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Volumn 163, Issue 4, 2003, Pages 1525-1537

Deficiency of NADPH oxidase components p47phox and gp91phox caused granulomatous synovitis and increased connective tissue destruction in experimental arthritis models

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT COMPONENT C3; GELATINASE B; GLYCOPROTEIN; INTERLEUKIN 1ALPHA; OXYGEN RADICAL; PROTEIN P47; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; STROMELYSIN; TARTARIC ACID; TUMOR NECROSIS FACTOR ALPHA;

EID: 0141648399     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)63509-2     Document Type: Article
Times cited : (78)

References (61)
  • 1
    • 0032741371 scopus 로고    scopus 로고
    • NADPH oxidase activation and assembly during phagocytosis
    • DeLeo FR, Allen LA, Apiceila M, Nauseef WM: NADPH oxidase activation and assembly during phagocytosis. J Immunol 1999, 163:6732-6740
    • (1999) J Immunol , vol.163 , pp. 6732-6740
    • DeLeo, F.R.1    Allen, L.A.2    Apiceila, M.3    Nauseef, W.M.4
  • 2
    • 0033609302 scopus 로고    scopus 로고
    • Phosphorylation induces conformational changes in the leukocyte NADPH oxidase subunit p47(phox)
    • Park HS, Kim IS, Park JW: Phosphorylation induces conformational changes in the leukocyte NADPH oxidase subunit p47(phox). Biochem Biophys Res Commun 1999, 259:38-42
    • (1999) Biochem Biophys Res Commun , vol.259 , pp. 38-42
    • Park, H.S.1    Kim, I.S.2    Park, J.W.3
  • 3
    • 0036710445 scopus 로고    scopus 로고
    • The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism
    • Vignais PV: The superoxide-generating NADPH oxidase: structural aspects and activation mechanism. Cell Mol Life Sci 2002, 59:1428-1459
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1428-1459
    • Vignais, P.V.1
  • 4
    • 0029443327 scopus 로고
    • NADPH oxidase and the respiratory burst
    • Wientjes FB, Segal AW: NADPH oxidase and the respiratory burst. Semin Cell Biol 1995, 6:357-365
    • (1995) Semin Cell Biol , vol.6 , pp. 357-365
    • Wientjes, F.B.1    Segal, A.W.2
  • 6
    • 0026628807 scopus 로고
    • Chronic granulomatous disease
    • Dinauer MC, Orkin SH: Chronic granulomatous disease. Annu Rev Med 1992, 43:117-24:117-124
    • (1992) Annu Rev Med , vol.43 , pp. 117-124
    • Dinauer, M.C.1    Orkin, S.H.2
  • 7
    • 0028984840 scopus 로고
    • The p47phox mouse knock-out model of chronic granulomatous disease
    • Jackson SH, Gallin JI, Holland SM: The p47phox mouse knock-out model of chronic granulomatous disease. J Exp Med 1995, 182:751-758
    • (1995) J Exp Med , vol.182 , pp. 751-758
    • Jackson, S.H.1    Gallin, J.I.2    Holland, S.M.3
  • 9
    • 0028315882 scopus 로고
    • Polyarthritis resembling juvenile rheumatoid arthritis in a girl with chronic granulomatous disease
    • Lee BW, Yap HK: Polyarthritis resembling juvenile rheumatoid arthritis in a girl with chronic granulomatous disease. Arthritis Rheum 1994, 37:773-776
    • (1994) Arthritis Rheum , vol.37 , pp. 773-776
    • Lee, B.W.1    Yap, H.K.2
  • 10
    • 0029825958 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in neutrophils from synovial fluid of patients with rheumatoid arthritis
    • Lloyds D, Davies EV, Williams BD, Hallett MB: Tyrosine phosphorylation in neutrophils from synovial fluid of patients with rheumatoid arthritis. Br J Rheumatol 1996, 35:846-852
    • (1996) Br J Rheumatol , vol.35 , pp. 846-852
    • Lloyds, D.1    Davies, E.V.2    Williams, B.D.3    Hallett, M.B.4
  • 11
    • 0029761147 scopus 로고    scopus 로고
    • Priming of NADPH oxidase by tumor necrosis factor-α in patients with inflammatory and autoimmune rheumatic diseases
    • Miesel R, Hartung R, Kroeger H: Priming of NADPH oxidase by tumor necrosis factor-α in patients with inflammatory and autoimmune rheumatic diseases. Inflammation 1996, 20:427-438
    • (1996) Inflammation , vol.20 , pp. 427-438
    • Miesel, R.1    Hartung, R.2    Kroeger, H.3
  • 12
    • 0022647765 scopus 로고
    • Superoxide production by polymorphonuclear leucocytes in rheumatoid arthritis and osteoarthritis: In vivo inhibition by the antirheumatic drug piroxicam due to interference with the activation of the NADPH-oxidase
    • Biemond P, Swaak AJ, Penders JM, Beindorff CM, Koster JF: Superoxide production by polymorphonuclear leucocytes in rheumatoid arthritis and osteoarthritis: in vivo inhibition by the antirheumatic drug piroxicam due to interference with the activation of the NADPH-oxidase. Ann Rheum Dis 1986, 45:249-255
    • (1986) Ann Rheum Dis , vol.45 , pp. 249-255
    • Biemond, P.1    Swaak, A.J.2    Penders, J.M.3    Beindorff, C.M.4    Koster, J.F.5
  • 13
    • 0036950568 scopus 로고    scopus 로고
    • NADPH oxidase priming and p47phox phosphorylation in neutrophils from synovial fluid of patients with rheumatoid arthritis and spondylarthropathy
    • El Benna J, Hayem G, Dang PM, Fay M, Chollet-Martin S, Elbim C, Meyer O, Gougerot-Pocidalo MA: NADPH oxidase priming and p47phox phosphorylation in neutrophils from synovial fluid of patients with rheumatoid arthritis and spondylarthropathy. Inflammation 2002, 26:273-278
    • (2002) Inflammation , vol.26 , pp. 273-278
    • El Benna, J.1    Hayem, G.2    Dang, P.M.3    Fay, M.4    Chollet-Martin, S.5    Elbim, C.6    Meyer, O.7    Gougerot-Pocidalo, M.A.8
  • 14
  • 15
    • 0025945343 scopus 로고
    • Inhibitors of reactive oxygen intermediates suppress bacterial cell-wall-induced arthritis
    • Skaleric U, Allen JB, Smith PD, Mergenhagen SE, Wahl SM: Inhibitors of reactive oxygen intermediates suppress bacterial cell-wall-induced arthritis. J Immunol 1991, 147:2559-2564
    • (1991) J Immunol , vol.147 , pp. 2559-2564
    • Skaleric, U.1    Allen, J.B.2    Smith, P.D.3    Mergenhagen, S.E.4    Wahl, S.M.5
  • 16
    • 0027444585 scopus 로고
    • The suppressive effect of gelatin-conjugated superoxide dismutase on disease development and severity of collagen-induced arthritis in mice
    • Kakimoto K, Kojima Y, Ishii K, Onoue K, Maeda H: The suppressive effect of gelatin-conjugated superoxide dismutase on disease development and severity of collagen-induced arthritis in mice. Clin Exp Immunol 1993, 94:241-246
    • (1993) Clin Exp Immunol , vol.94 , pp. 241-246
    • Kakimoto, K.1    Kojima, Y.2    Ishii, K.3    Onoue, K.4    Maeda, H.5
  • 17
    • 0022362555 scopus 로고
    • Cationization of catalase, peroxidase, and superoxide dismutase: Effect of improved intraarticular retention on experimental arthritis in mice
    • Schalkwijk J, van den Berg WB, van de Putte LB, Joosten LA, van den BL: Cationization of catalase, peroxidase, and superoxide dismutase: effect of improved intraarticular retention on experimental arthritis in mice. J Clin Invest 1985, 76:198-205
    • (1985) J Clin Invest , vol.76 , pp. 198-205
    • Schalkwijk, J.1    Van den Berg, W.B.2    Van de Putte, L.B.3    Joosten, L.A.4    Van den, B.L.5
  • 18
    • 0033052483 scopus 로고    scopus 로고
    • Failure of endotoxin-free superoxide dismutase to reduce some paw edemas and adjuvant arthritis in rats
    • Iida M, Saito K: Failure of endotoxin-free superoxide dismutase to reduce some paw edemas and adjuvant arthritis in rats. Inflamm Res 1999, 48:63-66
    • (1999) Inflamm Res , vol.48 , pp. 63-66
    • Iida, M.1    Saito, K.2
  • 19
    • 0028157617 scopus 로고
    • The requirement of p47 phosphorylation for activation of NADPH oxidase by opsonized zymosan in human neutrophils
    • Levy R, Dana R, Leto TL, Malech HL: The requirement of p47 phosphorylation for activation of NADPH oxidase by opsonized zymosan in human neutrophils. Biochim Biophys Acta 1994, 1220:253-260
    • (1994) Biochim Biophys Acta , vol.1220 , pp. 253-260
    • Levy, R.1    Dana, R.2    Leto, T.L.3    Malech, H.L.4
  • 20
    • 0034758046 scopus 로고    scopus 로고
    • Toll-like receptor-2 transduces signals for NF-κB activation, apoptosis and reactive oxygen species production
    • Aliprantis AO, Weiss DS, Zychlinsky A: Toll-like receptor-2 transduces signals for NF-κB activation, apoptosis and reactive oxygen species production. J Endotoxin Res 2001, 7:287-291
    • (2001) J Endotoxin Res , vol.7 , pp. 287-291
    • Aliprantis, A.O.1    Weiss, D.S.2    Zychlinsky, A.3
  • 21
    • 0033943686 scopus 로고    scopus 로고
    • Nonopsonic phagocytosis of zymosan and Mycobacterium kansasii by CR3 (CD11b/CD18) involves distinct molecular determinants and is or is not coupled with NADPH oxidase activation
    • Le Cabec V, Cols C, Maridonneau-Parini I: Nonopsonic phagocytosis of zymosan and Mycobacterium kansasii by CR3 (CD11b/CD18) involves distinct molecular determinants and is or is not coupled with NADPH oxidase activation. Infect Immun 2000, 68:4736-4745
    • (2000) Infect Immun , vol.68 , pp. 4736-4745
    • Le Cabec, V.1    Cols, C.2    Maridonneau-Parini, I.3
  • 23
    • 0035542767 scopus 로고    scopus 로고
    • Functional coupling of FcγRI to nicotinamide adenine dinucleotide phosphate (reduced form) oxidative burst and immune complex trafficking requires the activation of phospholipase D1
    • Melendez AJ, Bruetschy L, Floto RA, Harnett MM, Allen JM: Functional coupling of FcγRI to nicotinamide adenine dinucleotide phosphate (reduced form) oxidative burst and immune complex trafficking requires the activation of phospholipase D1. Blood 2001, 98:3421-3428
    • (2001) Blood , vol.98 , pp. 3421-3428
    • Melendez, A.J.1    Bruetschy, L.2    Floto, R.A.3    Harnett, M.M.4    Allen, J.M.5
  • 26
    • 0027178869 scopus 로고
    • Respective role of polymorphonuclear leukocytes and their integrins (CD-11/18) in the local or systemic toxicity of lipopolysaccharide
    • Chang HR, Vesin C, Grau GE, Pointaire P, Arsenijevic D, Strath M, Pechere JC, Piguet PF: Respective role of polymorphonuclear leukocytes and their integrins (CD-11/18) in the local or systemic toxicity of lipopolysaccharide. J Leukoc Biol 1993, 53:636-639
    • (1993) J Leukoc Biol , vol.53 , pp. 636-639
    • Chang, H.R.1    Vesin, C.2    Grau, G.E.3    Pointaire, P.4    Arsenijevic, D.5    Strath, M.6    Pechere, J.C.7    Piguet, P.F.8
  • 27
    • 0033000529 scopus 로고    scopus 로고
    • Kinetics of aggrecanase- and metalloproteinase-induced neoepitopes in various stages of cartilage destruction in murine arthritis
    • Van Meurs JB, Van Lent PL, Holthuysen AE, Singer II, Bayne EK, van den Berg WB: Kinetics of aggrecanase- and metalloproteinase-induced neoepitopes in various stages of cartilage destruction in murine arthritis. Arthritis Rheum 1999, 42:1128-1139
    • (1999) Arthritis Rheum , vol.42 , pp. 1128-1139
    • Van Meurs, J.B.1    Van Lent, P.L.2    Holthuysen, A.E.3    Singer, I.I.4    Bayne, E.K.5    Van den Berg, W.B.6
  • 28
    • 0031020940 scopus 로고    scopus 로고
    • Quantification of mRNA levels in joint capsule and articular cartilage of the murine knee joint by RT-PCR: Kinetics of stromelysin and IL-1 mRNA levels during arthritis
    • Van Meurs JB, Van Lent PL, Joosten LA, Van der Kraan PM, van den Berg WB: Quantification of mRNA levels in joint capsule and articular cartilage of the murine knee joint by RT-PCR: kinetics of stromelysin and IL-1 mRNA levels during arthritis. Rheumatol Int 1997, 16:197-205
    • (1997) Rheumatol Int , vol.16 , pp. 197-205
    • Van Meurs, J.B.1    Van Lent, P.L.2    Joosten, L.A.3    Van der Kraan, P.M.4    Van den Berg, W.B.5
  • 29
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson WR, Lipman DJ: Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 1988, 85:2444-2448
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 31
    • 0030051654 scopus 로고    scopus 로고
    • Suppression of inflammatory arthritis by simultaneous inhibition of nitric oxide synthase and NADPH oxidase
    • Miesel R, Kurpisz M, Kroger H: Suppression of inflammatory arthritis by simultaneous inhibition of nitric oxide synthase and NADPH oxidase. Free Radic Biol Med 1996, 20:75-81
    • (1996) Free Radic Biol Med , vol.20 , pp. 75-81
    • Miesel, R.1    Kurpisz, M.2    Kroger, H.3
  • 32
    • 0031926345 scopus 로고    scopus 로고
    • Reduced cartilage proteoglycan loss during zymosan-induced gonarthritis in NOS2-deficient mice and in anti-interleukin-1-treated wild-type mice with unabated joint inflammation
    • van de Loo FA, Arntz OJ, van Enckevort FH, Van Lent PL, van den Berg WB: Reduced cartilage proteoglycan loss during zymosan-induced gonarthritis in NOS2-deficient mice and in anti-interleukin-1-treated wild-type mice with unabated joint inflammation. Arthritis Rheum 1998, 41:634-646
    • (1998) Arthritis Rheum , vol.41 , pp. 634-646
    • Van de Loo, F.A.1    Arntz, O.J.2    Van Enckevort, F.H.3    Van Lent, P.L.4    Van den Berg, W.B.5
  • 33
    • 0034458228 scopus 로고    scopus 로고
    • The NADPH oxidase of endothelial cells
    • Bibber B: The NADPH oxidase of endothelial cells. IUBMB Life 2000, 50:267-269
    • (2000) IUBMB Life , vol.50 , pp. 267-269
    • Bibber, B.1
  • 35
    • 0033034095 scopus 로고    scopus 로고
    • The p47(phox-/-) mouse model of chronic granulomatous disease has normal granuloma formation and cytokine responses to Mycobacterium avium and Schistosoma mansoni eggs
    • Segal BH, Doherty TM, Wynn TA, Cheever AW, Sher A, Holland SM: The p47(phox-/-) mouse model of chronic granulomatous disease has normal granuloma formation and cytokine responses to Mycobacterium avium and Schistosoma mansoni eggs. Infect Immun 1999, 67:1659-1665
    • (1999) Infect Immun , vol.67 , pp. 1659-1665
    • Segal, B.H.1    Doherty, T.M.2    Wynn, T.A.3    Cheever, A.W.4    Sher, A.5    Holland, S.M.6
  • 36
    • 0031041884 scopus 로고    scopus 로고
    • Absence of respiratory burst in X-linked chronic granulomatous disease mice leads to abnormalities in both host defense and inflammatory response to Aspergillus fumigatus
    • Morgenstern DE, Gifford MA, Li LL, Doerschuk CM, Dinauer MC: Absence of respiratory burst in X-linked chronic granulomatous disease mice leads to abnormalities in both host defense and inflammatory response to Aspergillus fumigatus. J Exp Med 1997 185:207-218
    • (1997) J Exp Med , vol.185 , pp. 207-218
    • Morgenstern, D.E.1    Gifford, M.A.2    Li, L.L.3    Doerschuk, C.M.4    Dinauer, M.C.5
  • 37
    • 0037090069 scopus 로고    scopus 로고
    • Role of NADPH oxidase in the mechanism of lung neutrophil sequestration and microvessel injury induced by Gram-negative sepsis: Studies in p47phox-/- and gp91phox-/- mice
    • Gao XP, Standiford TJ, Rahman A, Newstead M, Holland SM, Dinauer MC, Liu QH, Malik AB: Role of NADPH oxidase in the mechanism of lung neutrophil sequestration and microvessel injury induced by Gram-negative sepsis: studies in p47phox-/- and gp91phox-/- mice. J Immunol 2002, 168:3974-3982
    • (2002) J Immunol , vol.168 , pp. 3974-3982
    • Gao, X.P.1    Standiford, T.J.2    Rahman, A.3    Newstead, M.4    Holland, S.M.5    Dinauer, M.C.6    Liu, Q.H.7    Malik, A.B.8
  • 38
    • 0037115158 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling
    • Forman HJ, Torres M: Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling. Am J Respir Crit Care Med 2002, 166:S4-S8
    • (2002) Am J Respir Crit Care Med , vol.166
    • Forman, H.J.1    Torres, M.2
  • 39
    • 0032416113 scopus 로고    scopus 로고
    • Activation of the JAK-STAT pathway by reactive oxygen species
    • Simon AR, Rai U, Fanburg BL, Cochran BH: Activation of the JAK-STAT pathway by reactive oxygen species. Am J Physiol 1998, 275: C1640-C1652
    • (1998) Am J Physiol , vol.275
    • Simon, A.R.1    Rai, U.2    Fanburg, B.L.3    Cochran, B.H.4
  • 41
    • 0021016311 scopus 로고
    • Leukotriene production and inactivation by normal, chronic granulomatous disease and myeloperoxidase-deficient neutrophils
    • Henderson WR, Klebanoff SJ: Leukotriene production and inactivation by normal, chronic granulomatous disease and myeloperoxidase-deficient neutrophils. J Biol Chem 1983, 258:13522-13527
    • (1983) J Biol Chem , vol.258 , pp. 13522-13527
    • Henderson, W.R.1    Klebanoff, S.J.2
  • 42
    • 0036521603 scopus 로고    scopus 로고
    • Thioglycollate peritonitis in mice lacking C5, 5-lipoxygenase, or p47(phox): Complement, leukotrienes, and reactive oxidants in acute inflammation
    • Segal BH, Kuhns DB, Ding L, Gallin JI, Holland SM: Thioglycollate peritonitis in mice lacking C5, 5-lipoxygenase, or p47(phox): complement, leukotrienes, and reactive oxidants in acute inflammation. J Leukoc Biol 2002, 71:410-416
    • (2002) J Leukoc Biol , vol.71 , pp. 410-416
    • Segal, B.H.1    Kuhns, D.B.2    Ding, L.3    Gallin, J.I.4    Holland, S.M.5
  • 43
    • 0033015425 scopus 로고    scopus 로고
    • Activation of the granule pool of the NADPH oxidase accelerates apoptosis in human neutrophils
    • Lundqvist-Gustafsson H, Bengtsson T: Activation of the granule pool of the NADPH oxidase accelerates apoptosis in human neutrophils. J Leukoc Biol 1999, 65:196-204
    • (1999) J Leukoc Biol , vol.65 , pp. 196-204
    • Lundqvist-Gustafsson, H.1    Bengtsson, T.2
  • 45
    • 0030737716 scopus 로고    scopus 로고
    • Seeing the wood for the trees: The forgotten role of neutrophils in rheumatoid arthritis
    • Edwards SW, Hallett MB: Seeing the wood for the trees: the forgotten role of neutrophils in rheumatoid arthritis. Immunol Today 1997, 18:320-324
    • (1997) Immunol Today , vol.18 , pp. 320-324
    • Edwards, S.W.1    Hallett, M.B.2
  • 47
    • 0026969079 scopus 로고
    • Gelatinase is the main matrix metalloproteinase involved in granuloma-induced cartilage degradation
    • Trancart MM, Chalmeigne N, Girardot C, Zarpanelian C, Prigent D: Gelatinase is the main matrix metalloproteinase involved in granuloma-induced cartilage degradation. Int J Tissue React 1992, 14:287-294
    • (1992) Int J Tissue React , vol.14 , pp. 287-294
    • Trancart, M.M.1    Chalmeigne, N.2    Girardot, C.3    Zarpanelian, C.4    Prigent, D.5
  • 49
    • 17044461667 scopus 로고    scopus 로고
    • Cleavage of aggrecan at the Asn341-Phe342 site coincides with the initiation of collagen damage in murine antigen-induced arthritis: A pivotal role for stromelysin 1 in matrix metalloproteinase activity
    • van Meurs J, van Lent P, Stoop R, Holthuysen A, Singer I, Bayne E, Mudgett J, Poole R, Billinghurst C, van der KP, Buma P, van den BW: Cleavage of aggrecan at the Asn341-Phe342 site coincides with the initiation of collagen damage in murine antigen-induced arthritis: a pivotal role for stromelysin 1 in matrix metalloproteinase activity. Arthritis Rheum 1999, 42:2074-2084
    • (1999) Arthritis Rheum , vol.42 , pp. 2074-2084
    • Van Meurs, J.1    Van Lent, P.2    Stoop, R.3    Holthuysen, A.4    Singer, I.5    Bayne, E.6    Mudgett, J.7    Poole, R.8    Billinghurst, C.9    Van der, K.P.10    Buma, P.11    Van den, B.W.12
  • 50
    • 0023092299 scopus 로고
    • Elastase secreted by activated polymorphonuclear leucocytes causes chondrocyte damage and matrix degradation in intact articular cartilage: Escape from inactivation by α-1-proteinase inhibitor
    • Schalkwijk J, van den Berg WB, van de Putte LB, Joosten LA: Elastase secreted by activated polymorphonuclear leucocytes causes chondrocyte damage and matrix degradation in intact articular cartilage: escape from inactivation by α-1-proteinase inhibitor. Br J Exp Pathol 1987, 68:81-88
    • (1987) Br J Exp Pathol , vol.68 , pp. 81-88
    • Schalkwijk, J.1    Van den Berg, W.B.2    Van de Putte, L.B.3    Joosten, L.A.4
  • 51
    • 0023276767 scopus 로고
    • Enhanced breakdown in vitro of bovine articular cartilage proteoglycans by conditional synovial medium. The effect of superoxide dismutase and catalase
    • Klamfeldt A, Marklund S: Enhanced breakdown in vitro of bovine articular cartilage proteoglycans by conditional synovial medium. The effect of superoxide dismutase and catalase. Scand J Rheumatol 1987, 16:41-45
    • (1987) Scand J Rheumatol , vol.16 , pp. 41-45
    • Klamfeldt, A.1    Marklund, S.2
  • 52
    • 0028891167 scopus 로고
    • Role of interleukin-1, tumor necrosis factor-α, and interleukin-6 in cartilage proteoglycan metabolism and destruction. Effect of in situ blocking in murine antigen- and zymosan-induced arthritis
    • van de Loo FA, Joosten LA, Van Lent PL, Arntz OJ, van den Berg WB: Role of interleukin-1, tumor necrosis factor-α, and interleukin-6 in cartilage proteoglycan metabolism and destruction. Effect of in situ blocking in murine antigen- and zymosan-induced arthritis. Arthritis Rheum 1995, 38:164-172
    • (1995) Arthritis Rheum , vol.38 , pp. 164-172
    • Van de Loo, F.A.1    Joosten, L.A.2    Van Lent, P.L.3    Arntz, O.J.4    Van den Berg, W.B.5
  • 53
    • 0031194918 scopus 로고    scopus 로고
    • Effect of interleukin-1 and leukaemia inhibitory factor on chondrocyte metabolism in articular cartilage from normal and interleukin-6-deficient mice: Role of nitric oxide and IL-6 in the suppression of proteoglycan synthesis
    • van de Loo FA, Arntz OJ, van den Berg WB: Effect of interleukin-1 and leukaemia inhibitory factor on chondrocyte metabolism in articular cartilage from normal and interleukin-6-deficient mice: role of nitric oxide and IL-6 in the suppression of proteoglycan synthesis. Cytokine 1997, 9:453-462
    • (1997) Cytokine , vol.9 , pp. 453-462
    • Van de Loo, F.A.1    Arntz, O.J.2    Van den Berg, W.B.3
  • 55
    • 0033599563 scopus 로고    scopus 로고
    • A new member of tumor necrosis factor ligand family, ODF/OPGL/TRANCE/RANKL, regulates osteoclast differentiation and function
    • Takahashi N, Udagawa N, Suda T: A new member of tumor necrosis factor ligand family, ODF/OPGL/TRANCE/RANKL, regulates osteoclast differentiation and function. Biochem Biophys Res Commun 1999, 256:449-455
    • (1999) Biochem Biophys Res Commun , vol.256 , pp. 449-455
    • Takahashi, N.1    Udagawa, N.2    Suda, T.3
  • 57
    • 0027930553 scopus 로고
    • NADPH-oxidase expression and in situ production of superoxide by osteoclasts actively resorbing bone
    • Steinbeck MJ, Appel WH Jr, Verhoeven AJ, Karnovsky MJ: NADPH-oxidase expression and in situ production of superoxide by osteoclasts actively resorbing bone. J Cell Biol 1994, 126:765-772
    • (1994) J Cell Biol , vol.126 , pp. 765-772
    • Steinbeck, M.J.1    Appel W.H., Jr.2    Verhoeven, A.J.3    Karnovsky, M.J.4
  • 58
    • 0030247622 scopus 로고    scopus 로고
    • Hydrogen peroxide, but not superoxide, stimulates bone resorption in mouse calvariae
    • Fraser JH, Helfrich MH, Wallace HM, Ralston SH: Hydrogen peroxide, but not superoxide, stimulates bone resorption in mouse calvariae. Bone 1996, 19:223-226
    • (1996) Bone , vol.19 , pp. 223-226
    • Fraser, J.H.1    Helfrich, M.H.2    Wallace, H.M.3    Ralston, S.H.4
  • 59
    • 0035937121 scopus 로고    scopus 로고
    • A new superoxide-generating oxidase in murine osteoclasts
    • Yang S, Madyastha P, Bingel S, Ries W, Key L: A new superoxide-generating oxidase in murine osteoclasts. J Biol Chem 2001, 276:5452-5458
    • (2001) J Biol Chem , vol.276 , pp. 5452-5458
    • Yang, S.1    Madyastha, P.2    Bingel, S.3    Ries, W.4    Key, L.5
  • 61
    • 0029851956 scopus 로고    scopus 로고
    • Mice lacking tartrate-resistant acid phosphatase (Acp 5) have disrupted endochondral ossification and mild osteopetrosis
    • Hayman AR, Jones SJ, Boyde A, Foster D, Colledge WH, Carlton MB, Evans MJ, Cox TM: Mice lacking tartrate-resistant acid phosphatase (Acp 5) have disrupted endochondral ossification and mild osteopetrosis. Development 1996, 122:3151-3162
    • (1996) Development , vol.122 , pp. 3151-3162
    • Hayman, A.R.1    Jones, S.J.2    Boyde, A.3    Foster, D.4    Colledge, W.H.5    Carlton, M.B.6    Evans, M.J.7    Cox, T.M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.