메뉴 건너뛰기




Volumn 22, Issue 6, 2000, Pages 431-443

Differential regulation of type IV collagenases and metalloelastase in murine macrophages by the synthetic bacterial lipopeptide JBT 3002

Author keywords

Lipopeptide; Macrophages; Metalloelastase; Metalloproteinases

Indexed keywords

ELASTASE; GAMMA INTERFERON; GELATINASE A; GELATINASE B; LIPOPEPTIDE; MATRIX METALLOPROTEINASE; N(G) METHYLARGININE; NITRIC OXIDE; TISSUE INHIBITOR OF METALLOPROTEINASE 1;

EID: 0034113374     PISSN: 01920561     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0192-0561(00)00008-4     Document Type: Article
Times cited : (6)

References (51)
  • 1
    • 0026896029 scopus 로고
    • The matrix-degrading metalloproteinases
    • Matrisian L.M. The matrix-degrading metalloproteinases. Bioassays. 14:1992;455-463.
    • (1992) Bioassays , vol.14 , pp. 455-463
    • Matrisian, L.M.1
  • 2
    • 0025637148 scopus 로고
    • Regulation of extracellular matrix-degradation by cell-extracellular matrix interactions
    • Werb Z., Tremble P., Damsky C.H. Regulation of extracellular matrix-degradation by cell-extracellular matrix interactions. Cell Differen. Dev. 32:1990;299-306.
    • (1990) Cell Differen. Dev. , vol.32 , pp. 299-306
    • Werb, Z.1    Tremble, P.2    Damsky, C.H.3
  • 3
    • 0024712236 scopus 로고
    • Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage
    • Dean D.D., Martel-Pelleier J., Pelleter J.P., Howell D.S., Woessner J.F. Jr. Evidence for metalloproteinase and metalloproteinase inhibitor imbalance in human osteoarthritic cartilage. J. Clin. Invest. 84:1989;678-685.
    • (1989) J. Clin. Invest. , vol.84 , pp. 678-685
    • Dean, D.D.1    Martel-Pelleier, J.2    Pelleter, J.P.3    Howell, D.S.4    Woessner J.F., Jr.5
  • 5
    • 0030823772 scopus 로고    scopus 로고
    • Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice
    • Hautamaki R.D., Kobayashi D.K., Senior R.M., Shapiro S.D. Requirement for macrophage elastase for cigarette smoke-induced emphysema in mice. Science. 277:1997;2002-2004.
    • (1997) Science , vol.277 , pp. 2002-2004
    • Hautamaki, R.D.1    Kobayashi, D.K.2    Senior, R.M.3    Shapiro, S.D.4
  • 6
    • 0022969477 scopus 로고
    • Tumor invasion through the human amniotic membrane: Requirement for a proteinase cascade
    • Mignatti P., Robbins E., Rifkin D.B. Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade. Cell. 47:1986;487-498.
    • (1986) Cell , vol.47 , pp. 487-498
    • Mignatti, P.1    Robbins, E.2    Rifkin, D.B.3
  • 7
    • 0025641098 scopus 로고
    • A novel metalloproteinase gene specifically expressed: Stromal cells of breast carcinoma
    • Basset P., Bellocq J.P., Wolf C., Stoll I., Limacher J.M., Podhajeer O.L., et al. A novel metalloproteinase gene specifically expressed: stromal cells of breast carcinoma. Nature. 348:1990;699-704.
    • (1990) Nature , vol.348 , pp. 699-704
    • Basset, P.1    Bellocq, J.P.2    Wolf, C.3    Stoll, I.4    Limacher, J.M.5    Podhajeer, O.L.6
  • 8
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner J.F. Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5:1991;2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner J.F., Jr.1
  • 9
    • 0024241283 scopus 로고
    • Selective upregulation of human alveolar macrophage collagenase production by lipopolysaccharide and comparison to collagenase production by fibroblasts
    • Cury J.D., Campbell E.J., Lazarus C.J., Albin R.J., Welgus H.G. Selective upregulation of human alveolar macrophage collagenase production by lipopolysaccharide and comparison to collagenase production by fibroblasts. J. Immunol. 141:1988;4306-4312.
    • (1988) J. Immunol. , vol.141 , pp. 4306-4312
    • Cury, J.D.1    Campbell, E.J.2    Lazarus, C.J.3    Albin, R.J.4    Welgus, H.G.5
  • 10
    • 0025059594 scopus 로고
    • Neutral metalloproteinases produced by human mononuclear phagocytes: Enzyme profile, regulation, and expression during cellular development
    • Welgus H.G., Campbell E.J., Curry J.D., Eisen A.Z., Senior R.M., Wilhelm S.M. Neutral metalloproteinases produced by human mononuclear phagocytes: enzyme profile, regulation, and expression during cellular development. J. Clin. Invest. 86:1990;1496-1502.
    • (1990) J. Clin. Invest. , vol.86 , pp. 1496-1502
    • Welgus, H.G.1    Campbell, E.J.2    Curry, J.D.3    Eisen, A.Z.4    Senior, R.M.5    Wilhelm, S.M.6
  • 11
    • 0023665299 scopus 로고
    • Monocyte procollagenase and tissue inhibitor of metalloproteinase: Identification, characterization, and regulation of secretion
    • Campbell E.J., Cury J.D., Lazarus C.J., Welgus H.G. Monocyte procollagenase and tissue inhibitor of metalloproteinase: identification, characterization, and regulation of secretion. J. Biol. Chem. 262:1987;15862-15868.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15862-15868
    • Campbell, E.J.1    Cury, J.D.2    Lazarus, C.J.3    Welgus, H.G.4
  • 12
    • 0028267620 scopus 로고
    • Regulatory mechanisms for the expression of type IV collagenases/gelatinases in murine macrophages
    • Xie B., Dong Z., Fidler I.J. Regulatory mechanisms for the expression of type IV collagenases/gelatinases in murine macrophages. J. Immunol. 152:1994;3637-3644.
    • (1994) J. Immunol. , vol.152 , pp. 3637-3644
    • Xie, B.1    Dong, Z.2    Fidler, I.J.3
  • 13
    • 0023514969 scopus 로고
    • Expression of a metalloproteinase that degrades native type V collagen and denatured collagens by cultured human alveolar macrophages
    • Hibbs M.S., Hoidal J.R., Kang A.J. Expression of a metalloproteinase that degrades native type V collagen and denatured collagens by cultured human alveolar macrophages. J. Clin. Invest. 80:1987;1644-1650.
    • (1987) J. Clin. Invest. , vol.80 , pp. 1644-1650
    • Hibbs, M.S.1    Hoidal, J.R.2    Kang, A.J.3
  • 14
    • 0027435065 scopus 로고
    • Tissue inhibitor of metalloproteinases (TIMP, aka EPA): Structure, control of expression and biological functions
    • Denhardt D.T., Feng B., Edwards D.R., Cocuzzi E.T., Malayanka U.M. Tissue inhibitor of metalloproteinases (TIMP, aka EPA): structure, control of expression and biological functions. Pharmacol. Ther. 59:1993;329-341.
    • (1993) Pharmacol. Ther. , vol.59 , pp. 329-341
    • Denhardt, D.T.1    Feng, B.2    Edwards, D.R.3    Cocuzzi, E.T.4    Malayanka, U.M.5
  • 15
    • 0030469388 scopus 로고    scopus 로고
    • Differential regulation of metalloelastase activity in murine peritoneal macrophages by granulocyte-macrophage colony-stimulating factor and macrophage colony-stimulating factor
    • Kumar R., Dong Z., Fidler I.J. Differential regulation of metalloelastase activity in murine peritoneal macrophages by granulocyte-macrophage colony-stimulating factor and macrophage colony-stimulating factor. J. Immunol. 157:1996;5104-5111.
    • (1996) J. Immunol. , vol.157 , pp. 5104-5111
    • Kumar, R.1    Dong, Z.2    Fidler, I.J.3
  • 16
    • 0016699108 scopus 로고
    • Elastase secretion by stimulated macrophages: Characterization and regulation
    • Werb Z., Gordon S. Elastase secretion by stimulated macrophages: characterization and regulation. J. Exp. Med. 142:1975;361-377.
    • (1975) J. Exp. Med. , vol.142 , pp. 361-377
    • Werb, Z.1    Gordon, S.2
  • 17
    • 0026762898 scopus 로고
    • Identification of TIMP-2 in human alveolar macrophages. Regulation of biosynthesis is opposite to that of metalloproteinases and TIMP-1
    • Shapiro S.D., Kobayashi D.K., Welgus H.G. Identification of TIMP-2 in human alveolar macrophages. Regulation of biosynthesis is opposite to that of metalloproteinases and TIMP-1. J. Biol. Chem. 267:1992;13890-13894.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13890-13894
    • Shapiro, S.D.1    Kobayashi, D.K.2    Welgus, H.G.3
  • 18
    • 0027012631 scopus 로고
    • Neutral proteinase expression by human mononuclear phagocytes: A prominent role of cellular differentiation
    • Welgus H.G., Senior R.M., Parks W.C., Kahn A.J., Ley T.J., Shapiro S.D., et al. Neutral proteinase expression by human mononuclear phagocytes: a prominent role of cellular differentiation. Matrix (suppl.). 1:1992;363-367.
    • (1992) Matrix (Suppl.) , vol.1 , pp. 363-367
    • Welgus, H.G.1    Senior, R.M.2    Parks, W.C.3    Kahn, A.J.4    Ley, T.J.5    Shapiro, S.D.6
  • 20
    • 0022254467 scopus 로고
    • Tumor-promoting phorbol esters and cell proliferation stimulate secretion of basement membrane (type IV) collagen-degrading metalloproteinases by human fibroblasts
    • Salo T., Turpeenniemi-Hujanen T., Tryggvason K. Tumor-promoting phorbol esters and cell proliferation stimulate secretion of basement membrane (type IV) collagen-degrading metalloproteinases by human fibroblasts. J. Biol. Chem. 260:1985;8526-8531.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8526-8531
    • Salo, T.1    Turpeenniemi-Hujanen, T.2    Tryggvason, K.3
  • 21
    • 0027223141 scopus 로고
    • Regulation of matrix metalloproteinases: Their role in tumor invasion and metastasis
    • Cottam D.W., Rees R.C. Regulation of matrix metalloproteinases: their role in tumor invasion and metastasis. Int. J. Oncol. 2:1993;861-869.
    • (1993) Int. J. Oncol. , vol.2 , pp. 861-869
    • Cottam, D.W.1    Rees, R.C.2
  • 22
    • 0030292766 scopus 로고    scopus 로고
    • TNF-α And IL-β selectively induce expression of 92-kDa gelatinase by human macrophages
    • Saren P., Welgus H.G., Kovanen P.T. TNF-α and IL-β selectively induce expression of 92-kDa gelatinase by human macrophages. J. Immunol. 157:1996;4159-4165.
    • (1996) J. Immunol. , vol.157 , pp. 4159-4165
    • Saren, P.1    Welgus, H.G.2    Kovanen, P.T.3
  • 23
    • 0025134586 scopus 로고
    • Immune modulation of metalloproteinase production in human macrophages. Selective pretranslational suppression of interstitial collagenase and stromelysin biosynthesis by interferon-γ
    • Shapiro S.D., Campbell E.J., Kobayashi D.K., Welgus H.G. Immune modulation of metalloproteinase production in human macrophages. Selective pretranslational suppression of interstitial collagenase and stromelysin biosynthesis by interferon-γ J. Clin. Invest. 86:1990;1204-1210.
    • (1990) J. Clin. Invest. , vol.86 , pp. 1204-1210
    • Shapiro, S.D.1    Campbell, E.J.2    Kobayashi, D.K.3    Welgus, H.G.4
  • 24
    • 0028900052 scopus 로고
    • Immobilized anti-CD3 antibody activates T cell clones to induce the production of interstitial collagenase, but not tissue inhibitor of metalloproteinases, in monocyte THP-1 cells and dermal fibroblasts
    • Miltenburg A.M., Lacraz S., Welgus H.G., Dayer J.-M. Immobilized anti-CD3 antibody activates T cell clones to induce the production of interstitial collagenase, but not tissue inhibitor of metalloproteinases, in monocyte THP-1 cells and dermal fibroblasts. J. Immunol. 154:1995;2655-2667.
    • (1995) J. Immunol. , vol.154 , pp. 2655-2667
    • Miltenburg, A.M.1    Lacraz, S.2    Welgus, H.G.3    Dayer, J.-M.4
  • 25
    • 0028021464 scopus 로고
    • Direct contact between T lymphocytes and monocytes is a major pathway for induction of metalloproteinase expression
    • Lacraz S., Isler P., Vey E., Welgus H.G., Dayer J.-M. Direct contact between T lymphocytes and monocytes is a major pathway for induction of metalloproteinase expression. J. Biol. Chem. 269:1994;22027-22033.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22027-22033
    • Lacraz, S.1    Isler, P.2    Vey, E.3    Welgus, H.G.4    Dayer, J.-M.5
  • 26
    • 0029026517 scopus 로고
    • Matrilysin expression by human mononuclear phagocytes and its regulation by cytokines and hormones
    • Busiek D.F., Baragi V., Nehring L.C., Parks W.C., Welgus H.G. Matrilysin expression by human mononuclear phagocytes and its regulation by cytokines and hormones. J. Immunol. 154:1995;6484-6491.
    • (1995) J. Immunol. , vol.154 , pp. 6484-6491
    • Busiek, D.F.1    Baragi, V.2    Nehring, L.C.3    Parks, W.C.4    Welgus, H.G.5
  • 27
    • 0026515544 scopus 로고
    • 2 synthesis blocks interstitial collagenase and 92-kDa type IV collagenase/gelatinase production by human monocytes
    • 2 synthesis blocks interstitial collagenase and 92-kDa type IV collagenase/gelatinase production by human monocytes. J. Biol. Chem. 267:1992;515-519.
    • (1992) J. Biol. Chem. , vol.267 , pp. 515-519
    • Corcoran, M.L.1    Stetler-Stevenson, W.G.2    Brown, P.D.3    Wahl, L.M.4
  • 28
    • 0027990831 scopus 로고
    • Interleukin 10 suppression of monocyte prostaglandin H synthase-2: Mechanism of inhibition of prostaglandin-dependent matrix metalloproteinase production
    • Mertz P.M., DeWitt D.L., Stetler-Stevenson W.G., Wahl L.M. Interleukin 10 suppression of monocyte prostaglandin H synthase-2: mechanism of inhibition of prostaglandin-dependent matrix metalloproteinase production. J. Biol. Chem. 269:1994;21322-21329.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21322-21329
    • Mertz, P.M.1    Dewitt, D.L.2    Stetler-Stevenson, W.G.3    Wahl, L.M.4
  • 29
    • 0025239695 scopus 로고
    • Inhibition of phospholipase activity in human monocytes by IFN-γ blocks endogenous prostaglandin E2-dependent collagenase production
    • Wahl L.M., Corcoran M.L., Mergenhagen S.E., Finbloom D.S. Inhibition of phospholipase activity in human monocytes by IFN-γ blocks endogenous prostaglandin E2-dependent collagenase production. J. Immunol. 144:1990;3518-3522.
    • (1990) J. Immunol. , vol.144 , pp. 3518-3522
    • Wahl, L.M.1    Corcoran, M.L.2    Mergenhagen, S.E.3    Finbloom, D.S.4
  • 30
    • 0028855894 scopus 로고
    • IL-10 inhibits metalloproteinase and stimulates TIMP-1 production in human mononuclear phagocytes
    • Lacraz S., Nicod L.P., Chicheportiche R., Welgus H.G., Dayer J.-M. IL-10 inhibits metalloproteinase and stimulates TIMP-1 production in human mononuclear phagocytes. J. Clin. Invest. 96:1995;2304-2310.
    • (1995) J. Clin. Invest. , vol.96 , pp. 2304-2310
    • Lacraz, S.1    Nicod, L.P.2    Chicheportiche, R.3    Welgus, H.G.4    Dayer, J.-M.5
  • 31
    • 0025734094 scopus 로고
    • Interleukin-6 induces the synthesis of tissue inhibitor of metalloproteinase-1/erythroid potentiating activity (TIMP-1/EPA)
    • Lotz M., Guerne P.-A. Interleukin-6 induces the synthesis of tissue inhibitor of metalloproteinase-1/erythroid potentiating activity (TIMP-1/EPA). J. Biol. Chem. 266:1991;2017-2020.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2017-2020
    • Lotz, M.1    Guerne, P.-A.2
  • 32
    • 0027419081 scopus 로고
    • Induction of macrophage metalloproteinases by extracellular matrix: Evidence for enzyme- And substrate-specific responses involving prostaglandin-dependent mechanisms
    • Shapiro S.D., Kobayashi D.K., Pentland A.P., Welgus H.G. Induction of macrophage metalloproteinases by extracellular matrix: evidence for enzyme- and substrate-specific responses involving prostaglandin-dependent mechanisms. J. Biol. Chem. 268:1993;8170-8175.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8170-8175
    • Shapiro, S.D.1    Kobayashi, D.K.2    Pentland, A.P.3    Welgus, H.G.4
  • 33
    • 0028932594 scopus 로고
    • Laminin SIKVAV peptide induction of monocyte/macrophage prostaglandin E2 and matrix metalloproteinases
    • Corcoran M.L., Kibbey M.C., Kleinman H.K., Wahl L.M. Laminin SIKVAV peptide induction of monocyte/macrophage prostaglandin E2 and matrix metalloproteinases. J. Biol. Chem. 270:1995;10365-10368.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10365-10368
    • Corcoran, M.L.1    Kibbey, M.C.2    Kleinman, H.K.3    Wahl, L.M.4
  • 35
    • 0025896343 scopus 로고
    • Comparative efficacy of liposomes containing synthetic bacterial cell wall analogues for tumoricidal activation of monocytes and macrophages
    • Utsugi T., Nii A., Fan D., Pak C., Denkins Y., van Hoogevest P., et al. Comparative efficacy of liposomes containing synthetic bacterial cell wall analogues for tumoricidal activation of monocytes and macrophages. Cancer Immunol. Immunother. 33:1991;285-292.
    • (1991) Cancer Immunol. Immunother. , vol.33 , pp. 285-292
    • Utsugi, T.1    Nii, A.2    Fan, D.3    Pak, C.4    Denkins, Y.5    Van Hoogevest, P.6
  • 36
    • 0025836425 scopus 로고
    • In situ activation of mouse macrophages and therapy of spontaneous renal cell cancer metastasis by liposomes containing the lipopeptide CGP 31362
    • Utsugi T., Dinney C.P.N., Killion J.J., Fidler I.J. In situ activation of mouse macrophages and therapy of spontaneous renal cell cancer metastasis by liposomes containing the lipopeptide CGP 31362. Cancer Immunol. Immunother. 33:1991;375-381.
    • (1991) Cancer Immunol. Immunother. , vol.33 , pp. 375-381
    • Utsugi, T.1    Dinney, C.P.N.2    Killion, J.J.3    Fidler, I.J.4
  • 37
    • 0025915955 scopus 로고
    • Optimization of the liposomes encapsulating a new lipopeptide CGP 31362 for efficient activation of tumoricidal properties in monocytes and macrophages
    • Nii A., Utsugi T., Fan D., Denkins Y., Pak C., Brown D., et al. Optimization of the liposomes encapsulating a new lipopeptide CGP 31362 for efficient activation of tumoricidal properties in monocytes and macrophages. J. Immunother. 10:1991;236-246.
    • (1991) J. Immunother. , vol.10 , pp. 236-246
    • Nii, A.1    Utsugi, T.2    Fan, D.3    Denkins, Y.4    Pak, C.5    Brown, D.6
  • 38
    • 0031657036 scopus 로고    scopus 로고
    • Induction of nitric oxide production and tumoricidal properties in murine macrophages by a new synthetic lipopeptide JBT 3002 encapsulated in liposomes
    • Eue I., Kumar R., Dong Z., Killion J.J., Fidler I.J. Induction of nitric oxide production and tumoricidal properties in murine macrophages by a new synthetic lipopeptide JBT 3002 encapsulated in liposomes. J. Immunother. 21:1998;340-351.
    • (1998) J. Immunother. , vol.21 , pp. 340-351
    • Eue, I.1    Kumar, R.2    Dong, Z.3    Killion, J.J.4    Fidler, I.J.5
  • 39
    • 0031441681 scopus 로고    scopus 로고
    • Expression of inflammatory cytokines by murine macrophages activated with a new synthetic lipopeptide JBT 3002
    • Kumar R., Eue I., Dong Z., Killion J.J., Fidler I.J. Expression of inflammatory cytokines by murine macrophages activated with a new synthetic lipopeptide JBT 3002. Cancer Biother. Radiopharmacol. 12:1997;333-340.
    • (1997) Cancer Biother. Radiopharmacol. , vol.12 , pp. 333-340
    • Kumar, R.1    Eue, I.2    Dong, Z.3    Killion, J.J.4    Fidler, I.J.5
  • 40
    • 0031748142 scopus 로고    scopus 로고
    • Activation of cytokine production and tumoricidal properties in human monocytes by a new synthetic lipopeptide JBT 3002 is independent of binding to serum LPS-binding protein and CD14
    • Dong Z., Killion J.J., Kumar R., Eue I., Yang X., Lu W., et al. Activation of cytokine production and tumoricidal properties in human monocytes by a new synthetic lipopeptide JBT 3002 is independent of binding to serum LPS-binding protein and CD14. J. Leukoc. Biol. 63:1998;766-774.
    • (1998) J. Leukoc. Biol. , vol.63 , pp. 766-774
    • Dong, Z.1    Killion, J.J.2    Kumar, R.3    Eue, I.4    Yang, X.5    Lu, W.6
  • 41
    • 0028999596 scopus 로고
    • Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase
    • MacMiking J.D., Nathan C., Hom G., et al. Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase. Cell. 81:1995;641-650.
    • (1995) Cell , vol.81 , pp. 641-650
    • MacMiking, J.D.1    Nathan, C.2    Hom, G.3
  • 42
    • 0020061756 scopus 로고
    • Effects of liposome structure and lipid composition on the activation of the tumoricidal properties of macrophages by liposomes containing muramyl dipeptide
    • Schroit A.J., Fidler I.J. Effects of liposome structure and lipid composition on the activation of the tumoricidal properties of macrophages by liposomes containing muramyl dipeptide. Cancer Res. 42:1982;161-167.
    • (1982) Cancer Res. , vol.42 , pp. 161-167
    • Schroit, A.J.1    Fidler, I.J.2
  • 43
    • 0021826891 scopus 로고
    • Synergistic activation by recombinant mouse IFN-γ And muramyl dipeptide of tumoricidal properties in mouse macrophages
    • Saiki I., Fidler I.J. Synergistic activation by recombinant mouse IFN-γ and muramyl dipeptide of tumoricidal properties in mouse macrophages. J. Immunol. 135:1985;684-688.
    • (1985) J. Immunol. , vol.135 , pp. 684-688
    • Saiki, I.1    Fidler, I.J.2
  • 44
    • 0020494591 scopus 로고
    • Detergent activation of latent collagenase and resolution of its component molecules
    • Birkedal-Hansen H., Taylor R.E. Detergent activation of latent collagenase and resolution of its component molecules. Biochem. Biophys. Res. Commun. 107:1982;1173-1178.
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 1173-1178
    • Birkedal-Hansen, H.1    Taylor, R.E.2
  • 45
    • 0027382375 scopus 로고
    • Taxol shares the ability of bacterial lipopolysaccharide to induce tyrosine phosphorylation of microtubule-associated protein kinase
    • Ding A., Sanchez E., Nathan C.F. Taxol shares the ability of bacterial lipopolysaccharide to induce tyrosine phosphorylation of microtubule-associated protein kinase. J. Immunol. 151:1993;5596-5602.
    • (1993) J. Immunol. , vol.151 , pp. 5596-5602
    • Ding, A.1    Sanchez, E.2    Nathan, C.F.3
  • 46
    • 0022552224 scopus 로고
    • Human recombinant interleukin-1 stimulates collagenase and prostaglandin E2 production by human synovial cells
    • Dayer J.M., de Rochemonteix B., Burrus B., Demczuk S., Dinarello C.A. Human recombinant interleukin-1 stimulates collagenase and prostaglandin E2 production by human synovial cells. J. Clin. Invest. 77:1986;645-648.
    • (1986) J. Clin. Invest. , vol.77 , pp. 645-648
    • Dayer, J.M.1    De Rochemonteix, B.2    Burrus, B.3    Demczuk, S.4    Dinarello, C.A.5
  • 47
    • 0022296893 scopus 로고
    • Cachectin tumor necrosis factor stimulates collagenase and prostaglandin E2 production by human synovial cells and dermal fibroblasts
    • Dayer J.M., Beutler B., Cerami A. Cachectin tumor necrosis factor stimulates collagenase and prostaglandin E2 production by human synovial cells and dermal fibroblasts. J. Exp. Med. 162:1985;2163-2168.
    • (1985) J. Exp. Med. , vol.162 , pp. 2163-2168
    • Dayer, J.M.1    Beutler, B.2    Cerami, A.3
  • 48
    • 0345214235 scopus 로고
    • Stimulation of rheumatoid synovial cell collagenase and prostaglandin production by partially purified lymphocyte-activating factor (interleukin-1)
    • Mizel S.B., Dayer J.M., Krane S.M., Mergenhagen S.E. Stimulation of rheumatoid synovial cell collagenase and prostaglandin production by partially purified lymphocyte-activating factor (interleukin-1). Proc. Natl. Acad. Sci. USA. 78:1981;2474-2477.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2474-2477
    • Mizel, S.B.1    Dayer, J.M.2    Krane, S.M.3    Mergenhagen, S.E.4
  • 49
    • 0025065325 scopus 로고
    • Gene regulation in macrophage activation: Differential regulation of genes encoding for tumor necrosis factor, interleukin-1. JE and KC by interferon-γ And lipopolysaccharide
    • Yu S.F., Koerner T.J., Adams D.O. Gene regulation in macrophage activation: differential regulation of genes encoding for tumor necrosis factor, interleukin-1. JE and KC by interferon-γ and lipopolysaccharide. J. Leukoc. Biol. 48:1990;412-419.
    • (1990) J. Leukoc. Biol. , vol.48 , pp. 412-419
    • Yu, S.F.1    Koerner, T.J.2    Adams, D.O.3
  • 50
    • 0026629902 scopus 로고
    • Nitric oxide as a secretary product of mammalian cells
    • Nathan C. Nitric oxide as a secretary product of mammalian cells. FASEB J. 6:1992;3051-3064.
    • (1992) FASEB J. , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 51
    • 0028853421 scopus 로고
    • Characterization of nitric oxide-stimulated ADP-ribosylation of various proteins from the mouse macrophage cell line ANA-1 using sodium nitroprusside and the novel nitric oxide-donating compound diethylamine dinitric oxide
    • Sheffler L.A., Wink D.A., Melillo G., Cox G.W. Characterization of nitric oxide-stimulated ADP-ribosylation of various proteins from the mouse macrophage cell line ANA-1 using sodium nitroprusside and the novel nitric oxide-donating compound diethylamine dinitric oxide. J. Leukoc. Biol. 57:1995;152-159.
    • (1995) J. Leukoc. Biol. , vol.57 , pp. 152-159
    • Sheffler, L.A.1    Wink, D.A.2    Melillo, G.3    Cox, G.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.