메뉴 건너뛰기




Volumn 77, Issue 4, 2005, Pages 439-443

Neutrophils and keratinocytes in innate immunity - Cooperative actions to provide antimicrobial defense at the right time and place

Author keywords

Antibiotic peptides; hCAP 18; NGAL

Indexed keywords

CATHELICIDIN; LIPOCALIN; NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN; PEPTIDE HCAP18; POLYPEPTIDE ANTIBIOTIC AGENT; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 16844363111     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1189/jlb.0704381     Document Type: Conference Paper
Times cited : (52)

References (75)
  • 1
    • 0037296467 scopus 로고    scopus 로고
    • Neutrophil abnormalities
    • Boxer, L. A. (2003) Neutrophil abnormalities. Pediatr. Rev. 24, 52-62.
    • (2003) Pediatr. Rev. , vol.24 , pp. 52-62
    • Boxer, L.A.1
  • 2
    • 0036390103 scopus 로고    scopus 로고
    • Clinical symptoms and neutropenia: The balance of neutrophil development, functional activity, and cell death
    • Kuijpers, T. W. (2002) Clinical symptoms and neutropenia: the balance of neutrophil development, functional activity, and cell death. Eur. J. Pediatr. 161 (Suppl. 1), S75-S82.
    • (2002) Eur. J. Pediatr. , vol.161 , Issue.SUPPL. 1
    • Kuijpers, T.W.1
  • 3
    • 0035937107 scopus 로고    scopus 로고
    • Isolation and characterization of human β-defensin-3, a novel human-inducible peptide antibiotic
    • Harder, J., Bartels, J., Christophers, E., Schroder, J. M. (2001) Isolation and characterization of human β-defensin-3, a novel human-inducible peptide antibiotic. J. Biol. Chem. 276, 5707-5713.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5707-5713
    • Harder, J.1    Bartels, J.2    Christophers, E.3    Schroder, J.M.4
  • 4
    • 0031461206 scopus 로고    scopus 로고
    • Epithelial cells as sensors for microbial infection
    • Kagnoff, M. F., Eckmann, L. (1997) Epithelial cells as sensors for microbial infection. J. Clin. Invest. 100, 6-10.
    • (1997) J. Clin. Invest. , vol.100 , pp. 6-10
    • Kagnoff, M.F.1    Eckmann, L.2
  • 5
    • 0032734313 scopus 로고    scopus 로고
    • Expression and regulation of the human β-defensins hBD-1 and hBD-2 in intestinal epithelium
    • O'Neil, D. A., Porter, E. M., Elewaut, D., Anderson, G. M., Eckmann, L., Ganz, T., Kagnoff, M. F. (1999) Expression and regulation of the human β-defensins hBD-1 and hBD-2 in intestinal epithelium. J. Immunol. 163, 6718-6724.
    • (1999) J. Immunol. , vol.163 , pp. 6718-6724
    • O'Neil, D.A.1    Porter, E.M.2    Elewaut, D.3    Anderson, G.M.4    Eckmann, L.5    Ganz, T.6    Kagnoff, M.F.7
  • 7
    • 0038189571 scopus 로고    scopus 로고
    • Wound healing and expression of antimicrobial peptides/polypeptides in human keratinocytes, a consequence of common growth factors
    • Sorensen, O. E., Cowland, J. B., Theilgaard-Monch, K., Liu, L., Ganz, T., Borregaard, N. (2003) Wound healing and expression of antimicrobial peptides/polypeptides in human keratinocytes, a consequence of common growth factors. J. Immunol. 170, 5583-5589.
    • (2003) J. Immunol. , vol.170 , pp. 5583-5589
    • Sorensen, O.E.1    Cowland, J.B.2    Theilgaard-Monch, K.3    Liu, L.4    Ganz, T.5    Borregaard, N.6
  • 8
    • 2942592237 scopus 로고    scopus 로고
    • The transcriptional activation program of human neutrophils in skin lesions supports their important role in wound healing
    • Theilgaard-Monch, K., Knudsen, S., Follin, P., Borregaard, N. (2004) The transcriptional activation program of human neutrophils in skin lesions supports their important role in wound healing. J. Immunol. 172, 7684-7693.
    • (2004) J. Immunol. , vol.172 , pp. 7684-7693
    • Theilgaard-Monch, K.1    Knudsen, S.2    Follin, P.3    Borregaard, N.4
  • 9
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic polymorphonuclear leukocyte
    • Borregaard, N., Cowland, J. B. (1997) Granules of the human neutrophilic polymorphonuclear leukocyte. Blood 89, 3503-3521.
    • (1997) Blood , vol.89 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 10
    • 0029947655 scopus 로고    scopus 로고
    • Targeting of proteins to granule subsets determined by timing not by sorting: The specific granule protein NGAL is localized to azurophil granules when expressed in HL-60 cells
    • Le Cabec, V., Cowland, J. B., Calafat, J., Borregaard, N. (1996) Targeting of proteins to granule subsets determined by timing not by sorting: the specific granule protein NGAL is localized to azurophil granules when expressed in HL-60 cells. Proc. Natl. Acad. Sci. USA 93, 6454-6457.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6454-6457
    • Le Cabec, V.1    Cowland, J.B.2    Calafat, J.3    Borregaard, N.4
  • 11
    • 0038819118 scopus 로고    scopus 로고
    • The in vivo profile of transcription factors during neutrophil differentiation in human bone marrow
    • Bjerregaard, M. D., Jurlander, J., Klausen, P., Borregaard, N., Cowland, J. B. (2003) The in vivo profile of transcription factors during neutrophil differentiation in human bone marrow. Blood 101, 4322-4332.
    • (2003) Blood , vol.101 , pp. 4322-4332
    • Bjerregaard, M.D.1    Jurlander, J.2    Klausen, P.3    Borregaard, N.4    Cowland, J.B.5
  • 12
    • 0036134958 scopus 로고    scopus 로고
    • Neutrophil-specific granule deficiency and mutations in the gene encoding transcription factor C/EBP(ε)
    • Gombart, A. F., Koeffler, H. P. (2002) Neutrophil-specific granule deficiency and mutations in the gene encoding transcription factor C/EBP(ε). Curr. Opin. Hematol. 9, 36-42.
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 36-42
    • Gombart, A.F.1    Koeffler, H.P.2
  • 14
    • 0027955338 scopus 로고
    • Identification of neutrophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils
    • Kjeldsen, L., Bainton, D. F., Sengeløv, H., Borregaard, N. (1994) Identification of neutrophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils. Blood 83, 799-807.
    • (1994) Blood , vol.83 , pp. 799-807
    • Kjeldsen, L.1    Bainton, D.F.2    Sengeløv, H.3    Borregaard, N.4
  • 15
    • 0030880531 scopus 로고    scopus 로고
    • The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils
    • Sorensen, O., Arnljots, K., Cowland, J. B., Bainton, D. F., Borregaard, N. (1997) The human antibacterial cathelicidin, hCAP-18, is synthesized in myelocytes and metamyelocytes and localized to specific granules in neutrophils. Blood 90, 2796-2803.
    • (1997) Blood , vol.90 , pp. 2796-2803
    • Sorensen, O.1    Arnljots, K.2    Cowland, J.B.3    Bainton, D.F.4    Borregaard, N.5
  • 20
    • 0031756983 scopus 로고    scopus 로고
    • Timing targeting and sorting of azurophil granule proteins in human myeloid cells
    • Arnljots, K., Sorensen, O., Lollike, K., Borregaard, N. (1998) Timing targeting and sorting of azurophil granule proteins in human myeloid cells. Leukemia 12, 1789-1795.
    • (1998) Leukemia , vol.12 , pp. 1789-1795
    • Arnljots, K.1    Sorensen, O.2    Lollike, K.3    Borregaard, N.4
  • 21
    • 0028203752 scopus 로고
    • The heterogeneity of azurophil granules in neutrophil promyelocytes: Immunogold localization of myeloperoxidase, cathepsin G, elastase, proteinase 3, and bactericidal permeability-increasing protein
    • Egesten, A., Breton-Gorius, J., Guichard, J., Gullberg, U., Olsson, I. (1994) The heterogeneity of azurophil granules in neutrophil promyelocytes: immunogold localization of myeloperoxidase, cathepsin G, elastase, proteinase 3, and bactericidal permeability-increasing protein. Blood 83, 2985-2994.
    • (1994) Blood , vol.83 , pp. 2985-2994
    • Egesten, A.1    Breton-Gorius, J.2    Guichard, J.3    Gullberg, U.4    Olsson, I.5
  • 22
    • 0023123560 scopus 로고
    • Cellular and subcellular localization of the bactericidal/permability- increasing protein of neutrophils
    • Weiss, J., Olsson, I. (1987) Cellular and subcellular localization of the bactericidal/permability-increasing protein of neutrophils. Blood 69, 652-659.
    • (1987) Blood , vol.69 , pp. 652-659
    • Weiss, J.1    Olsson, I.2
  • 23
    • 0041566749 scopus 로고    scopus 로고
    • Expression of BPI (bactericidal/permeability-increasing protein) in human mucosal epithelia
    • Levy, O., Canny, G., Serhan, C. N., Colgan, S. P. (2003) Expression of BPI (bactericidal/permeability-increasing protein) in human mucosal epithelia. Biochem. Soc. Trans. 31, 795-800.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 795-800
    • Levy, O.1    Canny, G.2    Serhan, C.N.3    Colgan, S.P.4
  • 24
    • 0002489099 scopus 로고
    • Developmental biology of neutrophils and eosinophils
    • (Gallin, J. I., Coldslein, I. M., Snyderman, R., eds), Raven Press Ltd., New York
    • Bainton, D. F. (1992) Developmental biology of neutrophils and eosinophils. In Inflammation: Basic Principles and Clinical Correlates. (Gallin, J. I., Coldslein, I. M., Snyderman, R., eds), Raven Press Ltd., New York, 303-324.
    • (1992) Inflammation: Basic Principles and Clinical Correlates , pp. 303-324
    • Bainton, D.F.1
  • 25
    • 0029893253 scopus 로고    scopus 로고
    • The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes
    • Gudmundsson, G. H., Agerberth, B., Odeberg, J., Bergman, T., Olsson, B., Salcedo, R. (1996) The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur. J. Biochem. 238, 325-332.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 325-332
    • Gudmundsson, G.H.1    Agerberth, B.2    Odeberg, J.3    Bergman, T.4    Olsson, B.5    Salcedo, R.6
  • 26
    • 0036135697 scopus 로고    scopus 로고
    • Cathelicidins: A family of endogenous antimicrobial peptides
    • Lehrer, R. I., Ganz, T. (2002) Cathelicidins: a family of endogenous antimicrobial peptides. Curr. Opin. Hematol. 9, 18-22.
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 18-22
    • Lehrer, R.I.1    Ganz, T.2
  • 27
    • 0842326097 scopus 로고    scopus 로고
    • Cathelicidins, multifunctional peptides of the innate immunity
    • Zanetti, M. (2004) Cathelicidins, multifunctional peptides of the innate immunity. J. Leukoc. Biol. 75, 39-48.
    • (2004) J. Leukoc. Biol. , vol.75 , pp. 39-48
    • Zanetti, M.1
  • 28
    • 0037960231 scopus 로고    scopus 로고
    • Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence
    • Zaiou, M., Nizet, V., Gallo, R. L. (2003) Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence. J. Invest. Dermatol. 120, 810-816.
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 810-816
    • Zaiou, M.1    Nizet, V.2    Gallo, R.L.3
  • 29
    • 0034596945 scopus 로고    scopus 로고
    • LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells
    • Yang, D., Chen, Q., Schmidt, A. P., Anderson, G. M., Wang, J. M., Wooters, J., Oppenheim, J. J., Chertov, O. (2000) LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells. J. Exp. Med. 192, 1069-1074.
    • (2000) J. Exp. Med. , vol.192 , pp. 1069-1074
    • Yang, D.1    Chen, Q.2    Schmidt, A.P.3    Anderson, G.M.4    Wang, J.M.5    Wooters, J.6    Oppenheim, J.J.7    Chertov, O.8
  • 30
    • 0346996865 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor
    • Tjabringa, G. S., Aarbiou, J., Ninaber, D. K., Drijfhout, J. W., Sorensen, O. E., Borregaard, N., Rabe, K. F., Hiemstra, P. S. (2003) The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor. J. Immunol. 171, 6690-6696.
    • (2003) J. Immunol. , vol.171 , pp. 6690-6696
    • Tjabringa, G.S.1    Aarbiou, J.2    Ninaber, D.K.3    Drijfhout, J.W.4    Sorensen, O.E.5    Borregaard, N.6    Rabe, K.F.7    Hiemstra, P.S.8
  • 31
    • 0036785559 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses
    • Scott, M. G., Davidson, D. J., Gold, M. R., Bowdish, D., Hancock, R. E. (2002) The human antimicrobial peptide LL-37 is a multifunctional modulator of innate immune responses. J. Immunol. 169, 3883-3891.
    • (2002) J. Immunol. , vol.169 , pp. 3883-3891
    • Scott, M.G.1    Davidson, D.J.2    Gold, M.R.3    Bowdish, D.4    Hancock, R.E.5
  • 33
    • 2342520028 scopus 로고    scopus 로고
    • The human antimicrobial peptide LL-37 transfers extracellular DNA plasmid to the nuclear compartment of mammalian cells via lipid rafts and proteoglycan-dependent endocytosis
    • Sandgren, S., Wittrup, A., Cheng, F., Jonsson, M., Eklund, E., Busch, S., Belting, M. (2004) The human antimicrobial peptide LL-37 transfers extracellular DNA plasmid to the nuclear compartment of mammalian cells via lipid rafts and proteoglycan-dependent endocytosis. J. Biol. Chem. 279, 17951-17956.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17951-17956
    • Sandgren, S.1    Wittrup, A.2    Cheng, F.3    Jonsson, M.4    Eklund, E.5    Busch, S.6    Belting, M.7
  • 34
    • 0035884820 scopus 로고    scopus 로고
    • Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibits the expression of TNF-α by blocking the binding of LPS to CD14(+) cells
    • Nagaoka, I., Hirota, S., Niyonsaba, F., Hirata, M., Adachi, Y., Tamura, H., Heumann, D. (2001) Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibits the expression of TNF-α by blocking the binding of LPS to CD14(+) cells. J. Immunol. 167, 3329-3338.
    • (2001) J. Immunol. , vol.167 , pp. 3329-3338
    • Nagaoka, I.1    Hirota, S.2    Niyonsaba, F.3    Hirata, M.4    Adachi, Y.5    Tamura, H.6    Heumann, D.7
  • 36
    • 0035877995 scopus 로고    scopus 로고
    • Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3
    • Sorensen, O. E., Follin, P., Johnsen, A. H., Calafat, J., Tjabringa, G. S., Hiemstra, P. S., Borregaard, N. (2001) Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3. Blood 97, 3951-3959.
    • (2001) Blood , vol.97 , pp. 3951-3959
    • Sorensen, O.E.1    Follin, P.2    Johnsen, A.H.3    Calafat, J.4    Tjabringa, G.S.5    Hiemstra, P.S.6    Borregaard, N.7
  • 38
    • 0019480640 scopus 로고
    • The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH
    • Segal, A. W., Geisow, M., Garcia, R., Harper, A., Miller, R. (1981) The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH. Nature 290, 406-409.
    • (1981) Nature , vol.290 , pp. 406-409
    • Segal, A.W.1    Geisow, M.2    Garcia, R.3    Harper, A.4    Miller, R.5
  • 41
    • 0021203722 scopus 로고
    • Proton secretion by stimulated neutrophils. Significance of hexose monophosphate shunt activity as source of electrons and protons for the respiratory burst
    • Borregaard, N., Schwartz, J. H., Tauber, A. I. (1984) Proton secretion by stimulated neutrophils. Significance of hexose monophosphate shunt activity as source of electrons and protons for the respiratory burst. J. Clin. Invest. 74, 455-459.
    • (1984) J. Clin. Invest. , vol.74 , pp. 455-459
    • Borregaard, N.1    Schwartz, J.H.2    Tauber, A.I.3
  • 42
    • 0030862762 scopus 로고    scopus 로고
    • The arachidonate-activatable, NADPH oxidase-associated H+ channel is contained within the multi-membrane-spanning N- terminal region of gp91phox
    • Henderson, L. M., Thomas, S., Banting, G., Chappell, J. B. (1997) The arachidonate-activatable, NADPH oxidase-associated H+ channel is contained within the multi-membrane-spanning N- terminal region of gp91phox. Biochem. J. 325, 701-705.
    • (1997) Biochem. J. , vol.325 , pp. 701-705
    • Henderson, L.M.1    Thomas, S.2    Banting, G.3    Chappell, J.B.4
  • 43
    • 0036899247 scopus 로고    scopus 로고
    • Proton conduction through gp91phox
    • Henderson, L. M., Meech, R. W. (2002) Proton conduction through gp91phox. J. Gen. Physiol. 120, 759-765.
    • (2002) J. Gen. Physiol. , vol.120 , pp. 759-765
    • Henderson, L.M.1    Meech, R.W.2
  • 44
    • 0037155215 scopus 로고    scopus 로고
    • Determinants of the phagosomal pH in neutrophils
    • Jankowski, A., Scott, C. C., Grinstein, S. (2002) Determinants of the phagosomal pH in neutrophils. J. Biol. Chem. 277, 6059-6066.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6059-6066
    • Jankowski, A.1    Scott, C.C.2    Grinstein, S.3
  • 46
    • 0033918174 scopus 로고    scopus 로고
    • The human cationic antimicrobial protein (hCAP-18) is expressed in the epithelium of human epididymis, is present in seminal plasma at high concentrations, and is attached to spermatozoa
    • Malm, J., Sorensen, O., Persson, T., Frohm-Nilsson, M., Johansson, B., Bjartell, A., Lilja, H., Stahle-Backdahl, M., Borregaard, N., Egesten, A. (2000) The human cationic antimicrobial protein (hCAP-18) is expressed in the epithelium of human epididymis, is present in seminal plasma at high concentrations, and is attached to spermatozoa. Infect. Immun. 68, 4297-4302.
    • (2000) Infect. Immun. , vol.68 , pp. 4297-4302
    • Malm, J.1    Sorensen, O.2    Persson, T.3    Frohm-Nilsson, M.4    Johansson, B.5    Bjartell, A.6    Lilja, H.7    Stahle-Backdahl, M.8    Borregaard, N.9    Egesten, A.10
  • 49
    • 0037335205 scopus 로고    scopus 로고
    • The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium
    • Heilborn, J. D., Nilsson, M. F., Kratz, G., Weber, G., Sorensen, O., Borregaard, N., Stahle-Backdahl, M. (2003) The cathelicidin anti-microbial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium. J. Invest. Dermatol. 120, 379-389.
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 379-389
    • Heilborn, J.D.1    Nilsson, M.F.2    Kratz, G.3    Weber, G.4    Sorensen, O.5    Borregaard, N.6    Stahle-Backdahl, M.7
  • 51
    • 0035163451 scopus 로고    scopus 로고
    • Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds
    • Cole, A. M., Shi, J. S., Ceccarelli, A., Kim, Y. H., Park, A., Ganz, T. (2001) Inhibition of neutrophil elastase prevents cathelicidin activation and impairs clearance of bacteria from wounds. Blood 97, 297-304.
    • (2001) Blood , vol.97 , pp. 297-304
    • Cole, A.M.1    Shi, J.S.2    Ceccarelli, A.3    Kim, Y.H.4    Park, A.5    Ganz, T.6
  • 52
    • 0026680779 scopus 로고
    • Insulin-like growth factors I and II expression in the healing wound
    • Gartner, M. H., Benson, J. D., Caldwell, M. D. (1992) Insulin-like growth factors I and II expression in the healing wound. J. Surg. Res. 52, 389-394.
    • (1992) J. Surg. Res. , vol.52 , pp. 389-394
    • Gartner, M.H.1    Benson, J.D.2    Caldwell, M.D.3
  • 53
    • 0026555610 scopus 로고
    • The insulin-like growth factor I receptor is overexpressed in psoriatic epidermis, but is differentially regulated from the epidermal growth factor receptor
    • Krane, J. F., Cottlieb, A. B., Carter, D. M., Krueger, J. C. (1992) The insulin-like growth factor I receptor is overexpressed in psoriatic epidermis, but is differentially regulated from the epidermal growth factor receptor. J. Exp. Med. 175, 1081-1090.
    • (1992) J. Exp. Med. , vol.175 , pp. 1081-1090
    • Krane, J.F.1    Cottlieb, A.B.2    Carter, D.M.3    Krueger, J.C.4
  • 54
    • 0027256664 scopus 로고
    • Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
    • Kjeldsen, L., Johnsen, A. H., Sengeløv, H., Borregaard, N. (1993) Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. J. Biol. Chem. 268, 10425-10432.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10425-10432
    • Kjeldsen, L.1    Johnsen, A.H.2    Sengeløv, H.3    Borregaard, N.4
  • 55
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: Structure and function
    • Flower, D. R. (1996) The lipocalin protein family: structure and function. Biochem. J. 318, 1-14.
    • (1996) Biochem. J. , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 56
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., Strong, R. K. (2002) The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 10, 1033-1043.
    • (2002) Mol. Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 57
    • 0028850367 scopus 로고
    • Siderophores: Structure and function of microbial iron transport compounds
    • Neilands, J. B. (1995) Siderophores: structure and function of microbial iron transport compounds. J. Biol. Chem. 270, 26723-26726.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26723-26726
    • Neilands, J.B.1
  • 58
    • 0028265107 scopus 로고
    • Isolation and characterization of gelatinase granules from human neutrophils
    • Kjeldsen, L., Sengeløv, H., Lollike, K., Nielsen, M. H., Borregaard, N. (1994) Isolation and characterization of gelatinase granules from human neutrophils. Blood 83, 1640-1649.
    • (1994) Blood , vol.83 , pp. 1640-1649
    • Kjeldsen, L.1    Sengeløv, H.2    Lollike, K.3    Nielsen, M.H.4    Borregaard, N.5
  • 59
    • 0029981266 scopus 로고    scopus 로고
    • Induction of NGAL synthesis in epithelial cells of human colorectal neoplasia and inflammatory bowel disease
    • Nielsen, B. S., Borregaard, N., Bundgaard, J. R., Timshel, S., Sehested, M., Kjeldsen, L. (1996) Induction of NGAL synthesis in epithelial cells of human colorectal neoplasia and inflammatory bowel disease. Gut 38, 414-420.
    • (1996) Gut , vol.38 , pp. 414-420
    • Nielsen, B.S.1    Borregaard, N.2    Bundgaard, J.R.3    Timshel, S.4    Sehested, M.5    Kjeldsen, L.6
  • 60
    • 0346996867 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin is up-regulated in human epithelial cells by IL-1β, but not by TNF-α
    • Cowland, J. B., Sorensen, O. E., Sehested, M., Borregaard, N. (2003) Neutrophil gelatinase-associated lipocalin is up-regulated in human epithelial cells by IL-1β, but not by TNF-α. J. Immunol. 171, 6630-6639.
    • (2003) J. Immunol. , vol.171 , pp. 6630-6639
    • Cowland, J.B.1    Sorensen, O.E.2    Sehested, M.3    Borregaard, N.4
  • 62
    • 0021981476 scopus 로고
    • Ultrastructural localization of lactoferrin and myeloperoxidase in human neutrophils by immunogold
    • Cramer, E., Pryzwansky, K. B., Villeval, J-L., Testa, U., Breton-Gorius, J. (1985) Ultrastructural localization of lactoferrin and myeloperoxidase in human neutrophils by immunogold. Blood 65, 423-432.
    • (1985) Blood , vol.65 , pp. 423-432
    • Cramer, E.1    Pryzwansky, K.B.2    Villeval, J.-L.3    Testa, U.4    Breton-Gorius, J.5
  • 64
    • 0028226536 scopus 로고
    • Leucocyte-endothelial interactions and regulation of leucocyte migration
    • Adams, D. H., Shaw, S. (1994) Leucocyte-endothelial interactions and regulation of leucocyte migration. Lancet 343, 831-836.
    • (1994) Lancet , vol.343 , pp. 831-836
    • Adams, D.H.1    Shaw, S.2
  • 65
    • 0028214238 scopus 로고
    • The microcirculation and inflammation: Modulation of leukocyte- endothelial cell adhesion
    • Granger, D. N., Kubes, P. (1994) The microcirculation and inflammation: modulation of leukocyte- endothelial cell adhesion. J. Leukoc. Biol. 55, 662-675.
    • (1994) J. Leukoc. Biol. , vol.55 , pp. 662-675
    • Granger, D.N.1    Kubes, P.2
  • 67
    • 0033402250 scopus 로고    scopus 로고
    • Skin-chamber technique for study of in vivo exudated human neutrophils
    • Follin, P. (1999) Skin-chamber technique for study of in vivo exudated human neutrophils. J. Immunol. Methods 232, 55-65.
    • (1999) J. Immunol. Methods , vol.232 , pp. 55-65
    • Follin, P.1
  • 68
    • 0035075706 scopus 로고    scopus 로고
    • Chemokines in cutaneous wound healing
    • Gillitzer, R., Goebeler, M. (2001) Chemokines in cutaneous wound healing. J. Leukoc. Biol. 69, 513-521.
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 513-521
    • Gillitzer, R.1    Goebeler, M.2
  • 70
    • 0035942278 scopus 로고    scopus 로고
    • In vivo restoration of laminin 5 β 3 expression and function in junctional epidermolysis bullosa
    • Robbins, P. B., Lin, Q., Goodnough, J. B., Tian, H., Chen, X., Khavari, P. A. (2001) In vivo restoration of laminin 5 β 3 expression and function in junctional epidermolysis bullosa. Proc. Natl. Acad. Sci. USA 98, 5193-5198.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5193-5198
    • Robbins, P.B.1    Lin, Q.2    Goodnough, J.B.3    Tian, H.4    Chen, X.5    Khavari, P.A.6
  • 71
    • 0036906177 scopus 로고    scopus 로고
    • uPAR: A versatile signaling orchestrator
    • Blasi, F., Carmeliet, P. (2002) uPAR: a versatile signaling orchestrator. Nat. Rev. Mol. Cell Biol. 3, 932-943.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 932-943
    • Blasi, F.1    Carmeliet, P.2
  • 73
    • 2942532399 scopus 로고    scopus 로고
    • Shear-dependent capping of L-selectin and P-selectin glycoprotein ligand 1 by E-selectin signals activation of high-avidity β2-integrin on neutrophils
    • Green, C. E., Pearson, D. N., Camphausen, R. T., Staunton, D. E., Simon, S. I. (2004) Shear-dependent capping of L-selectin and P-selectin glycoprotein ligand 1 by E-selectin signals activation of high-avidity β2-integrin on neutrophils. J. Immunol. 172, 7780-7790.
    • (2004) J. Immunol. , vol.172 , pp. 7780-7790
    • Green, C.E.1    Pearson, D.N.2    Camphausen, R.T.3    Staunton, D.E.4    Simon, S.I.5
  • 74
    • 0035877649 scopus 로고    scopus 로고
    • Subcellular distribution and cytokine- and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils
    • Kang, T., Yi, J., Guo, A., Wang, X., Overall, C. M., Jiang, W., Elde, R., Borregaard, N., Pei, D. (2001) Subcellular distribution and cytokine- and chemokine-regulated secretion of leukolysin/MT6-MMP/MMP-25 in neutrophils. J. Biol. Chem. 276, 21960-21968.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21960-21968
    • Kang, T.1    Yi, J.2    Guo, A.3    Wang, X.4    Overall, C.M.5    Jiang, W.6    Elde, R.7    Borregaard, N.8    Pei, D.9
  • 75
    • 0027420678 scopus 로고
    • Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: Identification of a distinct gelatinase- containing granule subset by combined immunocytochemistry and subcellular fractionation
    • Kjeldsen, L., Bainton, D. F., Sengeløv, H., Borregaard, N. (1993) Structural and functional heterogeneity among peroxidase-negative granules in human neutrophils: identification of a distinct gelatinase-containing granule subset by combined immunocytochemistry and subcellular fractionation. Blood 82, 3183-3191.
    • (1993) Blood , vol.82 , pp. 3183-3191
    • Kjeldsen, L.1    Bainton, D.F.2    Sengeløv, H.3    Borregaard, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.