메뉴 건너뛰기




Volumn 30, Issue 3, 1998, Pages 357-366

Antimalarial drugs inhibit phospholipase A2 activation and induction of interleukin 1β and tumor necrosis factor α in macrophages: Implications for their mode of action in rheumatoid arthritis

Author keywords

Antimalarials; Arachidonate; Chloroquine; Hydroxychloroquine; Interleukin 1; Phospholipase A2; Quinacrine; Tumor necrosis factor

Indexed keywords

ANTIMALARIAL AGENT; CHLOROQUINE; CYTOKINE; HYDROXYCHLOROQUINE; ICOSANOID; INTERLEUKIN 1BETA; MEPACRINE; PHOSPHOLIPASE A2; TUMOR NECROSIS FACTOR ALPHA;

EID: 0032033594     PISSN: 03063623     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0306-3623(97)00269-3     Document Type: Article
Times cited : (63)

References (35)
  • 1
    • 0027403224 scopus 로고
    • Interleukin-1-mediated phospholipid breakdown and arachidonic acid release in human synovial cells
    • Angel J., Colard O., Chevy F., Fournier C. Interleukin-1-mediated phospholipid breakdown and arachidonic acid release in human synovial cells. Arthritis Rheum. 36:1993;158-167.
    • (1993) Arthritis Rheum. , vol.36 , pp. 158-167
    • Angel, J.1    Colard, O.2    Chevy, F.3    Fournier, C.4
  • 2
    • 0028861236 scopus 로고
    • Inhibition of the production and effects of interleukin-1 and tumor necrosis factor α in rheumatoid arthritis
    • Arend W. P., Dayer J.-M. Inhibition of the production and effects of interleukin-1 and tumor necrosis factor α in rheumatoid arthritis. Arthritis Rheum. 38:1995;151-160.
    • (1995) Arthritis Rheum. , vol.38 , pp. 151-160
    • Arend, W.P.1    Dayer, J.-M.2
  • 3
    • 0017905777 scopus 로고
    • 2 activity of guinea-pig isolated perfused lungs: Stimulation, and inhibition by anti-inflammatory steroids
    • 2 activity of guinea-pig isolated perfused lungs. stimulation, and inhibition by anti-inflammatory steroids Br. J. Pharmac. 62:1978;79-89.
    • (1978) Br. J. Pharmac. , vol.62 , pp. 79-89
    • Blackwell, G.J.1    Flower, R.J.2    Nijkamp, F.P.3    Vane, J.R.4
  • 5
    • 0028169743 scopus 로고
    • 2 and subsequent eicosanoid formation in macrophages
    • 2 and subsequent eicosanoid formation in macrophages. Biochem. Pharmac. 48:1994;1171-1179.
    • (1994) Biochem. Pharmac. , vol.48 , pp. 1171-1179
    • Bondeson, J.1    Sundler, R.2
  • 6
    • 0029589336 scopus 로고
    • Auranofin inhibits the induction of interleukin 1β and tumor necrosis factor α in macrophages
    • Bondeson J., Sundler R. Auranofin inhibits the induction of interleukin 1β and tumor necrosis factor α in macrophages. Biochem. Pharmac. 50:1995;1753-1759.
    • (1995) Biochem. Pharmac. , vol.50 , pp. 1753-1759
    • Bondeson, J.1    Sundler, R.2
  • 7
    • 0029889270 scopus 로고    scopus 로고
    • Differential effects of tenidap on the zymosan- and lipopolysaccharide-induced expression of mRNA for proinflammatory cytokines in macrophages
    • Bondeson J., Sundler R. Differential effects of tenidap on the zymosan- and lipopolysaccharide-induced expression of mRNA for proinflammatory cytokines in macrophages. Biochem. Pharmac. 52:1996;35-42.
    • (1996) Biochem. Pharmac. , vol.52 , pp. 35-42
    • Bondeson, J.1    Sundler, R.2
  • 8
    • 0023277545 scopus 로고
    • Single-step method of mRNA isolation by acid guadinium thiocyanate-phenol-chloroform extraction
    • Chomzynski P., Sacchi N. Single-step method of mRNA isolation by acid guadinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomzynski, P.1    Sacchi, N.2
  • 9
    • 0026346448 scopus 로고
    • The effect of slow-acting anti-rheumatic drugs (SAARDs) and combinations of SAARDs on monokine production in vitro
    • Danis V. A., Franic G. M., Brooks P. M. The effect of slow-acting anti-rheumatic drugs (SAARDs) and combinations of SAARDs on monokine production in vitro. Drugs Exp. Clin. Res. 17:1991;549-554.
    • (1991) Drugs Exp. Clin. Res. , vol.17 , pp. 549-554
    • Danis, V.A.1    Franic, G.M.2    Brooks, P.M.3
  • 11
    • 0021356529 scopus 로고
    • Differential activation of phosphatidylinositol deacylation and a pathway via diphosphoinositide in macrophages responding to zymosan and ionophore A23187
    • Emilsson A., Sundler R. Differential activation of phosphatidylinositol deacylation and a pathway via diphosphoinositide in macrophages responding to zymosan and ionophore A23187. J. Biol. Chem. 259:1984;3111-3116.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3111-3116
    • Emilsson, A.1    Sundler, R.2
  • 12
    • 0025986663 scopus 로고
    • Chloroquine attenuates hemorrhagic shock-induced suppression of Kupffer cell antigen presentation and major histocompatibility complex class II antigen expression through blockade of tumor necrosis factor and prostaglandin release
    • Ertel W., Morrison M. H., Ayala A., Chaudry I. H. Chloroquine attenuates hemorrhagic shock-induced suppression of Kupffer cell antigen presentation and major histocompatibility complex class II antigen expression through blockade of tumor necrosis factor and prostaglandin release. Blood. 78:1991;1781-1788.
    • (1991) Blood , vol.78 , pp. 1781-1788
    • Ertel, W.1    Morrison, M.H.2    Ayala, A.3    Chaudry, I.H.4
  • 14
    • 0025084541 scopus 로고
    • The comparative efficacy and toxicity of second-line drugs in rheumatoid arthritis
    • Felson D. T., Anderson J. J., Meenan R. F. The comparative efficacy and toxicity of second-line drugs in rheumatoid arthritis. Arthritis Rheum. 33:1990;1449-1461.
    • (1990) Arthritis Rheum. , vol.33 , pp. 1449-1461
    • Felson, D.T.1    Anderson, J.J.2    Meenan, R.F.3
  • 16
    • 0028954072 scopus 로고
    • 2 in mouse macrophages and suppresses its activation
    • 2 in mouse macrophages and suppresses its activation. Biochem. J. 307:1995;499-504.
    • (1995) Biochem. J. , vol.307 , pp. 499-504
    • Gewert, K.1    Sundler, R.2
  • 17
    • 0019307389 scopus 로고
    • Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyne secretion by impairing receptor recycling
    • Gonzales-Noriega A., Grubb J. H., Talkad V., Sly W. S. Chloroquine inhibits lysosomal enzyme pinocytosis and enhances lysosomal enzyne secretion by impairing receptor recycling. J. Cell Biol. 85:1980;839-852.
    • (1980) J. Cell Biol. , vol.85 , pp. 839-852
    • Gonzales-Noriega, A.1    Grubb, J.H.2    Talkad, V.3    Sly, W.S.4
  • 19
    • 0022901544 scopus 로고
    • Differential effects of mepacrine, chloroquine and hydroxychloroquine on superoxide anion generation, phospholipid methylation and arachidonic acid release by human blood monocytes
    • Hurst N. P., French J. K., Bell A. L., Nuki G., O'Donnell M. L., Betts W. H., Cleland L. G. Differential effects of mepacrine, chloroquine and hydroxychloroquine on superoxide anion generation, phospholipid methylation and arachidonic acid release by human blood monocytes. Biochem. Pharm. 35:1986;3083-3089.
    • (1986) Biochem. Pharm. , vol.35 , pp. 3083-3089
    • Hurst, N.P.1    French, J.K.2    Bell, A.L.3    Nuki, G.4    O'Donnell, M.L.5    Betts, W.H.6    Cleland, L.G.7
  • 20
    • 0023270790 scopus 로고
    • Studies on the mechanism of inhibition of chemotactic tripeptide stimulated human neutrophil polymorphonuclear leucocyte superoxide production by chloroquine and hydroxychloroquine
    • Hurst N. P., French J. K., Gorjatschko L., Betts W. H. Studies on the mechanism of inhibition of chemotactic tripeptide stimulated human neutrophil polymorphonuclear leucocyte superoxide production by chloroquine and hydroxychloroquine. Ann. Rheum. Dis. 46:1987;750-756.
    • (1987) Ann. Rheum. Dis. , vol.46 , pp. 750-756
    • Hurst, N.P.1    French, J.K.2    Gorjatschko, L.3    Betts, W.H.4
  • 23
    • 0023686557 scopus 로고
    • Role of lysosomes in hepatic accumulation of chloroquine
    • MacIntyre A. C., Cutler D. J. Role of lysosomes in hepatic accumulation of chloroquine. J. Pharm. Sci. 77:1988;196-199.
    • (1988) J. Pharm. Sci. , vol.77 , pp. 196-199
    • MacIntyre, A.C.1    Cutler, D.J.2
  • 24
    • 0018942047 scopus 로고
    • Inhibition of lysosomal phospholipase A and phospholipase C by chloroquine and 4,4′-bis(diethylaminoethoxy)α,β-diethyldiphenylethane
    • Matsuzawa Y., Hostetler K. Y. Inhibition of lysosomal phospholipase A and phospholipase C by chloroquine and 4,4′-bis(diethylaminoethoxy)α,β-diethyldiphenylethane. J. Biol. Chem. 255:1980;5190-5194.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5190-5194
    • Matsuzawa, Y.1    Hostetler, K.Y.2
  • 25
  • 26
    • 0027517280 scopus 로고
    • Chloroquine-induced inhibition of the production of TNF, but not of IL-6, is affected by disruption of iron metabolism
    • Picot S., Peyron F., Donadille A., Vuillez J.-P., Barbe G., Ambroise-Thomas P. Chloroquine-induced inhibition of the production of TNF, but not of IL-6, is affected by disruption of iron metabolism. Immunology. 80:1993;127-133.
    • (1993) Immunology , vol.80 , pp. 127-133
    • Picot, S.1    Peyron, F.2    Donadille, A.3    Vuillez, J.-P.4    Barbe, G.5    Ambroise-Thomas, P.6
  • 27
    • 0019866088 scopus 로고
    • Effect of weak bases on the intralysosomal pH in mouse peritoneal macrophages
    • Poole B., Ohkuma S. Effect of weak bases on the intralysosomal pH in mouse peritoneal macrophages. J. Cell Biol. 90:1981;665-669.
    • (1981) J. Cell Biol. , vol.90 , pp. 665-669
    • Poole, B.1    Ohkuma, S.2
  • 28
    • 0021024776 scopus 로고
    • Mepacrine blockade of arachidonate-induced washed platelet aggregation: Relationship to mepacrine inhibition of platelet cyclooxygenase
    • Raz A. Mepacrine blockade of arachidonate-induced washed platelet aggregation. relationship to mepacrine inhibition of platelet cyclooxygenase Thromb. Haemostasis. 50:1983;784-786.
    • (1983) Thromb. Haemostasis , vol.50 , pp. 784-786
    • Raz, A.1
  • 29
    • 0020559879 scopus 로고
    • Immunosuppressive potential of antimalarials
    • Salmeron G., Lipsky P. E. Immunosuppressive potential of antimalarials. Am. J. Med. 75(Suppl.):1983;19-24.
    • (1983) Am. J. Med. , vol.75 , Issue.SUPPL. , pp. 19-24
    • Salmeron, G.1    Lipsky, P.E.2
  • 30
    • 0027155777 scopus 로고
    • Selective regulation of cytokine secretion by hydroxychloroquine: Inhibition of interleukin 1 alpha (IL-1-α) and IL-6 in human monocytes and T cells
    • Sperber K., Quraishi H., Kalb T. H., Panja A., Stecher V., Mayer L. Selective regulation of cytokine secretion by hydroxychloroquine. inhibition of interleukin 1 alpha (IL-1-α) and IL-6 in human monocytes and T cells J. Rheumatol. 20:1993;803-808.
    • (1993) J. Rheumatol. , vol.20 , pp. 803-808
    • Sperber, K.1    Quraishi, H.2    Kalb, T.H.3    Panja, A.4    Stecher, V.5    Mayer, L.6
  • 32
    • 0024383472 scopus 로고
    • The use of quinacrine (Atabrine) in rheumatic diseases: A reexamination
    • Wallace D. J. The use of quinacrine (Atabrine) in rheumatic diseases. a reexamination Semin. Arthritis Rheum. 18:1989;282-289.
    • (1989) Semin. Arthritis Rheum. , vol.18 , pp. 282-289
    • Wallace, D.J.1
  • 33
    • 0000699864 scopus 로고
    • Labilization and stabilization of lysosomes
    • Weissmann G. Labilization and stabilization of lysosomes. Fed. Proc. 23:1964;1038-1044.
    • (1964) Fed. Proc. , vol.23 , pp. 1038-1044
    • Weissmann, G.1
  • 34
    • 0024494378 scopus 로고
    • A role for the protein kinase C-mediated phosphorylation in the mobilization of arachidonic acid in macrophages
    • Wijkander J., Sundler R. A role for the protein kinase C-mediated phosphorylation in the mobilization of arachidonic acid in macrophages. Biochim. Biophys. Acta. 1010:1989;78-87.
    • (1989) Biochim. Biophys. Acta , vol.1010 , pp. 78-87
    • Wijkander, J.1    Sundler, R.2
  • 35
    • 0027361813 scopus 로고
    • Chloroquine inhibits macrophage tumour necrosis factor-α mRNA transcription
    • Zhu X., Ertel W., Ayala A., Morrison M. H., Perrin M. M., Chaudry I. H. Chloroquine inhibits macrophage tumour necrosis factor-α mRNA transcription. Immunology. 80:1993;122-126.
    • (1993) Immunology , vol.80 , pp. 122-126
    • Zhu, X.1    Ertel, W.2    Ayala, A.3    Morrison, M.H.4    Perrin, M.M.5    Chaudry, I.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.