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Volumn 76, Issue 6, 2008, Pages 2259-2272

Multiple roles of phospholipase A2 during lung infection and inflammation

Author keywords

[No Author keywords available]

Indexed keywords

ASBESTOS; CHEMOKINE; CIGARETTE SMOKE; CYTOKINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 10; INTERLEUKIN 6; INTERLEUKIN 8; LUNG SURFACTANT; MACROPHAGE INFLAMMATORY PROTEIN 1BETA; MITOGEN ACTIVATED PROTEIN KINASE; MONOCYTE CHEMOTACTIC PROTEIN 1; PHOSPHOLIPASE A2; PHOSPHOLIPID; TUMOR NECROSIS FACTOR ALPHA;

EID: 46249083367     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.00059-08     Document Type: Short Survey
Times cited : (52)

References (136)
  • 1
    • 33845580262 scopus 로고    scopus 로고
    • Positional specificity of lysosomal phospholipase A2
    • Abe, A., M. Hiraoka, and J. A. Shayman. 2006. Positional specificity of lysosomal phospholipase A2. J. Lipid Res. 47:2268-2279.
    • (2006) J. Lipid Res , vol.47 , pp. 2268-2279
    • Abe, A.1    Hiraoka, M.2    Shayman, J.A.3
  • 2
    • 5644289431 scopus 로고    scopus 로고
    • Lysosomal phospholipase A2 is selectively expressed in alveolar macrophages
    • Abe, A., M. Hiraoka, S. Wild, S. E. Wilcoxen, R. Paine III, and J. A. Shayman. 2004. Lysosomal phospholipase A2 is selectively expressed in alveolar macrophages. J. Biol. Chem. 279:42605-42611.
    • (2004) J. Biol. Chem , vol.279 , pp. 42605-42611
    • Abe, A.1    Hiraoka, M.2    Wild, S.3    Wilcoxen, S.E.4    Paine III, R.5    Shayman, J.A.6
  • 3
    • 0036669403 scopus 로고    scopus 로고
    • Platelet-activating factor acetylhydrolase
    • Arai, H. 2002. Platelet-activating factor acetylhydrolase. Prostaglandins Other Lipid Mediat. 68-69:83-94.
    • (2002) Prostaglandins Other Lipid Mediat , vol.68-69 , pp. 83-94
    • Arai, H.1
  • 4
    • 0031182988 scopus 로고    scopus 로고
    • Endotoxin induces expression of type II phospholipase A2 in macrophages during acute lung injury in guinea pigs: Involvement of TNF-alpha in lipopolysaccharide-induced type II phospholipase A2 synthesis
    • Arbibe, L., D. Vial, I. Rosinski-Chupin, N. Havet, M. Huerre, B. B. Vargaftig, and L. Touqui. 1997. Endotoxin induces expression of type II phospholipase A2 in macrophages during acute lung injury in guinea pigs: involvement of TNF-alpha in lipopolysaccharide-induced type II phospholipase A2 synthesis. J. Immunol. 159:391-400.
    • (1997) J. Immunol , vol.159 , pp. 391-400
    • Arbibe, L.1    Vial, D.2    Rosinski-Chupin, I.3    Havet, N.4    Huerre, M.5    Vargaftig, B.B.6    Touqui, L.7
  • 5
    • 0032530764 scopus 로고    scopus 로고
    • Generation of lyso-phospholipids from surfactant in acute lung injury is mediated by type-II phospholipase A2 and inhibited by a direct surfactant protein A-phospholipase A2 protein interaction
    • Arbibe, L., K. Koumanov, D. Vial, C. Rougeot, G. Faure, N. Havet, S. Longacre, B. B. Vargaftig, G. Bereziat, D. R. Voelker, C. Wolf, and L. Touqui. 1998. Generation of lyso-phospholipids from surfactant in acute lung injury is mediated by type-II phospholipase A2 and inhibited by a direct surfactant protein A-phospholipase A2 protein interaction. J. Clin. Investig. 102:1152-1160.
    • (1998) J. Clin. Investig , vol.102 , pp. 1152-1160
    • Arbibe, L.1    Koumanov, K.2    Vial, D.3    Rougeot, C.4    Faure, G.5    Havet, N.6    Longacre, S.7    Vargaftig, B.B.8    Bereziat, G.9    Voelker, D.R.10    Wolf, C.11    Touqui, L.12
  • 7
    • 33750940385 scopus 로고    scopus 로고
    • Group V sPLA2: Classical and novel functions
    • Balestrieri, B., and J. P. Arm. 2006. Group V sPLA2: classical and novel functions. Biochim. Biophys. Acta 1761:1280-1288.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1280-1288
    • Balestrieri, B.1    Arm, J.P.2
  • 8
    • 21644483621 scopus 로고    scopus 로고
    • Cellular regulation and proposed biological functions of group VIA calcium-independent phospholipase A2 in activated cells
    • Balsinde, J., and M. A. Balboa. 2005. Cellular regulation and proposed biological functions of group VIA calcium-independent phospholipase A2 in activated cells. Cell. Signal. 17:1052-1062.
    • (2005) Cell. Signal , vol.17 , pp. 1052-1062
    • Balsinde, J.1    Balboa, M.A.2
  • 9
    • 33750931770 scopus 로고    scopus 로고
    • Calcium-independent phospholipase A2 and apoptosis
    • Balsinde, J., R. Perez, and M. A. Balboa. 2006. Calcium-independent phospholipase A2 and apoptosis. Biochim. Biophys. Acta 1761:1344-1350.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1344-1350
    • Balsinde, J.1    Perez, R.2    Balboa, M.A.3
  • 10
    • 1642365547 scopus 로고    scopus 로고
    • Patatin-like proteins: A new family of lipolytic enzymes present in bacteria?
    • Banerji, S., and A. Flieger. 2004. Patatin-like proteins: a new family of lipolytic enzymes present in bacteria? Microbiology 150:522-525.
    • (2004) Microbiology , vol.150 , pp. 522-525
    • Banerji, S.1    Flieger, A.2
  • 11
    • 17644374820 scopus 로고    scopus 로고
    • Characterization of the major secreted zinc metalloprotease-dependent glycerophospholipid:cholesterol acyltransferase, PlaC, of Legionella pneumophila
    • Banerji, S., M. Bewersdorff, B. Hermes, N. P. Cianciotto, and A. Flieger. 2005. Characterization of the major secreted zinc metalloprotease-dependent glycerophospholipid:cholesterol acyltransferase, PlaC, of Legionella pneumophila. Infect. Immun. 73:2899-2909.
    • (2005) Infect. Immun , vol.73 , pp. 2899-2909
    • Banerji, S.1    Bewersdorff, M.2    Hermes, B.3    Cianciotto, N.P.4    Flieger, A.5
  • 13
    • 33644936973 scopus 로고    scopus 로고
    • Handle with care: Targeting neutrophils in chronic obstructive pulmonary disease and severe asthma?
    • Beeh, K. M., and J. Beier. 2006. Handle with care: targeting neutrophils in chronic obstructive pulmonary disease and severe asthma? Clin. Exp. Allergy 36:142-157.
    • (2006) Clin. Exp. Allergy , vol.36 , pp. 142-157
    • Beeh, K.M.1    Beier, J.2
  • 15
    • 0034739437 scopus 로고    scopus 로고
    • The antibacterial properties of secreted phospholipases A(2)
    • Buckland, A. G., and D. C. Wilton. 2000. The antibacterial properties of secreted phospholipases A(2). Biochim. Biophys. Acta 1488:71-82.
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 71-82
    • Buckland, A.G.1    Wilton, D.C.2
  • 17
    • 0037378123 scopus 로고    scopus 로고
    • Unique structural features that influence neutrophil emigration into the lung
    • Burns, A. R., C. W. Smith, and D. C. Walker. 2003. Unique structural features that influence neutrophil emigration into the lung. Physiol. Rev. 83:309-336.
    • (2003) Physiol. Rev , vol.83 , pp. 309-336
    • Burns, A.R.1    Smith, C.W.2    Walker, D.C.3
  • 18
    • 0037771393 scopus 로고    scopus 로고
    • Inhibitory effects of surfactant protein A on surfactant phospholipid hydrolysis by secreted phospholipases A2
    • Chabot, S., K. Koumanov, G. Lambeau, M. H. Gelb, V. Balloy, M. Chignard, J. A. Whitsett, and L. Touqui. 2003. Inhibitory effects of surfactant protein A on surfactant phospholipid hydrolysis by secreted phospholipases A2. J. Immunol. 171:995-1000.
    • (2003) J. Immunol , vol.171 , pp. 995-1000
    • Chabot, S.1    Koumanov, K.2    Lambeau, G.3    Gelb, M.H.4    Balloy, V.5    Chignard, M.6    Whitsett, J.A.7    Touqui, L.8
  • 19
    • 0034666290 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities
    • Chen, J. W., C. Dodia, S. I. Feinstein, M. K. Jain, and A. B. Fisher. 2000. 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. J. Biol. Chem. 275:28421- 28427.
    • (2000) J. Biol. Chem , vol.275 , pp. 28421-28427
    • Chen, J.W.1    Dodia, C.2    Feinstein, S.I.3    Jain, M.K.4    Fisher, A.B.5
  • 20
    • 2942737134 scopus 로고    scopus 로고
    • Rac and protein kinase C-δ regulate ERKs and cytosolic phospholipase A2 in FcεRI signaling to cysteinyl leukotriene synthesis in mast cells
    • Cho, S. H., H. J. You, C. H. Woo, Y. J. Yoo, and J. H. Kim. 2004. Rac and protein kinase C-δ regulate ERKs and cytosolic phospholipase A2 in FcεRI signaling to cysteinyl leukotriene synthesis in mast cells. J. Immunol. 173: 624-631.
    • (2004) J. Immunol , vol.173 , pp. 624-631
    • Cho, S.H.1    You, H.J.2    Woo, C.H.3    Yoo, Y.J.4    Kim, J.H.5
  • 22
    • 33745590720 scopus 로고    scopus 로고
    • The type III pseudomonal exotoxin U activates the c-Jun NH2-terminal kinase pathway and increases human epithelial interleukin-8 production
    • Cuzick, A., F. R. Stirling, S. L. Lindsay, and T. J. Evans. 2006. The type III pseudomonal exotoxin U activates the c-Jun NH2-terminal kinase pathway and increases human epithelial interleukin-8 production. Infect. Immun. 74:4104-4113.
    • (2006) Infect. Immun , vol.74 , pp. 4104-4113
    • Cuzick, A.1    Stirling, F.R.2    Lindsay, S.L.3    Evans, T.J.4
  • 24
    • 1542644985 scopus 로고    scopus 로고
    • Bactericidal properties of group IIa secreted phospholipase A(2) against Pseudomonas aeruginosa clinical isolates
    • Dubouix, A., C. Campanac, J. Fauvel, M. F. Simon, J. P. Salles, C. Roques, H. Chap, and N. Marty. 2003. Bactericidal properties of group IIa secreted phospholipase A(2) against Pseudomonas aeruginosa clinical isolates. J. Med. Microbiol. 52:1039-1045.
    • (2003) J. Med. Microbiol , vol.52 , pp. 1039-1045
    • Dubouix, A.1    Campanac, C.2    Fauvel, J.3    Simon, M.F.4    Salles, J.P.5    Roques, C.6    Chap, H.7    Marty, N.8
  • 25
    • 33746290411 scopus 로고    scopus 로고
    • Analysis of expression of secreted phospholipases A2 in mouse tissues at protein and mRNA levels
    • Eerola, L. I., F. Surrel, T. J. Nevalainen, M. H. Gelb, G. Lambeau, and V. J. Laine. 2006. Analysis of expression of secreted phospholipases A2 in mouse tissues at protein and mRNA levels. Biochim. Biophys. Acta 1761:745-756.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 745-756
    • Eerola, L.I.1    Surrel, F.2    Nevalainen, T.J.3    Gelb, M.H.4    Lambeau, G.5    Laine, V.J.6
  • 26
    • 0031065987 scopus 로고    scopus 로고
    • Role of acidic Ca2+-independent phospholipase A2 in synthesis of lung dipalmitoyl phosphatidylcholine
    • Fisher, A. B., and C. Dodia. 1997. Role of acidic Ca2+-independent phospholipase A2 in synthesis of lung dipalmitoyl phosphatidylcholine. Am. J. Physiol. 272:L238-L243.
    • (1997) Am. J. Physiol , vol.272
    • Fisher, A.B.1    Dodia, C.2
  • 27
    • 33746769448 scopus 로고    scopus 로고
    • Lung phospholipid metabolism in transgenic mice overexpressing peroxiredoxin 6
    • Fisher, A. B., C. Dodia, K. Yu, Y. Manevich, and S. I. Feinstein. 2006. Lung phospholipid metabolism in transgenic mice overexpressing peroxiredoxin 6. Biochim. Biophys. Acta 1761:785-792.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 785-792
    • Fisher, A.B.1    Dodia, C.2    Yu, K.3    Manevich, Y.4    Feinstein, S.I.5
  • 28
    • 24944523382 scopus 로고    scopus 로고
    • Altered lung phospholipid metabolism in mice with targeted deletion of lysosomal-type phospholipase A2
    • Fisher, A. B., C. Dodia, S. I. Feinstein, and Y. S. Ho. 2005. Altered lung phospholipid metabolism in mice with targeted deletion of lysosomal-type phospholipase A2. J. Lipid Res. 46:1248-1256.
    • (2005) J. Lipid Res , vol.46 , pp. 1248-1256
    • Fisher, A.B.1    Dodia, C.2    Feinstein, S.I.3    Ho, Y.S.4
  • 29
    • 0036840406 scopus 로고    scopus 로고
    • Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine
    • Flieger, A., B. Neumeister, and N. P. Cianciotto. 2002. Characterization of the gene encoding the major secreted lysophospholipase A of Legionella pneumophila and its role in detoxification of lysophosphatidylcholine. Infect. Immun. 70:6094-6106.
    • (2002) Infect. Immun , vol.70 , pp. 6094-6106
    • Flieger, A.1    Neumeister, B.2    Cianciotto, N.P.3
  • 30
    • 2142707243 scopus 로고    scopus 로고
    • Cloning and characterization of the gene encoding the major cell-associated phospholipase A of Legionella pneumophila, plaB, exhibiting hemolytic activity
    • Flieger, A., K. Rydzewski, S. Banerji, M. Broich, and K. Heuner. 2004. Cloning and characterization of the gene encoding the major cell-associated phospholipase A of Legionella pneumophila, plaB, exhibiting hemolytic activity. Infect. Immun. 72:2648-2658.
    • (2004) Infect. Immun , vol.72 , pp. 2648-2658
    • Flieger, A.1    Rydzewski, K.2    Banerji, S.3    Broich, M.4    Heuner, K.5
  • 32
    • 0031689398 scopus 로고    scopus 로고
    • Mechanisms that account for the selective release of arachidonic acid from intact cells by secretory phospholipase A2
    • Fonteh, A. N., J. M. Samet, M. Surette, W. Reed, and F. H. Chilton. 1998. Mechanisms that account for the selective release of arachidonic acid from intact cells by secretory phospholipase A2. Biochim. Biophys. Acta 1393: 253-266.
    • (1998) Biochim. Biophys. Acta , vol.1393 , pp. 253-266
    • Fonteh, A.N.1    Samet, J.M.2    Surette, M.3    Reed, W.4    Chilton, F.H.5
  • 34
    • 33745220978 scopus 로고    scopus 로고
    • Identification of the expressed form of human cytosolic phospholipase A2β (cPLA2β): CPLA2β 3 is a novel variant localized to mitochondria and early endosomes
    • Ghosh, M., R. Loper, M. H. Gelb, and C. C. Leslie. 2006. Identification of the expressed form of human cytosolic phospholipase A2β (cPLA2β): cPLA2β 3 is a novel variant localized to mitochondria and early endosomes. J. Biol. Chem. 281:16615-16624.
    • (2006) J. Biol. Chem , vol.281 , pp. 16615-16624
    • Ghosh, M.1    Loper, R.2    Gelb, M.H.3    Leslie, C.C.4
  • 35
    • 1542283687 scopus 로고    scopus 로고
    • A novel role for phospholipase A2 isoforms in the checkpoint control of acute inflammation
    • Gilroy, D. W., J. Newson, P. Sawmynaden, D. A. Willoughby, and J. D. Croxtall. 2004. A novel role for phospholipase A2 isoforms in the checkpoint control of acute inflammation. FASEB J. 18:489-498.
    • (2004) FASEB J , vol.18 , pp. 489-498
    • Gilroy, D.W.1    Newson, J.2    Sawmynaden, P.3    Willoughby, D.A.4    Croxtall, J.D.5
  • 36
    • 2942702104 scopus 로고    scopus 로고
    • High bactericidal efficiency of type IIa phospholipase A2 against Bacillus anthracis and inhibition of its secretion by the lethal toxin
    • Gimenez, A. P., Y. Z. Wu, M. Paya, C. Delclaux, L. Touqui, and P. L. Goossens. 2004. High bactericidal efficiency of type IIa phospholipase A2 against Bacillus anthracis and inhibition of its secretion by the lethal toxin. J. Immunol. 173:521-530.
    • (2004) J. Immunol , vol.173 , pp. 521-530
    • Gimenez, A.P.1    Wu, Y.Z.2    Paya, M.3    Delclaux, C.4    Touqui, L.5    Goossens, P.L.6
  • 37
    • 33748465176 scopus 로고    scopus 로고
    • The proinflammatory mediator Platelet Activating Factor is an effective substrate for human group X secreted phospholipase A2
    • Gora, S., G. Lambeau, J. G. Bollinger, M. Gelb, E. Ninio, and S. A. Karabina. 2006. The proinflammatory mediator Platelet Activating Factor is an effective substrate for human group X secreted phospholipase A2. Biochim. Biophys. Acta 1761:1093-1099.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1093-1099
    • Gora, S.1    Lambeau, G.2    Bollinger, J.G.3    Gelb, M.4    Ninio, E.5    Karabina, S.A.6
  • 38
    • 33746238519 scopus 로고    scopus 로고
    • Signaling events involved in cytokine and chemokine production induced by secretory phospholipase A2 in human lung macrophages
    • Granata, F., A. Frattini, S. Loffredo, A. Del Prete, S. Sozzani, G. Marone, and M. Triggiani. 2006. Signaling events involved in cytokine and chemokine production induced by secretory phospholipase A2 in human lung macrophages. Eur. J. Immunol. 36:1938-1950.
    • (2006) Eur. J. Immunol , vol.36 , pp. 1938-1950
    • Granata, F.1    Frattini, A.2    Loffredo, S.3    Del Prete, A.4    Sozzani, S.5    Marone, G.6    Triggiani, M.7
  • 40
    • 0037350247 scopus 로고    scopus 로고
    • Platelet-activating factor acetylhydrolase is increased in lung lavage fluid from patients with acute respiratory distress syndrome
    • Grissom, C. K., J. F. Orme, Jr., L. D. Richer, T. M. McIntyre, G. A. Zimmerman, and M. R. Elstad. 2003. Platelet-activating factor acetylhydrolase is increased in lung lavage fluid from patients with acute respiratory distress syndrome. Crit. Care Med. 31:770-775.
    • (2003) Crit. Care Med , vol.31 , pp. 770-775
    • Grissom, C.K.1    Orme Jr., J.F.2    Richer, L.D.3    McIntyre, T.M.4    Zimmerman, G.A.5    Elstad, M.R.6
  • 41
    • 0037097770 scopus 로고    scopus 로고
    • Bactericidal group IIA phospholipase A2 in serum of patients with bacterial infections
    • Gronroos, J. O., V. J. Laine, and T. J. Nevalainen. 2002. Bactericidal group IIA phospholipase A2 in serum of patients with bacterial infections. J. Infect. Dis. 185:1767-1772.
    • (2002) J. Infect. Dis , vol.185 , pp. 1767-1772
    • Gronroos, J.O.1    Laine, V.J.2    Nevalainen, T.J.3
  • 43
    • 0036669794 scopus 로고    scopus 로고
    • Phospholipase A2 receptor: A regulator of biological functions of secretory phospholipase A2
    • Hanasaki, K., and H. Arita. 2002. Phospholipase A2 receptor: a regulator of biological functions of secretory phospholipase A2. Prostaglandins Other Lipid Mediat. 68-69:71-82.
    • (2002) Prostaglandins Other Lipid Mediat , vol.68-69 , pp. 71-82
    • Hanasaki, K.1    Arita, H.2
  • 46
    • 0343484308 scopus 로고    scopus 로고
    • Recombinant human platelet-activating factor-acetylhydrolase inhibits airway inflammation and hyperreactivity in mouse asthma model
    • Henderson, W. R., Jr., J. Lu, K. M. Poole, G. N. Dietsch, and E. Y. Chi. 2000. Recombinant human platelet-activating factor-acetylhydrolase inhibits airway inflammation and hyperreactivity in mouse asthma model. J. Immunol. 164:3360-3367.
    • (2000) J. Immunol , vol.164 , pp. 3360-3367
    • Henderson Jr., W.R.1    Lu, J.2    Poole, K.M.3    Dietsch, G.N.4    Chi, E.Y.5
  • 47
    • 0033841610 scopus 로고    scopus 로고
    • Henig, N. R., M. L. Aitken, M. C. Liu, A. S. Yu, and W. R. Henderson, Jr. 2000. Effect of recombinant human platelet-activating factor-acetylhydrolase on allergen-induced asthmatic responses. Am. J. Respir. Crit. Care Med. 162:523-527.
    • Henig, N. R., M. L. Aitken, M. C. Liu, A. S. Yu, and W. R. Henderson, Jr. 2000. Effect of recombinant human platelet-activating factor-acetylhydrolase on allergen-induced asthmatic responses. Am. J. Respir. Crit. Care Med. 162:523-527.
  • 48
    • 0037155846 scopus 로고    scopus 로고
    • Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase
    • Hiraoka, M., A. Abe, and J. A. Shayman. 2002. Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase. J. Biol. Chem. 277:10090-10099.
    • (2002) J. Biol. Chem , vol.277 , pp. 10090-10099
    • Hiraoka, M.1    Abe, A.2    Shayman, J.A.3
  • 51
    • 32044435823 scopus 로고    scopus 로고
    • Lysophospholipid and fatty acid inhibition of pulmonary surfactant: Non-enzymatic models of phospholipase A2 surfactant hydrolysis
    • Hite, R. D., M. C. Seeds, R. B. Jacinto, B. L. Grier, B. M. Waite, and D. A. Bass. 2005. Lysophospholipid and fatty acid inhibition of pulmonary surfactant: non-enzymatic models of phospholipase A2 surfactant hydrolysis. Biochim. Biophys. Acta 1720:14-21.
    • (2005) Biochim. Biophys. Acta , vol.1720 , pp. 14-21
    • Hite, R.D.1    Seeds, M.C.2    Jacinto, R.B.3    Grier, B.L.4    Waite, B.M.5    Bass, D.A.6
  • 52
    • 17344363135 scopus 로고    scopus 로고
    • Hydrolysis of surfactant-associated phosphatidylcholine by mammalian secretory phospholipases A2
    • Hite, R. D., M. C. Seeds, R. B. Jacinto, R. Balasubramanian, M. Waite, and D. Bass. 1998. Hydrolysis of surfactant-associated phosphatidylcholine by mammalian secretory phospholipases A2. Am. J. Physiol. 275:L740-L747.
    • (1998) Am. J. Physiol , vol.275
    • Hite, R.D.1    Seeds, M.C.2    Jacinto, R.B.3    Balasubramanian, R.4    Waite, M.5    Bass, D.6
  • 53
    • 33646540772 scopus 로고    scopus 로고
    • Involvement of phospholipase A2 in Pseudomonas aeruginosa-mediated PMN transepithelial migration
    • Hurley, B. P., N. L. Williams, and B. A. McCormick. 2006. Involvement of phospholipase A2 in Pseudomonas aeruginosa-mediated PMN transepithelial migration. Am. J. Physiol. Lung Cell Mol. Physiol. 290:L703-L709.
    • (2006) Am. J. Physiol. Lung Cell Mol. Physiol , vol.290
    • Hurley, B.P.1    Williams, N.L.2    McCormick, B.A.3
  • 54
    • 0032513056 scopus 로고    scopus 로고
    • Characterization of a mammalian peroxiredoxin that contains one conserved cysteine
    • Kang, S. W., I. C. Baines, and S. G. Rhee. 1998. Characterization of a mammalian peroxiredoxin that contains one conserved cysteine. J. Biol. Chem. 273:6303-6311.
    • (1998) J. Biol. Chem , vol.273 , pp. 6303-6311
    • Kang, S.W.1    Baines, I.C.2    Rhee, S.G.3
  • 55
    • 33750943178 scopus 로고    scopus 로고
    • Clinical aspects of plasma platelet-activating factoracetylhydrolase
    • Karasawa, K. 2006. Clinical aspects of plasma platelet-activating factoracetylhydrolase. Biochim. Biophys. Acta 1761:1359-1372.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1359-1372
    • Karasawa, K.1
  • 56
    • 14444284835 scopus 로고    scopus 로고
    • Kim, T. S., C. S. Sundaresh, S. I. Feinstein, C. Dodia, W. R. Skach, M. K. Jain, T. Nagase, N. Seki, K. Ishikawa, N. Nomura, and A. B. Fisher. 1997. Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein. J. Biol. Chem. 272:2542-2550. (Erratum, 272:10981.)
    • Kim, T. S., C. S. Sundaresh, S. I. Feinstein, C. Dodia, W. R. Skach, M. K. Jain, T. Nagase, N. Seki, K. Ishikawa, N. Nomura, and A. B. Fisher. 1997. Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein. J. Biol. Chem. 272:2542-2550. (Erratum, 272:10981.)
  • 57
    • 0037184110 scopus 로고    scopus 로고
    • Group V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2
    • Kim, Y. J., K. P. Kim, S. K. Han, N. M. Munoz, X. Zhu, H. Sano, A. R. Leff, and W. Cho. 2002. Group V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2. J. Biol. Chem. 277:36479-36488.
    • (2002) J. Biol. Chem , vol.277 , pp. 36479-36488
    • Kim, Y.J.1    Kim, K.P.2    Han, S.K.3    Munoz, N.M.4    Zhu, X.5    Sano, H.6    Leff, A.R.7    Cho, W.8
  • 58
    • 31844435408 scopus 로고    scopus 로고
    • Phospholipase A2 functions in Pseudomonas aeruginosa-induced apoptosis
    • Kirschnek, S., and E. Gulbins. 2006. Phospholipase A2 functions in Pseudomonas aeruginosa-induced apoptosis. Infect. Immun. 74:850-860.
    • (2006) Infect. Immun , vol.74 , pp. 850-860
    • Kirschnek, S.1    Gulbins, E.2
  • 59
    • 0037155144 scopus 로고    scopus 로고
    • Koduri, R. S., J. O. Gronroos, V. J. Laine, C. Le Calvez, G. Lambeau, T. J. Nevalainen, and M. H. Gelb. 2002. Bactericidal properties of human and murine groups I, II, V, X, and XII secreted phospholipases A(2). J. Biol. Chem. 277:5849-5857.
    • Koduri, R. S., J. O. Gronroos, V. J. Laine, C. Le Calvez, G. Lambeau, T. J. Nevalainen, and M. H. Gelb. 2002. Bactericidal properties of human and murine groups I, II, V, X, and XII secreted phospholipases A(2). J. Biol. Chem. 277:5849-5857.
  • 60
    • 0033830031 scopus 로고    scopus 로고
    • Neutrophil response of transgenic mice expressing human group IIA phospholipase A2 in bacterial infections
    • Laine, V. J., A. Rajamaki, D. S. Grass, and T. J. Nevalainen. 2000. Neutrophil response of transgenic mice expressing human group IIA phospholipase A2 in bacterial infections. Scand. J. Immunol. 52:362-368.
    • (2000) Scand. J. Immunol , vol.52 , pp. 362-368
    • Laine, V.J.1    Rajamaki, A.2    Grass, D.S.3    Nevalainen, T.J.4
  • 61
    • 0033564947 scopus 로고    scopus 로고
    • Protection by group II phospholipase A2 against Staphylococcus aureus
    • Laine, V. J., D. S. Grass, and T. J. Nevalainen. 1999. Protection by group II phospholipase A2 against Staphylococcus aureus. J. Immunol. 162:7402-7408.
    • (1999) J. Immunol , vol.162 , pp. 7402-7408
    • Laine, V.J.1    Grass, D.S.2    Nevalainen, T.J.3
  • 62
    • 0033966028 scopus 로고    scopus 로고
    • Resistance of transgenic mice expressing human group II phospholipase A2 to Escherichia coli infection
    • Laine, V. J., D. S. Grass, and T. J. Nevalainen. 2000. Resistance of transgenic mice expressing human group II phospholipase A2 to Escherichia coli infection. Infect. Immun. 68:87-92.
    • (2000) Infect. Immun , vol.68 , pp. 87-92
    • Laine, V.J.1    Grass, D.S.2    Nevalainen, T.J.3
  • 64
    • 15944415469 scopus 로고    scopus 로고
    • Diversity of asthma: Evolving concepts of pathophysiology and lessons from genetics
    • Lilly, C. M. 2005. Diversity of asthma: evolving concepts of pathophysiology and lessons from genetics. J. Allergy Clin. Immunol. 115(Suppl. 4):S526-S531.
    • (2005) J. Allergy Clin. Immunol , vol.115 , Issue.SUPPL. 4
    • Lilly, C.M.1
  • 65
    • 0034909701 scopus 로고    scopus 로고
    • Expression of members of the phospholipase A2 family of enzymes in human nasal mucosa
    • Lindbom, J., A. G. Ljungman, M. Lindahl, and C. Tagesson. 2001. Expression of members of the phospholipase A2 family of enzymes in human nasal mucosa. Eur. Respir. J. 18:130-138.
    • (2001) Eur. Respir. J , vol.18 , pp. 130-138
    • Lindbom, J.1    Ljungman, A.G.2    Lindahl, M.3    Tagesson, C.4
  • 66
    • 0036396071 scopus 로고    scopus 로고
    • Increased gene expression of novel cytosolic and secretory phospholipase A(2) types in human airway epithelial cells induced by tumor necrosis factor-α and IFN-γ
    • Lindbom, J., A. G. Ljungman, M. Lindahl, and C. Tagesson. 2002. Increased gene expression of novel cytosolic and secretory phospholipase A(2) types in human airway epithelial cells induced by tumor necrosis factor-α and IFN-γ. J. Interferon Cytokine Res. 22:947-955.
    • (2002) J. Interferon Cytokine Res , vol.22 , pp. 947-955
    • Lindbom, J.1    Ljungman, A.G.2    Lindahl, M.3    Tagesson, C.4
  • 67
    • 0029943699 scopus 로고    scopus 로고
    • Endotoxin stimulates the expression of group II PLA2 in rat lung in vivo and in isolated perfused lungs
    • Ljungman, A. G., C. Tagesson, and M. Lindahl. 1996. Endotoxin stimulates the expression of group II PLA2 in rat lung in vivo and in isolated perfused lungs. Am. J. Physiol. 270:L752-L760.
    • (1996) Am. J. Physiol , vol.270
    • Ljungman, A.G.1    Tagesson, C.2    Lindahl, M.3
  • 68
    • 34047150002 scopus 로고    scopus 로고
    • Activation of cytosolic phospholipase A2 and 15-lipoxygenase by oxidized low-density lipoproteins in cultured human lung fibroblasts
    • Lupo, G., C. D. Anfuso, N. Ragusa, C. Tirolo, B. Marchetti, E. Gili, C. La Rosa, and C. Vancheri. 2007. Activation of cytosolic phospholipase A2 and 15-lipoxygenase by oxidized low-density lipoproteins in cultured human lung fibroblasts. Biochim. Biophys. Acta 1771:522-532.
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 522-532
    • Lupo, G.1    Anfuso, C.D.2    Ragusa, N.3    Tirolo, C.4    Marchetti, B.5    Gili, E.6    La Rosa, C.7    Vancheri, C.8
  • 69
    • 0036225688 scopus 로고    scopus 로고
    • Lung infections associated with cystic fibrosis
    • Lyczak, J. B., C. L. Cannon, and G. B. Pier. 2002. Lung infections associated with cystic fibrosis. Clin. Microbiol. Rev. 15:194-222.
    • (2002) Clin. Microbiol. Rev , vol.15 , pp. 194-222
    • Lyczak, J.B.1    Cannon, C.L.2    Pier, G.B.3
  • 70
    • 4143146273 scopus 로고    scopus 로고
    • Leptin augments alveolar macrophage leukotriene synthesis by increasing phospholipase activity and enhancing group IVC iPLA2 (cPLA2γ) protein expression
    • Mancuso, P., C. Canetti, A. Gottschalk, P. K. Tithof, and M. Peters-Golden. 2004. Leptin augments alveolar macrophage leukotriene synthesis by increasing phospholipase activity and enhancing group IVC iPLA2 (cPLA2γ) protein expression. Am. J. Physiol. Lung Cell Mol. Physiol. 287:L497-L502.
    • (2004) Am. J. Physiol. Lung Cell Mol. Physiol , vol.287
    • Mancuso, P.1    Canetti, C.2    Gottschalk, A.3    Tithof, P.K.4    Peters-Golden, M.5
  • 71
    • 18844400905 scopus 로고    scopus 로고
    • Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism
    • Manevich, Y., and A. B. Fisher. 2005. Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radic. Biol. Med. 38:1422-1432.
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 1422-1432
    • Manevich, Y.1    Fisher, A.B.2
  • 72
    • 17144363202 scopus 로고    scopus 로고
    • Expression of secretory phospholipase A2 enzymes in lungs of humans with pneumonia and their potential prostaglandinsynthetic function in human lung-derived cells
    • Masuda, S., M. Murakami, M. Mitsuishi, K. Komiyama, Y. Ishikawa, T. Ishii, and I. Kudo. 2005. Expression of secretory phospholipase A2 enzymes in lungs of humans with pneumonia and their potential prostaglandinsynthetic function in human lung-derived cells. Biochem. J. 387:27-38.
    • (2005) Biochem. J , vol.387 , pp. 27-38
    • Masuda, S.1    Murakami, M.2    Mitsuishi, M.3    Komiyama, K.4    Ishikawa, Y.5    Ishii, T.6    Kudo, I.7
  • 73
    • 0037034267 scopus 로고    scopus 로고
    • Community-acquired pneumonia in children
    • McIntosh, K. 2002. Community-acquired pneumonia in children. N. Engl. J. Med. 346:429-437.
    • (2002) N. Engl. J. Med , vol.346 , pp. 429-437
    • McIntosh, K.1
  • 74
    • 0141668951 scopus 로고    scopus 로고
    • Effector ExoU from the type III secretion system is an important modulator of gene expression in lung epithelial cells in response to Pseudomonas aeruginosa infection
    • McMorran, B., L. Town, E. Costelloe, J. Palmer, J. Engel, D. Hume, and B. Wainwright. 2003. Effector ExoU from the type III secretion system is an important modulator of gene expression in lung epithelial cells in response to Pseudomonas aeruginosa infection. Infect. Immun. 71:6035-6044.
    • (2003) Infect. Immun , vol.71 , pp. 6035-6044
    • McMorran, B.1    Town, L.2    Costelloe, E.3    Palmer, J.4    Engel, J.5    Hume, D.6    Wainwright, B.7
  • 75
    • 27144514336 scopus 로고    scopus 로고
    • Impact of CFTR DeltaF508 mutation on prostaglandin E2 production and type IIA phospholipase A2 expression by pulmonary epithelial cells
    • Medjane, S., B. Raymond, Y. Wu, and L. Touqui. 2005. Impact of CFTR DeltaF508 mutation on prostaglandin E2 production and type IIA phospholipase A2 expression by pulmonary epithelial cells. Am. J. Physiol. Lung Cell Mol. Physiol. 289:L816-L824.
    • (2005) Am. J. Physiol. Lung Cell Mol. Physiol , vol.289
    • Medjane, S.1    Raymond, B.2    Wu, Y.3    Touqui, L.4
  • 76
    • 0036177378 scopus 로고    scopus 로고
    • Clinical review: A paradigm shift: the bidirectional effect of inflammation on bacterial growth. Clinical implications for patients with acute respiratory distress syndrome
    • Meduri, G. U. 2002. Clinical review: a paradigm shift: the bidirectional effect of inflammation on bacterial growth. Clinical implications for patients with acute respiratory distress syndrome. Crit. Care 6:24-29.
    • (2002) Crit. Care , vol.6 , pp. 24-29
    • Meduri, G.U.1
  • 77
    • 33745298938 scopus 로고    scopus 로고
    • Transcellular secretion of group V phospholipase A2 from epithelium induces beta 2-integrin-mediated adhesion and synthesis of leukotriene C4 in eosinophils
    • Munoz, N. M., A. Y. Meliton, A. Lambertino, E. Boetticher, J. Learoyd, F. Sultan, X. Zhu, W. Cho, and A. R. Leff. 2006. Transcellular secretion of group V phospholipase A2 from epithelium induces beta 2-integrin-mediated adhesion and synthesis of leukotriene C4 in eosinophils. J. Immunol. 177:574-582.
    • (2006) J. Immunol , vol.177 , pp. 574-582
    • Munoz, N.M.1    Meliton, A.Y.2    Lambertino, A.3    Boetticher, E.4    Learoyd, J.5    Sultan, F.6    Zhu, X.7    Cho, W.8    Leff, A.R.9
  • 78
    • 49449112039 scopus 로고    scopus 로고
    • Deletion of secretory group V phospholipase A2 attenuates cell migration and airway hyperresponsiveness in immunosensitized mice
    • Munoz, N. M., A. Y. Meliton, J. P Arm, J. V. Bonventre, W. Cho, and A. R. Leff. 2007. Deletion of secretory group V phospholipase A2 attenuates cell migration and airway hyperresponsiveness in immunosensitized mice. J. Immunol. 179:4800-4807.
    • (2007) J. Immunol , vol.179 , pp. 4800-4807
    • Munoz, N.M.1    Meliton, A.Y.2    Arm, J.P.3    Bonventre, J.V.4    Cho, W.5    Leff, A.R.6
  • 80
    • 7044237564 scopus 로고    scopus 로고
    • Secretory phospholipase A2
    • Murakami, M., and I. Kudo. 2004. Secretory phospholipase A2. Biol. Pharm. Bull. 27:1158-1164.
    • (2004) Biol. Pharm. Bull , vol.27 , pp. 1158-1164
    • Murakami, M.1    Kudo, I.2
  • 83
    • 0034232013 scopus 로고    scopus 로고
    • Acute lung injury by sepsis and acid aspiration: A key role for cytosolic phospholipase A2
    • Nagase, T., N. Uozumi, S. Ishii, K. Kume, T. Izumi, Y. Ouchi, and T. Shimizu. 2000. Acute lung injury by sepsis and acid aspiration: a key role for cytosolic phospholipase A2. Nat. Immunol. 1:42-46.
    • (2000) Nat. Immunol , vol.1 , pp. 42-46
    • Nagase, T.1    Uozumi, N.2    Ishii, S.3    Kume, K.4    Izumi, T.5    Ouchi, Y.6    Shimizu, T.7
  • 85
    • 17044375549 scopus 로고    scopus 로고
    • Phospholipases A2 and platelet-activating-factor acetylhydrolase in patients with acute respiratory distress syndrome
    • Nakos, G., E. Kitsiouli, E. Hatzidaki, V. Koulouras, L. Touqui, and M. E. Lekka. 2005. Phospholipases A2 and platelet-activating-factor acetylhydrolase in patients with acute respiratory distress syndrome. Crit. Care Med. 33:772-779.
    • (2005) Crit. Care Med , vol.33 , pp. 772-779
    • Nakos, G.1    Kitsiouli, E.2    Hatzidaki, E.3    Koulouras, V.4    Touqui, L.5    Lekka, M.E.6
  • 88
    • 33846250034 scopus 로고    scopus 로고
    • Secretory phospholipases A2 stimulate mucus secretion, induce airway inflammation, and produce secretory hyperresponsiveness to neutrophil elastase in ferret trachea
    • Okamoto, K., J. S. Kim, and B. K. Rubin. 2007. Secretory phospholipases A2 stimulate mucus secretion, induce airway inflammation, and produce secretory hyperresponsiveness to neutrophil elastase in ferret trachea. Am. J. Physiol. Lung Cell Mol. Physiol. 292:L62-L67.
    • (2007) Am. J. Physiol. Lung Cell Mol. Physiol , vol.292
    • Okamoto, K.1    Kim, J.S.2    Rubin, B.K.3
  • 89
    • 10744219506 scopus 로고    scopus 로고
    • Opal, S., P. F. Laterre, E. Abraham, B. Francois, X. Wittebole, S. Lowry, J. F. Dhainaut, B. Warren, T. Dugernier, A. Lopez, M. Sanchez, I. Demeyer, L. Jauregui, J. A. Lorente, W. McGee, K. Reinhart, S. Kljucar, S. Souza, J. Pribble, et al. 2004. Recombinant human platelet-activating factor acetylhydrolase for treatment of severe sepsis: results of a phase III, multicenter, randomized, double-blind, placebo-controlled, clinical trial. Crit. Care Med. 32:332-341.
    • Opal, S., P. F. Laterre, E. Abraham, B. Francois, X. Wittebole, S. Lowry, J. F. Dhainaut, B. Warren, T. Dugernier, A. Lopez, M. Sanchez, I. Demeyer, L. Jauregui, J. A. Lorente, W. McGee, K. Reinhart, S. Kljucar, S. Souza, J. Pribble, et al. 2004. Recombinant human platelet-activating factor acetylhydrolase for treatment of severe sepsis: results of a phase III, multicenter, randomized, double-blind, placebo-controlled, clinical trial. Crit. Care Med. 32:332-341.
  • 90
    • 8544233545 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa causes acute lung injury via the catalytic activity of the patatin-like phospholipase domain of ExoU
    • Pankhaniya, R. R., M. Tamura, L. R. Allmond, K. Moriyama, T. Ajayi, J. P. Wiener-Kronish, and T. Sawa. 2004. Pseudomonas aeruginosa causes acute lung injury via the catalytic activity of the patatin-like phospholipase domain of ExoU. Crit. Care Med. 32:2293-2299.
    • (2004) Crit. Care Med , vol.32 , pp. 2293-2299
    • Pankhaniya, R.R.1    Tamura, M.2    Allmond, L.R.3    Moriyama, K.4    Ajayi, T.5    Wiener-Kronish, J.P.6    Sawa, T.7
  • 91
    • 0037031820 scopus 로고    scopus 로고
    • 85-kDa cytosolic phospholipase A2 mediates peroxisome proliferator-activated receptor γ activation in human lung epithelial cells
    • Pawliczak, R., C. Han, X. L. Huang, A. J. Demetris, J. H. Shelhamer, and T. Wu. 2002. 85-kDa cytosolic phospholipase A2 mediates peroxisome proliferator-activated receptor γ activation in human lung epithelial cells. J. Biol. Chem. 277:33153-33163.
    • (2002) J. Biol. Chem , vol.277 , pp. 33153-33163
    • Pawliczak, R.1    Han, C.2    Huang, X.L.3    Demetris, A.J.4    Shelhamer, J.H.5    Wu, T.6
  • 92
    • 10344233226 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 Group IVα but not secreted phospholipase A2 Group IIA, V, or X induces interleukin-8 and cyclooxygenase-2 gene and protein expression through peroxisome proliferator-activated receptors γ 1 and 2 in human lung cells
    • Pawliczak, R., C. Logun, P. Madara, M. Lawrence, G. Woszczek, A. Ptasinska, M. L. Kowalski, T. Wu, and J. H. Shelhamer. 2004. Cytosolic phospholipase A2 Group IVα but not secreted phospholipase A2 Group IIA, V, or X induces interleukin-8 and cyclooxygenase-2 gene and protein expression through peroxisome proliferator-activated receptors γ 1 and 2 in human lung cells. J. Biol. Chem. 279:48550-48561.
    • (2004) J. Biol. Chem , vol.279 , pp. 48550-48561
    • Pawliczak, R.1    Logun, C.2    Madara, P.3    Lawrence, M.4    Woszczek, G.5    Ptasinska, A.6    Kowalski, M.L.7    Wu, T.8    Shelhamer, J.H.9
  • 93
    • 0036890753 scopus 로고    scopus 로고
    • Oxidative stress induces arachidonate release from human lung cells through the epithelial growth factor receptor pathway
    • Pawliczak, R., X. L. Huang, U. B. Nanavaty, M. Lawrence, P. Madara, and J. H. Shelhamer. 2002. Oxidative stress induces arachidonate release from human lung cells through the epithelial growth factor receptor pathway. Am. J. Respir. Cell Mol. Biol. 27:722-731.
    • (2002) Am. J. Respir. Cell Mol. Biol , vol.27 , pp. 722-731
    • Pawliczak, R.1    Huang, X.L.2    Nanavaty, U.B.3    Lawrence, M.4    Madara, P.5    Shelhamer, J.H.6
  • 95
    • 0142135037 scopus 로고    scopus 로고
    • In vivo phospholipase activity of the Pseudomonas aeruginosa cytotoxin ExoU and protection of mammalian cells with phospholipase A2 inhibitors
    • Phillips, R. M., D. A. Six, E. A. Dennis, and P. Ghosh. 2003. In vivo phospholipase activity of the Pseudomonas aeruginosa cytotoxin ExoU and protection of mammalian cells with phospholipase A2 inhibitors. J. Biol. Chem. 278:41326-41332.
    • (2003) J. Biol. Chem , vol.278 , pp. 41326-41332
    • Phillips, R.M.1    Six, D.A.2    Dennis, E.A.3    Ghosh, P.4
  • 96
  • 98
    • 20044362184 scopus 로고    scopus 로고
    • Rubin, B. B., G. P. Downey, A. Koh, N. Degousee, F. Ghomashchi, L. Nallan, E. Stefanski, D. W. Harkin, C. Sun, B. P. Smart, T. F. Lindsay, V. Cherepanov, E. Vachon, D. Kelvin, M. Sadilek, G. E. Brown, M. B. Yaffe, J. Plumb, S. Grinstein, M. Glogauer, and M. H. Gelb. 2005. Cytosolic phospholipase A2-α is necessary for platelet-activating factor biosynthesis, efficient neutrophil-mediated bacterial killing, and the innate immune response to pulmonary infection: cPLA2-α does not regulate neutrophil NADPH oxidase activity. J. Biol. Chem. 280:7519-7529.
    • Rubin, B. B., G. P. Downey, A. Koh, N. Degousee, F. Ghomashchi, L. Nallan, E. Stefanski, D. W. Harkin, C. Sun, B. P. Smart, T. F. Lindsay, V. Cherepanov, E. Vachon, D. Kelvin, M. Sadilek, G. E. Brown, M. B. Yaffe, J. Plumb, S. Grinstein, M. Glogauer, and M. H. Gelb. 2005. Cytosolic phospholipase A2-α is necessary for platelet-activating factor biosynthesis, efficient neutrophil-mediated bacterial killing, and the innate immune response to pulmonary infection: cPLA2-α does not regulate neutrophil NADPH oxidase activity. J. Biol. Chem. 280:7519-7529.
  • 99
    • 13844269166 scopus 로고    scopus 로고
    • Group X secretory phospholipase A2 can induce arachidonic acid release and eicosanoid production without activation of cytosolic phospholipase A2 α
    • Saiga, A., N. Uozumi, T. Ono, K. Seno, Y. Ishimoto, H. Arita, T. Shimizu, and K. Hanasaki. 2005. Group X secretory phospholipase A2 can induce arachidonic acid release and eicosanoid production without activation of cytosolic phospholipase A2 α. Prostaglandins Other Lipid Mediat. 75: 79-89.
    • (2005) Prostaglandins Other Lipid Mediat , vol.75 , pp. 79-89
    • Saiga, A.1    Uozumi, N.2    Ono, T.3    Seno, K.4    Ishimoto, Y.5    Arita, H.6    Shimizu, T.7    Hanasaki, K.8
  • 101
    • 10344252269 scopus 로고    scopus 로고
    • The lung collectins, SP-A and SP-D, modulate pulmonary innate immunity
    • Sano, H., and Y. Kuroki. 2005. The lung collectins, SP-A and SP-D, modulate pulmonary innate immunity. Mol. Immunol. 42:279-287.
    • (2005) Mol. Immunol , vol.42 , pp. 279-287
    • Sano, H.1    Kuroki, Y.2
  • 102
    • 1942469349 scopus 로고    scopus 로고
    • Role of group V phospholipase A2 in zymosaninduced eicosanoid generation and vascular permeability revealed by targeted gene disruption
    • Satake, Y., B. L. Diaz, B. Balestrieri, B. K. Lam, Y. Kanaoka, M. J. Grusby, and J. P. Arm. 2004. Role of group V phospholipase A2 in zymosaninduced eicosanoid generation and vascular permeability revealed by targeted gene disruption. J. Biol. Chem. 279:16488-16494.
    • (2004) J. Biol. Chem , vol.279 , pp. 16488-16494
    • Satake, Y.1    Diaz, B.L.2    Balestrieri, B.3    Lam, B.K.4    Kanaoka, Y.5    Grusby, M.J.6    Arm, J.P.7
  • 103
    • 4444342607 scopus 로고    scopus 로고
    • ExoU is a potent intracellular phospholipase
    • Sato, H., and D. W. Frank. 2004. ExoU is a potent intracellular phospholipase. Mol. Microbiol. 53:1279-1290.
    • (2004) Mol. Microbiol , vol.53 , pp. 1279-1290
    • Sato, H.1    Frank, D.W.2
  • 105
    • 33748672064 scopus 로고    scopus 로고
    • Identification of superoxide dismutase as a cofactor for the pseudomonas type III toxin, ExoU
    • Sato, H., J. B. Feix, and D. W. Frank. 2006. Identification of superoxide dismutase as a cofactor for the pseudomonas type III toxin, ExoU. Biochemistry 45:10368-10375.
    • (2006) Biochemistry , vol.45 , pp. 10368-10375
    • Sato, H.1    Feix, J.B.2    Frank, D.W.3
  • 106
    • 33751028489 scopus 로고    scopus 로고
    • The phospholipase A2 superfamily and its group numbering system
    • Schaloske, R. H., and E. A. Dennis. 2006. The phospholipase A2 superfamily and its group numbering system. Biochim. Biophys. Acta 1761:1246-1259.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 1246-1259
    • Schaloske, R.H.1    Dennis, E.A.2
  • 107
    • 0037709808 scopus 로고    scopus 로고
    • Schuster, D. P., M. Metzler, S. Opal, S. Lowry, R. Balk, E. Abraham, H. Levy, G. Slotman, E. Coyne, S. Souza, J. Pribble, et al. 2003. Recombinant platelet-activating factor acetylhydrolase to prevent acute respiratory distress syndrome and mortality in severe sepsis: phase IIb, multicenter, randomized, placebo-controlled, clinical trial. Crit. Care Med. 31:1612-1619.
    • Schuster, D. P., M. Metzler, S. Opal, S. Lowry, R. Balk, E. Abraham, H. Levy, G. Slotman, E. Coyne, S. Souza, J. Pribble, et al. 2003. Recombinant platelet-activating factor acetylhydrolase to prevent acute respiratory distress syndrome and mortality in severe sepsis: phase IIb, multicenter, randomized, placebo-controlled, clinical trial. Crit. Care Med. 31:1612-1619.
  • 108
    • 0037335881 scopus 로고    scopus 로고
    • Human eosinophil group IID secretory phospholipase A2 causes surfactant dysfunction
    • Seeds, M. C., D. L. Bowton, R. D. Hite, J. I. Gyves, and D. A. Bass. 2003. Human eosinophil group IID secretory phospholipase A2 causes surfactant dysfunction. Chest 123(Suppl. 3):376S-377S.
    • (2003) Chest , vol.123 , Issue.SUPPL. 3
    • Seeds, M.C.1    Bowton, D.L.2    Hite, R.D.3    Gyves, J.I.4    Bass, D.A.5
  • 110
    • 34247847681 scopus 로고    scopus 로고
    • Resolution phase of inflammation: Novel endogenous anti-inflammatory and proresolving lipid mediators and pathways
    • Serhan, C. N. 2007. Resolution phase of inflammation: novel endogenous anti-inflammatory and proresolving lipid mediators and pathways. Annu. Rev. Immunol. 25:101-137.
    • (2007) Annu. Rev. Immunol , vol.25 , pp. 101-137
    • Serhan, C.N.1
  • 111
    • 18244410118 scopus 로고    scopus 로고
    • The pathogenesis of chronic obstructive pulmonary disease: Advances in the past 100 years
    • Shapiro, S. D., and E. P. Ingenito. 2005. The pathogenesis of chronic obstructive pulmonary disease: advances in the past 100 years. Am. J. Respir. Cell Mol. Biol. 32:367-372.
    • (2005) Am. J. Respir. Cell Mol. Biol , vol.32 , pp. 367-372
    • Shapiro, S.D.1    Ingenito, E.P.2
  • 112
    • 9244236027 scopus 로고    scopus 로고
    • Relative contributions of Pseudomonas aeruginosa ExoU, ExoS, and ExoT to virulence in the lung
    • Shaver, C. M., and A. R. Hauser. 2004. Relative contributions of Pseudomonas aeruginosa ExoU, ExoS, and ExoT to virulence in the lung. Infect. Immun. 72:6969-6977.
    • (2004) Infect. Immun , vol.72 , pp. 6969-6977
    • Shaver, C.M.1    Hauser, A.R.2
  • 113
    • 33846688692 scopus 로고    scopus 로고
    • Secreted bacterial phospholipase A2 enzymes: Better living through phospholipolysis
    • Sitkiewicz, I., K. E. Stockbauer, and J. M. Musser. 2007. Secreted bacterial phospholipase A2 enzymes: better living through phospholipolysis. Trends Microbiol. 15:63-69.
    • (2007) Trends Microbiol , vol.15 , pp. 63-69
    • Sitkiewicz, I.1    Stockbauer, K.E.2    Musser, J.M.3
  • 118
    • 0034739453 scopus 로고    scopus 로고
    • Platelet-activating factor acetylhydrolases in health and disease
    • Tjoelker, L. W., and D. M. Stafforini. 2000. Platelet-activating factor acetylhydrolases in health and disease. Biochim. Biophys. Acta 1488:102-123.
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 102-123
    • Tjoelker, L.W.1    Stafforini, D.M.2
  • 119
    • 27644566534 scopus 로고    scopus 로고
    • Secretory phospholipases A2 in inflammatory and allergic diseases: Not just enzymes
    • Triggiani, M., F. Granata, G. Giannattasio, and G. Marone. 2005. Secretory phospholipases A2 in inflammatory and allergic diseases: not just enzymes. J. Allergy Clin. Immunol. 116:1000-1006.
    • (2005) J. Allergy Clin. Immunol , vol.116 , pp. 1000-1006
    • Triggiani, M.1    Granata, F.2    Giannattasio, G.3    Marone, G.4
  • 122
    • 0346961783 scopus 로고    scopus 로고
    • The lung as a privileged site for the beneficial actions of PGE2
    • Vancheri, C., C. Mastruzzo, M. A. Sortino, and N. Crimi. 2004. The lung as a privileged site for the beneficial actions of PGE2. Trends Immunol. 25:40-46.
    • (2004) Trends Immunol , vol.25 , pp. 40-46
    • Vancheri, C.1    Mastruzzo, C.2    Sortino, M.A.3    Crimi, N.4
  • 123
    • 33646949950 scopus 로고    scopus 로고
    • Members of a Legionella pneumophila family of proteins with ExoU (phospholipase A) active sites are translocated to target cells
    • VanRheenen, S. M., Z. Q. Luo, T. O'Connor, and R. R. Isberg. 2006. Members of a Legionella pneumophila family of proteins with ExoU (phospholipase A) active sites are translocated to target cells. Infect. Immun. 74:3597-3606.
    • (2006) Infect. Immun , vol.74 , pp. 3597-3606
    • VanRheenen, S.M.1    Luo, Z.Q.2    O'Connor, T.3    Isberg, R.R.4
  • 124
    • 0033992175 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate induces arachidonic acid mobilization in A549 human lung adenocarcinoma cells
    • Vasta, V., E. Meacci, S. Catarzi, C. Donati, M. Farnararo, and P. Bruni. 2000. Sphingosine 1-phosphate induces arachidonic acid mobilization in A549 human lung adenocarcinoma cells. Biochim. Biophys. Acta 1483:154-160.
    • (2000) Biochim. Biophys. Acta , vol.1483 , pp. 154-160
    • Vasta, V.1    Meacci, E.2    Catarzi, S.3    Donati, C.4    Farnararo, M.5    Bruni, P.6
  • 125
    • 33645683071 scopus 로고    scopus 로고
    • Transgenic mice overexpressing peroxiredoxin 6 show increased resistance to lung injury in hyperoxia
    • Wang, Y., S. A. Phelan, Y. Manevich, S. I. Feinstein, and A. B. Fisher. 2006. Transgenic mice overexpressing peroxiredoxin 6 show increased resistance to lung injury in hyperoxia. Am. J. Respir. Cell Mol. Biol. 34:481-486.
    • (2006) Am. J. Respir. Cell Mol. Biol , vol.34 , pp. 481-486
    • Wang, Y.1    Phelan, S.A.2    Manevich, Y.3    Feinstein, S.I.4    Fisher, A.B.5
  • 126
    • 7444247318 scopus 로고    scopus 로고
    • Lung injury and mortality with hyperoxia are increased in peroxiredoxin 6 gene-targeted mice
    • Wang, Y., S. I. Feinstein, Y. Manevich, Y. S. Ho, and A. B. Fisher. 2004. Lung injury and mortality with hyperoxia are increased in peroxiredoxin 6 gene-targeted mice. Free Radic. Biol. Med. 37:1736-1743.
    • (2004) Free Radic. Biol. Med , vol.37 , pp. 1736-1743
    • Wang, Y.1    Feinstein, S.I.2    Manevich, Y.3    Ho, Y.S.4    Fisher, A.B.5
  • 127
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss, S. J. 1989. Tissue destruction by neutrophils. N. Engl. J. Med. 320:365-376.
    • (1989) N. Engl. J. Med , vol.320 , pp. 365-376
    • Weiss, S.J.1
  • 128
    • 33744998946 scopus 로고    scopus 로고
    • Systematic evaluation of transcellular activities of secretory phospholipases A2. High activity of group V phospholipases A2 to induce eicosanoid biosynthesis in neighboring inflammatory cells
    • Wijewickrama, G. T., J. H. Kim, Y. J. Kim, A. Abraham, Y. Oh, B. Ananthanarayanan, M. Kwatia, S. J. Ackerman, and W. Cho. 2006. Systematic evaluation of transcellular activities of secretory phospholipases A2. High activity of group V phospholipases A2 to induce eicosanoid biosynthesis in neighboring inflammatory cells. J. Biol. Chem. 281:10935-10944.
    • (2006) J. Biol. Chem , vol.281 , pp. 10935-10944
    • Wijewickrama, G.T.1    Kim, J.H.2    Kim, Y.J.3    Abraham, A.4    Oh, Y.5    Ananthanarayanan, B.6    Kwatia, M.7    Ackerman, S.J.8    Cho, W.9
  • 129
    • 0347479350 scopus 로고    scopus 로고
    • Involvement of p38 and p42/44 MAP kinases and protein kinase C in the interferon-γ and interleukin-1α-induced phosphorylation of 85-kDa cytosolic phospholipase A(2) in primary human bronchial epithelial cells
    • Wu, T., C. Han, and J. H. Shelhamer. 2004. Involvement of p38 and p42/44 MAP kinases and protein kinase C in the interferon-γ and interleukin-1α-induced phosphorylation of 85-kDa cytosolic phospholipase A(2) in primary human bronchial epithelial cells. Cytokine 25:11-20.
    • (2004) Cytokine , vol.25 , pp. 11-20
    • Wu, T.1    Han, C.2    Shelhamer, J.H.3
  • 130
    • 0030870433 scopus 로고    scopus 로고
    • Antisense inhibition of 85-kDa cPLA2 blocks arachidonic acid release from airway epithelial cells
    • Wu, T., S. J. Levine, M. Cowan, C. Logun, C. W. Angus, and J. H. Shelhamer. 1997. Antisense inhibition of 85-kDa cPLA2 blocks arachidonic acid release from airway epithelial cells. Am. J. Physiol. 273:L331-L338.
    • (1997) Am. J. Physiol , vol.273
    • Wu, T.1    Levine, S.J.2    Cowan, M.3    Logun, C.4    Angus, C.W.5    Shelhamer, J.H.6
  • 132
    • 0029670878 scopus 로고    scopus 로고
    • Tumor necrosis factor-α induces the 85-kDa cytosolic phospholipase A2 gene expression in human bronchial epithelial cells
    • Wu, T., T. Ikezono, C. W. Angus, and J. H. Shelhamer. 1996. Tumor necrosis factor-α induces the 85-kDa cytosolic phospholipase A2 gene expression in human bronchial epithelial cells. Biochim. Biophys. Acta 1310: 175-184.
    • (1996) Biochim. Biophys. Acta , vol.1310 , pp. 175-184
    • Wu, T.1    Ikezono, T.2    Angus, C.W.3    Shelhamer, J.H.4
  • 134
    • 0141506122 scopus 로고    scopus 로고
    • Surfactant protein-A and phosphatidylglycerol suppress type IIA phospholipase A2 synthesis via nuclear factor-κB
    • Wu, Y. Z., S. Medjane, S. Chabot, F. S. Kubrusly, I. Raw, M. Chignard, and L. Touqui. 2003. Surfactant protein-A and phosphatidylglycerol suppress type IIA phospholipase A2 synthesis via nuclear factor-κB. Am. J. Respir. Crit. Care Med. 168:692-699.
    • (2003) Am. J. Respir. Crit. Care Med , vol.168 , pp. 692-699
    • Wu, Y.Z.1    Medjane, S.2    Chabot, S.3    Kubrusly, F.S.4    Raw, I.5    Chignard, M.6    Touqui, L.7
  • 135
    • 33646358970 scopus 로고    scopus 로고
    • Interaction of surfactant protein A with peroxiredoxin 6 regulates phospholipase A2 activity
    • Wu, Y. Z., Y. Manevich, J. L. Baldwin, C. Dodia, K. Yu, S. I. Feinstein, and A. B. Fisher. 2006. Interaction of surfactant protein A with peroxiredoxin 6 regulates phospholipase A2 activity. J. Biol. Chem. 281:7515-7525.
    • (2006) J. Biol. Chem , vol.281 , pp. 7515-7525
    • Wu, Y.Z.1    Manevich, Y.2    Baldwin, J.L.3    Dodia, C.4    Yu, K.5    Feinstein, S.I.6    Fisher, A.B.7
  • 136
    • 4344619175 scopus 로고    scopus 로고
    • A pathway involving protein kinase Cδ up-regulates cytosolic phospholipase A(2)α in airway epithelium
    • You, H. J., J. W. Lee, Y. J. Yoo, and J. H. Kim. 2004. A pathway involving protein kinase Cδ up-regulates cytosolic phospholipase A(2)α in airway epithelium. Biochem. Biophys. Res. Commun. 321:657-664.
    • (2004) Biochem. Biophys. Res. Commun , vol.321 , pp. 657-664
    • You, H.J.1    Lee, J.W.2    Yoo, Y.J.3    Kim, J.H.4


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