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Volumn 183, Issue 11, 2009, Pages 7497-7504

Calcium-independent phospholipase A2β-Akt signaling is involved in lipopolysaccharide-induced NADPH oxidase 1 expression and foam cell formation

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINE; APOCYNIN; CALCIUM INDEPENDENT PHOSPHOLIPASE A2; CALCIUM INDEPENDENT PHOSPHOLIPASE A2BETA; LIPOPOLYSACCHARIDE; MESSENGER RNA; PROTEIN KINASE B; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 1; SMALL INTERFERING RNA; TOLL LIKE RECEPTOR 4; UNCLASSIFIED DRUG; OXIDOREDUCTASE; PHOSPHOLIPASE A2 GROUP IV; TLR4 PROTEIN, MOUSE;

EID: 73349125092     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.0900503     Document Type: Article
Times cited : (30)

References (48)
  • 1
    • 0035936802 scopus 로고    scopus 로고
    • Atherosclerosis. The road ahead
    • Glass, C. K., and J. L. Witztum. 2001. Atherosclerosis. the road ahead. Cell 104: 503-516.
    • (2001) Cell , vol.104 , pp. 503-516
    • Glass, C.K.1    Witztum, J.L.2
  • 2
    • 55049118368 scopus 로고    scopus 로고
    • A combination of Lox-1 and Nox1 regulates TLR9-mediated foam cell formation
    • Lee, J. G., E. J. Lim, D. W. Park, S. H. Lee, J. R. Kim, and S. H. Baek. 2008. A combination of Lox-1 and Nox1 regulates TLR9-mediated foam cell formation. Cell. Signal. 20: 2266-2275.
    • (2008) Cell. Signal. , vol.20 , pp. 2266-2275
    • Lee, J.G.1    Lim, E.J.2    Park, D.W.3    Lee, S.H.4    Kim, J.R.5    Baek, S.H.6
  • 3
    • 0027500143 scopus 로고
    • Lipopolysaccharide stimulation of RAW 264.7 macrophages induces lipid accumulation and foam cell formation
    • Funk, J. L., K. R. Feingold, A. H. Moser, and C. Grunfeld. 1993. Lipopolysaccharide stimulation of RAW 264.7 macrophages induces lipid accumulation and foam cell formation. Atherosclerosis 98: 67-82.
    • (1993) Atherosclerosis , vol.98 , pp. 67-82
    • Funk, J.L.1    Feingold, K.R.2    Moser, A.H.3    Grunfeld, C.4
  • 4
    • 0348109425 scopus 로고    scopus 로고
    • Reactive Oxygen Species in the Vasculature: Molecular and Cellular Mechanisms
    • DOI 10.1161/01.HYP.0000100443.09293.4F
    • Taniyama, Y., and K. K. Griendling. 2003. Reactive oxygen species in the vasculature: molecular and cellular mechanisms. Hypertension 42: 1075-1081. (Pubitemid 37549058)
    • (2003) Hypertension , vol.42 , Issue.6 , pp. 1075-1081
    • Taniyama, Y.1    Griendling, K.K.2
  • 5
    • 3242710174 scopus 로고    scopus 로고
    • Lack of Toll-like receptor 4 or myeloid differentiation factor 88 reduces atherosclerosis and alters plaque phenotype in mice deficient in apolipoprotein E
    • Michelsen, K. S., M. H. Wong, P. K. Shah, W. Zhang, J. Yano, T. M. Doherty, S. Akira, T. B. Rajavashisth, and M. Arditi. 2004. Lack of Toll-like receptor 4 or myeloid differentiation factor 88 reduces atherosclerosis and alters plaque phenotype in mice deficient in apolipoprotein E. Proc. Natl. Acad. Sci. USA 101: 10679-10684.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10679-10684
    • Michelsen, K.S.1    Wong, M.H.2    Shah, P.K.3    Zhang, W.4    Yano, J.5    Doherty, T.M.6    Akira, S.7    Rajavashisth, T.B.8    Arditi, M.9
  • 8
    • 0035844030 scopus 로고    scopus 로고
    • Novel gp91(phox) homologues in vascular smooth muscle cells: Nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways
    • Lassegue, B., D. Sorescu, K. Szocs, Q. Yin, M. Akers, Y. Zhang, S. L. Grant, J. D. Lambeth, and K. K. Griendling. 2001. Novel gp91(phox) homologues in vascular smooth muscle cells: nox1 mediates angiotensin II-induced superoxide formation and redox-sensitive signaling pathways. Circ. Res. 88: 888-894.
    • (2001) Circ. Res. , vol.88 , pp. 888-894
    • Lassegue, B.1    Sorescu, D.2    Szocs, K.3    Yin, Q.4    Akers, M.5    Zhang, Y.6    Grant, S.L.7    Lambeth, J.D.8    Griendling, K.K.9
  • 9
    • 0037134506 scopus 로고    scopus 로고
    • NADPH oxidase is involved in prostaglandin F2α-induced hypertrophy of vascular smooth muscle cells: Induction of NOX1 by PGF2α
    • Katsuyama, M., C. Fan, and C. Yabe-Nishimura. 2002. NADPH oxidase is involved in prostaglandin F2α-induced hypertrophy of vascular smooth muscle cells: induction of NOX1 by PGF2α. J. Biol. Chem. 277: 13438-13442.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13438-13442
    • Katsuyama, M.1    Fan, C.2    Yabe-Nishimura, C.3
  • 10
    • 25844507931 scopus 로고    scopus 로고
    • PKCdelta mediates up-regulation of NOX1, a catalytic subunit of NADPH oxidase, via transactivation of the EGF receptor: Possible involvement of PKCδ in vascular hypertrophy
    • Fan, C. Y., M. Katsuyama, and C. Yabe-Nishimura. 2005. PKCdelta mediates up-regulation of NOX1, a catalytic subunit of NADPH oxidase, via transactivation of the EGF receptor: possible involvement of PKCδ in vascular hypertrophy. Biochem. J. 390: 761-767.
    • (2005) Biochem. J. , vol.390 , pp. 761-767
    • Fan, C.Y.1    Katsuyama, M.2    Yabe-Nishimura, C.3
  • 11
    • 13844257289 scopus 로고    scopus 로고
    • Transactivation of the EGF receptor and a PI3 kinase-ATF-1 pathway is involved in the up-regulation of NOX1, a catalytic subunit of NADPH oxidase
    • Fan, C., M. Katsuyama, T. Nishinaka, and C. Yabe-Nishimura. 2005. Transactivation of the EGF receptor and a PI3 kinase-ATF-1 pathway is involved in the up-regulation of NOX1, a catalytic subunit of NADPH oxidase. FEBS Lett. 579: 1301-1305.
    • (2005) FEBS Lett. , vol.579 , pp. 1301-1305
    • Fan, C.1    Katsuyama, M.2    Nishinaka, T.3    Yabe-Nishimura, C.4
  • 12
    • 34748856721 scopus 로고    scopus 로고
    • Myocyte enhancer factor 2B is involved in the inducible expression of NOX1/NADPH oxidase, a vascular superoxide-producing enzyme
    • DOI 10.1111/j.1742-4658.2007.06034.x
    • Katsuyama, M., M. Ozgur Cevik, N. Arakawa, T. Kakehi, T. Nishinaka, K. Iwata, M. Ibi, K. Matsuno, and C. Yabe-Nishimura. 2007. Myocyte enhancer factor 2B is involved in the inducible expression of NOX1/NADPH oxidase, a vascular superoxide-producing enzyme. FEBS J. 274: 5128-5136. (Pubitemid 47481186)
    • (2007) FEBS Journal , vol.274 , Issue.19 , pp. 5128-5136
    • Katsuyama, M.1    Ozgur Cevik, M.2    Arakawa, N.3    Kakehi, T.4    Nishinaka, T.5    Iwata, K.6    Ibi, M.7    Matsuno, K.8    Yabe-Nishimura, C.9
  • 14
    • 33748367253 scopus 로고    scopus 로고
    • Novel transcripts of Nox1 are regulated by alternative promoters and expressed under phenotypic modulation of vascular smooth muscle cells
    • DOI 10.1042/BJ20060300
    • Arakawa, N., M. Katsuyama, K. Matsuno, N. Urao, Y. Tabuchi, M. Okigaki, H. Matsubara, and C. Yabe-Nishimura. 2006. Novel transcripts of Nox1 are regulated by alternative promoters and expressed under phenotypic modulation of vascular smooth muscle cells. Biochem. J. 398: 303-310. (Pubitemid 44338487)
    • (2006) Biochemical Journal , vol.398 , Issue.2 , pp. 303-310
    • Arakawa, N.1    Katsuyama, M.2    Matsuno, K.3    Urao, N.4    Tabuchi, Y.5    Okigaki, M.6    Matsubara, H.7    Yabe-Nishimura, C.8
  • 15
    • 0037031926 scopus 로고    scopus 로고
    • Identification of calcium-independent phospholipase A2 (iPLA2)β, and not iPLA2γ, as the mediator of arginine vasopressin-induced arachidonic acid release in A-10 smooth muscle cells: Enantioselective mechanism-based discrimination of mammalian iPLA2s
    • Jenkins, C. M., X. Han, D. J. Mancuso, and R. W. Gross. 2002. Identification of calcium-independent phospholipase A2 (iPLA2)β, and not iPLA2γ, as the mediator of arginine vasopressin-induced arachidonic acid release in A-10 smooth muscle cells: enantioselective mechanism-based discrimination of mammalian iPLA2s. J. Biol. Chem. 277: 32807-32814.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32807-32814
    • Jenkins, C.M.1    Han, X.2    Mancuso, D.J.3    Gross, R.W.4
  • 16
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth, J. D. 2004. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 4: 181-189.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 17
    • 34347257042 scopus 로고    scopus 로고
    • Nox enzymes, ROS, and chronic disease: An example of antagonistic pleiotropy
    • Lambeth, J. D. 2007. Nox enzymes, ROS, and chronic disease: an example of antagonistic pleiotropy. Free Radic. Biol. Med. 43: 332-347.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 332-347
    • Lambeth, J.D.1
  • 18
    • 33748775173 scopus 로고    scopus 로고
    • Dual role of peroxiredoxin I in macrophage-derived foam cells
    • Conway, J. P., and M. Kinter. 2006. Dual role of peroxiredoxin I in macrophage-derived foam cells. J. Biol. Chem. 281: 27991-28001.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27991-28001
    • Conway, J.P.1    Kinter, M.2
  • 19
    • 34547597709 scopus 로고    scopus 로고
    • PPARα in atherosclerosis and inflammation
    • Zandbergen, F., and J. Plutzky. 2007. PPARα in atherosclerosis and inflammation. Biochim. Biophys. Acta 1771: 972-982.
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 972-982
    • Zandbergen, F.1    Plutzky, J.2
  • 22
    • 36248959287 scopus 로고    scopus 로고
    • Toll-like receptor 9-stimulated monocyte chemoattractant protein-1 is mediated via JNK-cytosolic phospholipase A2-ROS signaling
    • Lee, J. G., S. H. Lee, D. W. Park, H. S. Yoon, B. R. Chin, J. H. Kim, J. R. Kim, and S. H. Baek. 2008. Toll-like receptor 9-stimulated monocyte chemoattractant protein-1 is mediated via JNK-cytosolic phospholipase A2-ROS signaling. Cell. Signal. 20: 105-111.
    • (2008) Cell. Signal. , vol.20 , pp. 105-111
    • Lee, J.G.1    Lee, S.H.2    Park, D.W.3    Yoon, H.S.4    Chin, B.R.5    Kim, J.H.6    Kim, J.R.7    Baek, S.H.8
  • 23
    • 53549127797 scopus 로고    scopus 로고
    • Differential vascular functions of Nox family NADPH oxidases
    • Brandes, R. P., and K. Schroder. 2008. Differential vascular functions of Nox family NADPH oxidases. Curr. Opin. Lipidol. 19: 513-518.
    • (2008) Curr. Opin. Lipidol. , vol.19 , pp. 513-518
    • Brandes, R.P.1    Schroder, K.2
  • 24
    • 0034121607 scopus 로고    scopus 로고
    • Impaired superoxide production due to a deficiency in phagocyte NADPH oxidase fails to inhibit atherosclerosis in mice
    • Kirk, E. A., M. C. Dinauer, H. Rosen, A. Chait, J. W. Heinecke, and R. C. LeBoeuf. 2000. Impaired superoxide production due to a deficiency in phagocyte NADPH oxidase fails to inhibit atherosclerosis in mice. Arterioscler. Thromb. Vasc. Biol. 20: 1529-1535.
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 1529-1535
    • Kirk, E.A.1    Dinauer, M.C.2    Rosen, H.3    Chait, A.4    Heinecke, J.W.5    LeBoeuf, R.C.6
  • 26
    • 24144502438 scopus 로고    scopus 로고
    • Thematic review series: The immune system and atherogenesis - Paying the price for pathogen protection: toll receptors in atherogenesis
    • Tobias, P., and L. K. Curtiss. 2005. Thematic review series: the immune system and atherogenesis - paying the price for pathogen protection: toll receptors in atherogenesis. J. Lipid. Res. 46: 404-411.
    • (2005) J. Lipid. Res. , vol.46 , pp. 404-411
    • Tobias, P.1    Curtiss, L.K.2
  • 27
    • 33646820712 scopus 로고    scopus 로고
    • Toll-like receptor signaling and atherosclerosis
    • Michelsen, K. S., and M. Arditi. 2006. Toll-like receptor signaling and atherosclerosis. Curr. Opin. Hematol. 13: 163-168.
    • (2006) Curr. Opin. Hematol. , vol.13 , pp. 163-168
    • Michelsen, K.S.1    Arditi, M.2
  • 28
    • 12344320204 scopus 로고    scopus 로고
    • Ecabet sodium inhibits Helicobacter pylori lipopolysaccharide-induced activation of NADPH oxidase 1 or apoptosis of guinea pig gastric mucosal cells
    • Kusumoto, K., T. Kawahara, Y. Kuwano, S. Teshima-Kondo, K. Morita, K. Kishi, and K. Rokutan. 2005. Ecabet sodium inhibits Helicobacter pylori lipopolysaccharide-induced activation of NADPH oxidase 1 or apoptosis of guinea pig gastric mucosal cells. Am. J. Physiol. 288: G300-G307.
    • (2005) Am. J. Physiol. , vol.288
    • Kusumoto, K.1    Kawahara, T.2    Kuwano, Y.3    Teshima-Kondo, S.4    Morita, K.5    Kishi, K.6    Rokutan, K.7
  • 29
    • 0038205912 scopus 로고    scopus 로고
    • phoxin the regulated production of superoxide by phagocytes
    • Geiszt, M., K. Lekstrom, S. Brenner, S. M. Hewitt, R. Dana, H. L. Malech, and T. L. Leto. 2003. NAD(P)H oxidase 1, a product of differentiated colon epithelial cells, can partially replace glycoprotein 91phox in the regulated production of superoxide by phagocytes. J. Immunol. 171: 299-306. (Pubitemid 36745301)
    • (2003) Journal of Immunology , vol.171 , Issue.1 , pp. 299-306
    • Geiszt, M.1    Lekstrom, K.2    Brenner, S.3    Hewitt, S.M.4    Dana, R.5    Malech, H.L.6    Leto, T.L.7
  • 30
    • 33644866770 scopus 로고    scopus 로고
    • Interferon γ activates transcription of NADPH oxidase 1 gene and up-regulates production of superoxide anion by human large intestinal epithelial cells
    • Kuwano, Y., T. Kawahara, H. Yamamoto, S. Teshima-Kondo, K. Tominaga, K. Masuda, K. Kishi, K. Morita, and K. Rokutan. 2006. Interferon γ activates transcription of NADPH oxidase 1 gene and up-regulates production of superoxide anion by human large intestinal epithelial cells. Am. J. Physiol. 290: C433-C443.
    • (2006) Am. J. Physiol. , vol.290
    • Kuwano, Y.1    Kawahara, T.2    Yamamoto, H.3    Teshima-Kondo, S.4    Tominaga, K.5    Masuda, K.6    Kishi, K.7    Morita, K.8    Rokutan, K.9
  • 31
    • 0035584538 scopus 로고    scopus 로고
    • Up-regulation of the vascular NAD(P)H-oxidase isoforms Nox1 and Nox4 by the renin-angiotensin system in vitro and in vivo
    • Wingler, K., S. Wunsch, R. Kreutz, L. Rothermund, M. Paul, and H. H. Schmidt. 2001. Up-regulation of the vascular NAD(P)H-oxidase isoforms Nox1 and Nox4 by the renin-angiotensin system in vitro and in vivo. Free Radic. Biol. Med. 31: 1456-1464.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1456-1464
    • Wingler, K.1    Wunsch, S.2    Kreutz, R.3    Rothermund, L.4    Paul, M.5    Schmidt, H.H.6
  • 32
    • 14844334642 scopus 로고    scopus 로고
    • Essential role of ATF-1 in induction of NOX1, a catalytic subunit of NADPH oxidase: Involvement of mitochondrial respiratory chain
    • Katsuyama, M., C. Fan, N. Arakawa, T. Nishinaka, M. Miyagishi, K. Taira, and C. Yabe-Nishimura. 2005. Essential role of ATF-1 in induction of NOX1, a catalytic subunit of NADPH oxidase: involvement of mitochondrial respiratory chain. Biochem. J. 386: 255-261.
    • (2005) Biochem. J. , vol.386 , pp. 255-261
    • Katsuyama, M.1    Fan, C.2    Arakawa, N.3    Nishinaka, T.4    Miyagishi, M.5    Taira, K.6    Yabe-Nishimura, C.7
  • 33
    • 0033637971 scopus 로고    scopus 로고
    • Regulation of growth and apoptosis of cultured guinea pig gastric mucosal cells by mitogenic oxidase 1
    • Teshima, S., H. Kutsumi, T. Kawahara, K. Kishi, and K. Rokutan. 2000. Regulation of growth and apoptosis of cultured guinea pig gastric mucosal cells by mitogenic oxidase 1. Am. J. Physiol. 279: G1169-G1176.
    • (2000) Am. J. Physiol. , vol.279
    • Teshima, S.1    Kutsumi, H.2    Kawahara, T.3    Kishi, K.4    Rokutan, K.5
  • 34
    • 33750912209 scopus 로고    scopus 로고
    • NADPH oxidases in the gastrointestinal tract: A potential role of Nox1 in innate immune response and carcinogenesis
    • Rokutan, K., T. Kawahara, Y. Kuwano, K. Tominaga, A. Sekiyama, and S. Teshima-Kondo. 2006. NADPH oxidases in the gastrointestinal tract: a potential role of Nox1 in innate immune response and carcinogenesis. Antioxid. Redox Signal. 8: 1573-1582.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1573-1582
    • Rokutan, K.1    Kawahara, T.2    Kuwano, Y.3    Tominaga, K.4    Sekiyama, A.5    Teshima-Kondo, S.6
  • 35
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K., and K. H. Krause. 2007. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 87: 245-313.
    • (2007) Physiol. Rev. , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 36
    • 0037303555 scopus 로고    scopus 로고
    • Superoxide production and expression of NAD(P)H oxidases by transformed and primary human colonic epithelial cells
    • Perner, A., L. Andresen, G. Pedersen, and J. Rask-Madsen. 2003. Superoxide production and expression of NAD(P)H oxidases by transformed and primary human colonic epithelial cells. Gut 52: 231-236.
    • (2003) Gut , vol.52 , pp. 231-236
    • Perner, A.1    Andresen, L.2    Pedersen, G.3    Rask-Madsen, J.4
  • 37
    • 0035885008 scopus 로고    scopus 로고
    • Calcium-independent phospholipase A2 is required for human monocyte chemotaxis to monocyte chemoattractant protein 1
    • Carnevale, K. A., and M. K. Cathcart. 2001. Calcium-independent phospholipase A2 is required for human monocyte chemotaxis to monocyte chemoattractant protein 1. J. Immunol. 167: 3414-3421.
    • (2001) J. Immunol. , vol.167 , pp. 3414-3421
    • Carnevale, K.A.1    Cathcart, M.K.2
  • 38
    • 39549122207 scopus 로고    scopus 로고
    • iPLA2β: Front and center in human monocyte chemotaxis to MCP-1
    • Mishra, R. S., K. A. Carnevale, and M. K. Cathcart. 2008. iPLA2β: front and center in human monocyte chemotaxis to MCP-1. J. Exp. Med. 205: 347-359.
    • (2008) J. Exp. Med. , vol.205 , pp. 347-359
    • Mishra, R.S.1    Carnevale, K.A.2    Cathcart, M.K.3
  • 39
    • 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
  • 40
    • 36348990292 scopus 로고    scopus 로고
    • Class A scavenger receptor-mediated macrophage adhesion requires coupling of calcium-independent phospholipase A2 and 12/15-lipoxygenase to Rac and Cdc42 activation
    • Nikolic, D. M., M. C. Gong, J. Turk, and S. R. Post. 2007. Class A scavenger receptor-mediated macrophage adhesion requires coupling of calcium-independent phospholipase A2 and 12/15-lipoxygenase to Rac and Cdc42 activation. J. Biol. Chem. 282: 33405-33411.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33405-33411
    • Nikolic, D.M.1    Gong, M.C.2    Turk, J.3    Post, S.R.4
  • 41
    • 33845971303 scopus 로고    scopus 로고
    • Group VIA calcium-independent phospholipase A2 mediates endothelial cell S-phase progression
    • Herbert, S. P., and J. H. Walker. 2006. Group VIA calcium-independent phospholipase A2 mediates endothelial cell S-phase progression. J. Biol. Chem. 281: 35709-35716.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35709-35716
    • Herbert, S.P.1    Walker, J.H.2
  • 42
    • 0035831490 scopus 로고    scopus 로고
    • Identification of the calmodulin-binding domain of recombinant calcium-independent phospholipase A2β: Implications for structure and function
    • Jenkins, C. M., M. J. Wolf, D. J. Mancuso, and R. W. Gross. 2001. Identification of the calmodulin-binding domain of recombinant calcium-independent phospholipase A2β: implications for structure and function. J. Biol. Chem. 276: 7129-7135.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7129-7135
    • Jenkins, C.M.1    Wolf, M.J.2    Mancuso, D.J.3    Gross, R.W.4
  • 43
    • 0142200309 scopus 로고    scopus 로고
    • Group V and X secretory phospholipase A2s-induced modification of high-density lipoprotein linked to the reduction of its antiatherogenic functions
    • Ishimoto, Y., K. Yamada, S. Yamamoto, T. Ono, M. Notoya, and K. Hanasaki. 2003. Group V and X secretory phospholipase A2s-induced modification of high-density lipoprotein linked to the reduction of its antiatherogenic functions. Biochim. Biophys. Acta 1642: 129-138.
    • (2003) Biochim. Biophys. Acta , vol.1642 , pp. 129-138
    • Ishimoto, Y.1    Yamada, K.2    Yamamoto, S.3    Ono, T.4    Notoya, M.5    Hanasaki, K.6
  • 44
    • 57749093002 scopus 로고    scopus 로고
    • Analyses of group III secreted phospholipase A2 transgenic mice reveal potential participation of this enzyme in plasma lipoprotein modification, macrophage foam cell formation, and atherosclerosis
    • Sato, H., R. Kato, Y. Isogai, G. Saka, M. Ohtsuki, Y. Taketomi, K. Yamamoto, K. Tsutsumi, J. Yamada, S. Masuda, et al. 2008. Analyses of group III secreted phospholipase A2 transgenic mice reveal potential participation of this enzyme in plasma lipoprotein modification, macrophage foam cell formation, and atherosclerosis. J. Biol. Chem. 283: 33483-33497.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33483-33497
    • Sato, H.1    Kato, R.2    Isogai, Y.3    Saka, G.4    Ohtsuki, M.5    Taketomi, Y.6    Yamamoto, K.7    Tsutsumi, K.8    Yamada, J.9    Masuda, S.10
  • 45
    • 67449168509 scopus 로고    scopus 로고
    • Syndecan-4 mediates macrophage uptake of group V secretory phospholipase A2-modified low density lipoprotein
    • Boyanovsky, B. B., P. Shridas, M. Simons, D. R. van der Westhuyzen, and N. R. Webb. 2008. Syndecan-4 mediates macrophage uptake of group V secretory phospholipase A2-modified low density lipoprotein. J. Lipid Res. 50: 641-650.
    • (2008) J. Lipid Res. , vol.50 , pp. 641-650
    • Boyanovsky, B.B.1    Shridas, P.2    Simons, M.3    Van Der Westhuyzen, D.R.4    Webb, N.R.5
  • 48
    • 33845678939 scopus 로고    scopus 로고
    • Atherogenic properties of LDL particles modified by human group X secreted phospholipase A2 on human endothelial cell function
    • Karabina, S. A., I. Brocheriou, G. Le Naour, M. Agrapart, H. Durand, M. Gelb, G. Lambeau, and E. Ninio. 2006. Atherogenic properties of LDL particles modified by human group X secreted phospholipase A2 on human endothelial cell function. FASEB J. 20: 2547-2549.
    • (2006) FASEB J. , vol.20 , pp. 2547-2549
    • Karabina, S.A.1    Brocheriou, I.2    Le Naour, G.3    Agrapart, M.4    Durand, H.5    Gelb, M.6    Lambeau, G.7    Ninio, E.8


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