메뉴 건너뛰기




Volumn 129, Issue 6, 2006, Pages 1683-1692

Do native and polymeric α1-antitrypsin activate human neutrophils in vitro?

Author keywords

Chemotaxis; Endotoxin; Neutrophils; Polymers; 1 antitrypsin

Indexed keywords

ALPHA 1 ANTITRYPSIN; ENDOTOXIN; FORMYLMETHIONYLLEUCYLPHENYLALANINE; INTERLEUKIN 8; LIPOPOLYSACCHARIDE; ZYMOSAN; BIOPOLYMER;

EID: 33745154191     PISSN: 00123692     EISSN: None     Source Type: Journal    
DOI: 10.1378/chest.129.6.1683     Document Type: Article
Times cited : (9)

References (32)
  • 2
    • 0036346760 scopus 로고    scopus 로고
    • Chronic obstructive pulmonary disease: 1. Susceptibility factors for COPD the genotype-environment interaction
    • Sandford AJ, Silverman EK. Chronic obstructive pulmonary disease: 1. Susceptibility factors for COPD the genotype-environment interaction. Thorax 2002; 57:736-741
    • (2002) Thorax , vol.57 , pp. 736-741
    • Sandford, A.J.1    Silverman, E.K.2
  • 3
    • 0024842004 scopus 로고
    • 1-antitrypsin deficiency gene and its deficiency states
    • 1-antitrypsin deficiency gene and its deficiency states. Trends Genet 1989; 5:411-417
    • (1989) Trends Genet , vol.5 , pp. 411-417
    • Crystal, R.G.1
  • 6
    • 0002582641 scopus 로고    scopus 로고
    • 1-Antitrypsin genotypes and phenotypes
    • Crystal RG, ed. New York, NY: Marcel Dekker
    • 1-Antitrypsin genotypes and phenotypes. In: Crystal RG, ed. α1-Antitrypsin deficiency. New York, NY: Marcel Dekker, 1996; 45-59
    • (1996) α1-Antitrypsin Deficiency , pp. 45-59
    • Brantly, M.1
  • 7
    • 0030448066 scopus 로고    scopus 로고
    • α1-antitrypsin deficiency: A conformational disease
    • Carrell RW, Lomas DA, Sidhar S, et al. α1-Antitrypsin deficiency: a conformational disease. Chest 1996; 110:243S-247S
    • (1996) Chest , vol.110
    • Carrell, R.W.1    Lomas, D.A.2    Sidhar, S.3
  • 8
    • 0035952980 scopus 로고    scopus 로고
    • Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles
    • Janciauskiene S. Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles. Biochim Biophys Acta 2001; 1535:221-235
    • (2001) Biochim Biophys Acta , vol.1535 , pp. 221-235
    • Janciauskiene, S.1
  • 9
    • 0030922043 scopus 로고    scopus 로고
    • Review: α1-antitrypsin deficiency associated liver disease
    • Qu D, Teckman JH, Perlmutter DH. Review: α1-antitrypsin deficiency associated liver disease. J Gastroenterol Hepatol 1997; 12:404-416
    • (1997) J Gastroenterol Hepatol , vol.12 , pp. 404-416
    • Qu, D.1    Teckman, J.H.2    Perlmutter, D.H.3
  • 10
    • 0032065494 scopus 로고    scopus 로고
    • Lung polymers in Z α1-antitrypsin deficiency-related emphysema
    • Elliott PR, Bilton D, Lomas DA. Lung polymers in Z α1-antitrypsin deficiency-related emphysema. Am J Respir Cell Mol Biol 1998; 18:670-674
    • (1998) Am J Respir Cell Mol Biol , vol.18 , pp. 670-674
    • Elliott, P.R.1    Bilton, D.2    Lomas, D.A.3
  • 11
    • 0037135563 scopus 로고    scopus 로고
    • Detection of circulating and endothelial cell polymers of Z and wild type α1-antitrypsin by a monoclonal antibody
    • Janciauskiene S, Dominaitiene R, Sternby NH, et al. Detection of circulating and endothelial cell polymers of Z and wild type α1-antitrypsin by a monoclonal antibody. J Biol Chem 2002; 277:26540-26546
    • (2002) J Biol Chem , vol.277 , pp. 26540-26546
    • Janciauskiene, S.1    Dominaitiene, R.2    Sternby, N.H.3
  • 12
    • 14044279288 scopus 로고    scopus 로고
    • α1-antitrypsin polymerization: A fluorescence correlation spectroscopic study
    • Purkayastha P, Klemke JW, Lavender S, et al. α1-Antitrypsin polymerization: a fluorescence correlation spectroscopic study. Biochemistry 2005; 44:2642-2649
    • (2005) Biochemistry , vol.44 , pp. 2642-2649
    • Purkayastha, P.1    Klemke, J.W.2    Lavender, S.3
  • 13
    • 0036882160 scopus 로고    scopus 로고
    • Acid denaturation of α1-antitrypsin: Characterization of a novel mechanism of serpin polymerization
    • Devlin GL, Chow MK, Howlett GJ, et al. Acid denaturation of α1-antitrypsin: characterization of a novel mechanism of serpin polymerization. J Mol Biol 2002; 324:859-870
    • (2002) J Mol Biol , vol.324 , pp. 859-870
    • Devlin, G.L.1    Chow, M.K.2    Howlett, G.J.3
  • 14
    • 0034969249 scopus 로고    scopus 로고
    • Prevention of polymerization of M and Z α1-antitrypsin (α1-AT) with trimethylamine N-oxide: Implications for the treatment of α1-AT deficiency
    • Devlin GL, Parfrey H, Tew DJ, et al. Prevention of polymerization of M and Z α1-antitrypsin (α1-AT) with trimethylamine N-oxide: implications for the treatment of α1-AT deficiency. Am J Respir Cell Mol Biol 2001; 24:727-732
    • (2001) Am J Respir Cell Mol Biol , vol.24 , pp. 727-732
    • Devlin, G.L.1    Parfrey, H.2    Tew, D.J.3
  • 15
    • 0036014834 scopus 로고    scopus 로고
    • Polymers of α(1)-antitrypsin are chemotactic for human neutrophils: A new paradigm for the pathogenesis of emphysema
    • Parmar JS, Mahadeva R, Reed BJ, et al. Polymers of α(1)-antitrypsin are chemotactic for human neutrophils: a new paradigm for the pathogenesis of emphysema. Am J Respir Cell Mol Biol 2002; 26:723-730
    • (2002) Am J Respir Cell Mol Biol , vol.26 , pp. 723-730
    • Parmar, J.S.1    Mahadeva, R.2    Reed, B.J.3
  • 16
    • 2442488539 scopus 로고    scopus 로고
    • Z α1-antitrypsin polymerizes in the lung and acts as a neutrophil chemoattractant
    • Mulgrew AT, Taggart CC, Lawless MW, et al. Z α1-antitrypsin polymerizes in the lung and acts as a neutrophil chemoattractant. Chest 2004; 125:1952-1957
    • (2004) Chest , vol.125 , pp. 1952-1957
    • Mulgrew, A.T.1    Taggart, C.C.2    Lawless, M.W.3
  • 17
    • 19944430698 scopus 로고    scopus 로고
    • Polymers of Z α1-antitrypsin co-localize with neutrophils in emphysematous alveoli and are chemotactic in vivo
    • Mahadeva R, Atkinson C, Li Z, et al. Polymers of Z α1-antitrypsin co-localize with neutrophils in emphysematous alveoli and are chemotactic in vivo. Am J Pathol 2005; 166:377-386
    • (2005) Am J Pathol , vol.166 , pp. 377-386
    • Mahadeva, R.1    Atkinson, C.2    Li, Z.3
  • 18
    • 0842289045 scopus 로고    scopus 로고
    • Divergent effects of α1-antitrypsin on neutrophil activation, in vitro
    • Janciauskiene S, Zelvyte I, Jansson L, et al. Divergent effects of α1-antitrypsin on neutrophil activation, in vitro. Biochem Biophys Res Commun 2004; 315:288-296
    • (2004) Biochem Biophys Res Commun , vol.315 , pp. 288-296
    • Janciauskiene, S.1    Zelvyte, I.2    Jansson, L.3
  • 19
    • 4344673827 scopus 로고    scopus 로고
    • Inhibition of lipopolysaccharide-mediated human monocyte activation, in vitro, by α1-antitrypsin
    • Janciauskiene S, Larsson S, Larsson P, et al. Inhibition of lipopolysaccharide-mediated human monocyte activation, in vitro, by α1-antitrypsin. Biochem Biophys Res Commun 2004; 321:592-600
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 592-600
    • Janciauskiene, S.1    Larsson, S.2    Larsson, P.3
  • 20
    • 0036049386 scopus 로고    scopus 로고
    • A longitudinal cohort study on the prevalence of Helicobacter pylori antibodies in Swedish children and adolescents
    • Granquist A, Bredberg A, Sveger T, et al., A longitudinal cohort study on the prevalence of Helicobacter pylori antibodies in Swedish children and adolescents. Acta Paediatr 2002; 91:636-640
    • (2002) Acta Paediatr , vol.91 , pp. 636-640
    • Granquist, A.1    Bredberg, A.2    Sveger, T.3
  • 21
    • 10644267224 scopus 로고    scopus 로고
    • Circulating monocytes from healthy individuals and COPD patients
    • Aldonyte R, Jansson L, Pütulainen E, et al. Circulating monocytes from healthy individuals and COPD patients. Respir Res 2003; 4:11
    • (2003) Respir Res , vol.4 , pp. 11
    • Aldonyte, R.1    Jansson, L.2    Pütulainen, E.3
  • 22
    • 0031438767 scopus 로고    scopus 로고
    • Environmental endotoxin measurement: Interference and sources of variation in the Limulus assay of house dust
    • Milton DK, Johnson DK, Park JH. Environmental endotoxin measurement: interference and sources of variation in the Limulus assay of house dust. Am Ind Hyg Assoc J 1997; 58:861-867
    • (1997) Am Ind Hyg Assoc J , vol.58 , pp. 861-867
    • Milton, D.K.1    Johnson, D.K.2    Park, J.H.3
  • 23
    • 18744427927 scopus 로고    scopus 로고
    • A rapid and simple photometric assay for quantification of eosinophil chemotaxis
    • Nagase H, Yamaguchi M, Jibiki S, et al. A rapid and simple photometric assay for quantification of eosinophil chemotaxis. Int Arch Allergy Appl Immunol 2000; 49:10-14
    • (2000) Int Arch Allergy Appl Immunol , vol.49 , pp. 10-14
    • Nagase, H.1    Yamaguchi, M.2    Jibiki, S.3
  • 24
    • 0017347752 scopus 로고
    • Inflammatory effects of endotoxin-like contaminants in commonly used protein preparations
    • Bito LZ. Inflammatory effects of endotoxin-like contaminants in commonly used protein preparations. Science 1977; 196:83-85
    • (1977) Science , vol.196 , pp. 83-85
    • Bito, L.Z.1
  • 25
    • 0037027896 scopus 로고    scopus 로고
    • Chromatographic removal of endotoxin from protein solutions by polymer particles
    • Hirayama C, Sakata M. Chromatographic removal of endotoxin from protein solutions by polymer particles. J Chromatogr B Analyt Technol Biomed Life Sci 2002; 781:419-432
    • (2002) J Chromatogr B Analyt Technol Biomed Life Sci , vol.781 , pp. 419-432
    • Hirayama, C.1    Sakata, M.2
  • 26
    • 18644373359 scopus 로고    scopus 로고
    • Questioning current concepts in acute pancreatitis: Endotoxin contamination of porcine pancreatic elastase is responsible for experimental pancreatitis-associated distant organ failure
    • Geisler F, Algul H, Riemann M, et al. Questioning current concepts in acute pancreatitis: endotoxin contamination of porcine pancreatic elastase is responsible for experimental pancreatitis-associated distant organ failure. J Immunol 2005; 174:6431-6439
    • (2005) J Immunol , vol.174 , pp. 6431-6439
    • Geisler, F.1    Algul, H.2    Riemann, M.3
  • 27
    • 0037636017 scopus 로고    scopus 로고
    • Gene expression in human neutrophils during activation and priming by bacterial lipopolysaccharide
    • Tsukahara Y, Lian Z, Zhang X, et al. Gene expression in human neutrophils during activation and priming by bacterial lipopolysaccharide. J Cell Biochem 2003; 89:848-861
    • (2003) J Cell Biochem , vol.89 , pp. 848-861
    • Tsukahara, Y.1    Lian, Z.2    Zhang, X.3
  • 28
    • 0000701007 scopus 로고
    • On the composition of zymosan
    • DiCarlo FJ, Fiore JV. On the composition of zymosan. Science 1957; 127:756-758
    • (1957) Science , vol.127 , pp. 756-758
    • DiCarlo, F.J.1    Fiore, J.V.2
  • 29
    • 0018830604 scopus 로고
    • Zymosan-induced experimental hypersensitivity pneumonitis in rabbits
    • Barrios R, Santos GG, Figueroa J, et al. Zymosan-induced experimental hypersensitivity pneumonitis in rabbits. Am J Pathol 1980; 99:731-740
    • (1980) Am J Pathol , vol.99 , pp. 731-740
    • Barrios, R.1    Santos, G.G.2    Figueroa, J.3
  • 30
    • 0035827579 scopus 로고    scopus 로고
    • Molecular mechanism of tumor necrosis factor-α production in 1->3-β-glucan (zymosan)-activated macrophages
    • Young SH, Ye J, Frazer DG, et al. Molecular mechanism of tumor necrosis factor-α production in 1->3-β-glucan (zymosan)-activated macrophages. J Biol Chem 2001; 276:20781-20787
    • (2001) J Biol Chem , vol.276 , pp. 20781-20787
    • Young, S.H.1    Ye, J.2    Frazer, D.G.3
  • 31
    • 0042031488 scopus 로고    scopus 로고
    • α-1-antitrypsin ameliorates cigarette smoke-induced emphysema in the mouse
    • Churg A, Wang RD, Xie C, et al. α-1-Antitrypsin ameliorates cigarette smoke-induced emphysema in the mouse. Am J Respir Crit Care Med 2003; 168:199-207
    • (2003) Am J Respir Crit Care Med , vol.168 , pp. 199-207
    • Churg, A.1    Wang, R.D.2    Xie, C.3
  • 32
    • 0034883830 scopus 로고    scopus 로고
    • α-1-antitrypsin and a broad spectrum metalloprotease inhibitor, RS113456, have similar acute anti-inflammatory effects
    • Churg A, Dai J, Zay K, et al. α-1-Antitrypsin and a broad spectrum metalloprotease inhibitor, RS113456, have similar acute anti-inflammatory effects. Lab Invest 2001; 81:1119-1131
    • (2001) Lab Invest , vol.81 , pp. 1119-1131
    • Churg, A.1    Dai, J.2    Zay, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.