouellette, A.J.1    Lualdi, J.C.2
  • 65
    • 0028809672 scopus 로고
    • Ontogenic regulation of spatial differentiation in the crypt-villus axis of normal and isografted small intestine
    • Gutierrez ED, Grapperhaus KJ, Rubin DC: Ontogenic regulation of spatial differentiation in the crypt-villus axis of normal and isografted small intestine. Am J Physiol 1995, 269:G500-G511.
    • (1995) Am J Physiol , vol.269
    • Gutierrez, E.D.1    Grapperhaus, K.J.2    Rubin, D.C.3
  • 66
    • 0026764105 scopus 로고
    • Use of fetal intestinal isografts from normal and transgenic mice to study the programming of positional information along the duodenal-to-colonic axis
    • Rubin DC, Swietlicki E, Roth KA, Gordon JI: Use of fetal intestinal isografts from normal and transgenic mice to study the programming of positional information along the duodenal-to-colonic axis. J Biol Chem 1992, 267:15122-15133.
    • (1992) J Biol Chem , vol.267 , pp. 15122-15133
    • Rubin, D.C.1    Swietlicki, E.2    Roth, K.A.3    Gordon, J.I.4
  • 67
    • 0030739939 scopus 로고    scopus 로고
    • Induction of epithelial chloride secretion by channel forming cryptdins 2 and 3
    • Lencer WI, Cheung G, Strohmeier GR, Currie MG, Ouellette AJ, Selsted ME, Madara JL: Induction of epithelial chloride secretion by channel forming cryptdins 2 and 3. Proc Natl Acad Sci U S A 1997, 94:8585-8589. These experiments show that mouse cryptdins 2 and 3 are potent stimulators of chloride secretion when administered apically to cultured human T84 intestinal epithelial cells. The studies suggest that release of α-defensins may influence the biology of the crypt microenvironment in addition to contributing to innate immunity.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8585-8589
    • Lencer, W.I.1    Cheung, G.2    Strohmeier, G.R.3    Currie, M.G.4    Ouellette, A.J.5    Selsted, M.E.6    Madara, J.L.7
  • 68
    • 15844422471 scopus 로고    scopus 로고
    • The isolation and characterization of a novel corticostatin/defensin-like peptide from the kidney
    • Bateman A, Macleod RJ, Lembessis P, Hu J, Esch F, Solomon S: The isolation and characterization of a novel corticostatin/defensin-like peptide from the kidney. J Biol Chem 1996, 271:10654-10659
    • (1996) J Biol Chem , vol.271 , pp. 10654-10659
    • Bateman, A.1    Macleod, R.J.2    Lembessis, P.3    Hu, J.4    Esch, F.5    Solomon, S.6
  • 70
    • 0027549241 scopus 로고
    • Defensins reduce the barrier integrity of a cultured epithelial monolayer without cytotoxicity
    • Nygaard SD, Ganz T, Peterson MW: Defensins reduce the barrier integrity of a cultured epithelial monolayer without cytotoxicity. Am J Respir Cell Mol Biol 1993, 8:193-200.
    • (1993) Am J Respir Cell Mol Biol , vol.8 , pp. 193-200
    • Nygaard, S.D.1    Ganz, T.2    Peterson, M.W.3
  • 71
    • 0028331319 scopus 로고
    • Defensins: A family of antimicrobial and cytotoxic peptides
    • Kagan BL, Ganz T, Lehrer RI: Defensins: A family of antimicrobial and cytotoxic peptides. Toxicology 1994, 87:131-149.
    • (1994) Toxicology , vol.87 , pp. 131-149
    • Kagan, B.L.1    Ganz, T.2    Lehrer, R.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.