메뉴 건너뛰기




Volumn 161, Issue 3, 1998, Pages 1525-1532

Sustained phosphorylation of cytosolic phospholipase A2 accompanies cycloheximide- and adenovirus-induced susceptibility to TNF

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOHEXIMIDE; MITOGEN ACTIVATED PROTEIN KINASE; ORTHOVANADIC ACID; PHOSPHATASE INHIBITOR; PHOSPHOLIPASE A2; PHOSPHOPROTEIN; RECOMBINANT TUMOR NECROSIS FACTOR; UNCLASSIFIED DRUG; VERAPAMIL;

EID: 0032146856     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (15)

References (64)
  • 2
    • 0022633381 scopus 로고
    • Recombinant TNF: Its effect and its synergism with IFN-γ on a variety of normal and transformed cell lines
    • Fransen, L., J. Van Der Heyden, R. Ruysschaert, and W. Fiers. 1986. Recombinant TNF: its effect and its synergism with IFN-γ on a variety of normal and transformed cell lines. Eur. J. Cancer Clin. Oncol. 22:419.
    • (1986) Eur. J. Cancer Clin. Oncol. , vol.22 , pp. 419
    • Fransen, L.1    Van Der Heyden, J.2    Ruysschaert, R.3    Fiers, W.4
  • 3
    • 0019818075 scopus 로고
    • Possible requirement of internalization in the mechanism of in vitro cytotoxicity in tumor necrosis serum
    • Kull, F. C., and P. Cuatrecasas. 1981. Possible requirement of internalization in the mechanism of in vitro cytotoxicity in tumor necrosis serum. Cancer Res. 41:4885.
    • (1981) Cancer Res. , vol.41 , pp. 4885
    • Kull, F.C.1    Cuatrecasas, P.2
  • 4
    • 0018349752 scopus 로고
    • Stimulation of RNA synthesis in L929 cells by rabbit TNF
    • Ostrove, J. M., and G. E. Gifford. 1979. Stimulation of RNA synthesis in L929 cells by rabbit TNF. Proc. Soc. Exp. Biol. Med. 160:354.
    • (1979) Proc. Soc. Exp. Biol. Med. , vol.160 , pp. 354
    • Ostrove, J.M.1    Gifford, G.E.2
  • 5
    • 0024428198 scopus 로고
    • Manganous Superoxide dismutase is essential for cellular resistance to cytotoxicity of TNF
    • Wong, G. H. W., J. H. Elwell, L. W. Oberley, and D. V. Goeddel. 1989. Manganous Superoxide dismutase is essential for cellular resistance to cytotoxicity of TNF. Cell 58:923.
    • (1989) Cell , vol.58 , pp. 923
    • Wong, G.H.W.1    Elwell, J.H.2    Oberley, L.W.3    Goeddel, D.V.4
  • 6
    • 0025764038 scopus 로고
    • Sensitivity to TNF-mediated cytolysis is unrelated to manganous Superoxide dismutase messenger RNA levels among transformed mouse fibroblasts
    • Boss, J. M., S. M. Laster, and L. R. Gooding. 1991. Sensitivity to TNF-mediated cytolysis is unrelated to manganous Superoxide dismutase messenger RNA levels among transformed mouse fibroblasts. Immunology 73:309.
    • (1991) Immunology , vol.73 , pp. 309
    • Boss, J.M.1    Laster, S.M.2    Gooding, L.R.3
  • 7
    • 0025746246 scopus 로고
    • Protection from TNF-mediated cytolysis by overexpression of plasminogen activator inhibitor type-2
    • Kumar, S., and C. Baglioni. 1991. Protection from TNF-mediated cytolysis by overexpression of plasminogen activator inhibitor type-2. J. Biol. Chem. 266:20960.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20960
    • Kumar, S.1    Baglioni, C.2
  • 8
    • 0025103776 scopus 로고
    • Plasminogen activator inhibitor type-2 is a major protein induced in human fibroblasts and SK-MEL-109 melanoma cells by TNF
    • Pytel, B. A., K. Peppel, and C. Baglioni. 1990. Plasminogen activator inhibitor type-2 is a major protein induced in human fibroblasts and SK-MEL-109 melanoma cells by TNF. J. Cell. Physiol. 144:416.
    • (1990) J. Cell. Physiol. , vol.144 , pp. 416
    • Pytel, B.A.1    Peppel, K.2    Baglioni, C.3
  • 9
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-KB in preventing TNF-α-induced cell death
    • Beg, A. A., and D. Baltimore. 1996. An essential role for NF-KB in preventing TNF-α-induced cell death. Science 274:782.
    • (1996) Science , vol.274 , pp. 782
    • Beg, A.A.1    Baltimore, D.2
  • 12
    • 0024852851 scopus 로고
    • Adenovirus E1A renders infected cells sensitive to cytolysis by TNF
    • Duerksen-Hughes, P., W. S. M. Wold, and L. R. Gooding. 1989. Adenovirus E1A renders infected cells sensitive to cytolysis by TNF. J. Immunol. 143:4193.
    • (1989) J. Immunol. , vol.143 , pp. 4193
    • Duerksen-Hughes, P.1    Wold, W.S.M.2    Gooding, L.R.3
  • 13
    • 0030787584 scopus 로고    scopus 로고
    • Hepatitis B virus HBx protein sensitizes cells to apoptotic killing by TNF
    • Su, F., and R. J. Schneider. 1997. Hepatitis B virus HBx protein sensitizes cells to apoptotic killing by TNF. Proc. Natl. Acad. Aci USA 94:8744.
    • (1997) Proc. Natl. Acad. Aci USA , vol.94 , pp. 8744
    • Su, F.1    Schneider, R.J.2
  • 14
    • 0023723833 scopus 로고
    • Newcastle disease virus as an antineoplastic agent: Induction of TNF-α and augmentation of its cytotoxicity
    • Lorence, R. M., P. A. Rood, and K. W. Kelley. 1988. Newcastle disease virus as an antineoplastic agent: induction of TNF-α and augmentation of its cytotoxicity. J. Natl. Cancer Inst. 80:1305.
    • (1988) J. Natl. Cancer Inst. , vol.80 , pp. 1305
    • Lorence, R.M.1    Rood, P.A.2    Kelley, K.W.3
  • 15
    • 0024360335 scopus 로고
    • Cytocidal effect of TNF on cells chronically infected with human immunodeficiency virus (HIV): Enhancement of HIV replication
    • Matsuyama, T., Y. Hamamoto, G.-I. Soma, D. Mizuno, N. Yamamoto, and N. Kobyashi. 1989. Cytocidal effect of TNF on cells chronically infected with human immunodeficiency virus (HIV): enhancement of HIV replication. J. Virol. 63:2504.
    • (1989) J. Virol. , vol.63 , pp. 2504
    • Matsuyama, T.1    Hamamoto, Y.2    Soma, G.-I.3    Mizuno, D.4    Yamamoto, N.5    Kobyashi, N.6
  • 16
    • 0022920868 scopus 로고
    • Human TNF-α kills herpes virus-infected cells but not normal cells
    • Koff, W. C., and A. V. Fann. 1986. Human TNF-α kills herpes virus-infected cells but not normal cells. Lymphokine Res. 5:215.
    • (1986) Lymphokine Res. , vol.5 , pp. 215
    • Koff, W.C.1    Fann, A.V.2
  • 17
    • 0025019251 scopus 로고
    • Molecular mechanisms by which adenoviruses counteract antiviral immune defenses
    • Gooding, L. R., and W. S. M. Wold. 1990. Molecular mechanisms by which adenoviruses counteract antiviral immune defenses. Crit. Rev. Immunoi 10:53.
    • (1990) Crit. Rev. Immunoi , vol.10 , pp. 53
    • Gooding, L.R.1    Wold, W.S.M.2
  • 18
    • 0025727524 scopus 로고
    • Independent transformation activity by adenovirus-5 E1A-conserved regions 1 or 2 mutants
    • Svensson, C., M. Bindesson, E. Nyberg, S. Under, N. Jones, and G. Akusjarvi. 1991. Independent transformation activity by adenovirus-5 E1A-conserved regions 1 or 2 mutants. Virology 182:553.
    • (1991) Virology , vol.182 , pp. 553
    • Svensson, C.1    Bindesson, M.2    Nyberg, E.3    Under, S.4    Jones, N.5    Akusjarvi, G.6
  • 19
    • 0028246161 scopus 로고
    • E1A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators
    • Arany, Z., W. R. Sellers, D. M. Livingston, and R. Eckner. 1994. E1A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators. Cell 77:799.
    • (1994) Cell , vol.77 , pp. 799
    • Arany, Z.1    Sellers, W.R.2    Livingston, D.M.3    Eckner, R.4
  • 20
    • 0025869428 scopus 로고
    • Adenovirus E1A prevents the retinoblastoma gene product from complexing with a cellular transcription factor
    • Bandara, L. R., and N. B. La Thangue. 1991. Adenovirus E1A prevents the retinoblastoma gene product from complexing with a cellular transcription factor. Nature 351:494.
    • (1991) Nature , vol.351 , pp. 494
    • Bandara, L.R.1    La Thangue, N.B.2
  • 21
    • 0029655544 scopus 로고    scopus 로고
    • Induction of susceptibility to TNF by E1A is dependent of binding to either p300 or p105-Rb and induction of DNA synthesis
    • Shisler, J., P. Duerksen-Hughes, T. M. Hermiston, W. S. M. Wold, and L. R. Gooding. 1996. Induction of susceptibility to TNF by E1A is dependent of binding to either p300 or p105-Rb and induction of DNA synthesis. J. Virol. 70:68.
    • (1996) J. Virol. , vol.70 , pp. 68
    • Shisler, J.1    Duerksen-Hughes, P.2    Hermiston, T.M.3    Wold, W.S.M.4    Gooding, L.R.5
  • 22
    • 0026773471 scopus 로고
    • The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by TNF-α
    • White, E., P. Sabbatini, M. Debbas, W. S. M. Wold, D. I. Kusher, and L. R. Gooding. 1992. The 19-kilodalton adenovirus E1B transforming protein inhibits programmed cell death and prevents cytolysis by TNF-α. Mol Cell. Biol. 12:2570.
    • (1992) Mol Cell. Biol. , vol.12 , pp. 2570
    • White, E.1    Sabbatini, P.2    Debbas, M.3    Wold, W.S.M.4    Kusher, D.I.5    Gooding, L.R.6
  • 23
    • 0023881028 scopus 로고
    • A 14,700 MW protein from the E3 region of adenovirus inhibits cytolysis by TNF
    • Gooding, L. R., L. W. Elmore, A. E. Tollefson, H. A. Brady, and W. S. M. Wold. 1988. A 14,700 MW protein from the E3 region of adenovirus inhibits cytolysis by TNF. Cell 53:341.
    • (1988) Cell , vol.53 , pp. 341
    • Gooding, L.R.1    Elmore, L.W.2    Tollefson, A.E.3    Brady, H.A.4    Wold, W.S.M.5
  • 25
    • 0025812952 scopus 로고
    • The 10,4000- And 14,500-dalton proteins encoded by region E3 of adenovirus function together to protect many but not all mouse cell lines against lysis by TNF
    • Gooding, L. R., T. S. Ranheim, A. E. Tollefson, L. Aquino, P. Duerksen-Hughers, T. M. Horton, and W. S. M. Wold. 1991. The 10,4000- and 14,500-dalton proteins encoded by region E3 of adenovirus function together to protect many but not all mouse cell lines against lysis by TNF. J. Virol. 65:4114.
    • (1991) J. Virol. , vol.65 , pp. 4114
    • Gooding, L.R.1    Ranheim, T.S.2    Tollefson, A.E.3    Aquino, L.4    Duerksen-Hughers, P.5    Horton, T.M.6    Wold, W.S.M.7
  • 26
    • 0024340819 scopus 로고
    • Role of TNF-α in El A oncogene-induced susceptibility of neoplastic cells to lysis by NK cells and activated macrophages
    • Cook, J. L., D. L. May, B. A. Wilson, B. Holskin, M. Chen, D. Shalloway, and T. A. Walker. 1989. Role of TNF-α in El A oncogene-induced susceptibility of neoplastic cells to lysis by NK cells and activated macrophages. J. Immunol. 142:4527.
    • (1989) J. Immunol. , vol.142 , pp. 4527
    • Cook, J.L.1    May, D.L.2    Wilson, B.A.3    Holskin, B.4    Chen, M.5    Shalloway, D.6    Walker, T.A.7
  • 27
    • 0025951941 scopus 로고
    • E1A oncogene induction of cytolytic susceptibility eliminates sarcoma cell tumorigenicity
    • Walker, T. A., B. A. Wilson, A. M. Lewis, Jr., and J. L. Cook. 1991. E1A oncogene induction of cytolytic susceptibility eliminates sarcoma cell tumorigenicity. Proc. Natl. Acad. Sci. USA 88:6491.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6491
    • Walker, T.A.1    Wilson, B.A.2    Lewis A.M., Jr.3    Cook, J.L.4
  • 30
    • 0029862747 scopus 로고    scopus 로고
    • Identification of phosphorylation sites of human 85-kDa cytosolic phospholipase A2 expressed in insect cells and present in human monocytes
    • de Carvalho, M. G. S., A. L. McCormack, E. Olson, F. Ghomashchi, M. H. Gelb, J. R. Yates III, and C. C. Leslie. 1996. Identification of phosphorylation sites of human 85-kDa cytosolic phospholipase A2 expressed in insect cells and present in human monocytes. J. Biol. Chem. 271:6987.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6987
    • De Carvalho, M.G.S.1    McCormack, A.L.2    Olson, E.3    Ghomashchi, F.4    Gelb, M.H.5    Yates III, J.R.6    Leslie, C.C.7
  • 31
    • 0025833807 scopus 로고
    • Receptor-mediated activation of arachidonic acid release in mouse peritoneal-macrophage s is linked to extracellular calcium influx
    • Fernandez, B., and J. Basinde. 1991. Receptor-mediated activation of arachidonic acid release in mouse peritoneal-macrophage s is linked to extracellular calcium influx. Biochem. Biophys. Res. Commun. 180:1036.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 1036
    • Fernandez, B.1    Basinde, J.2
  • 39
    • 0018581742 scopus 로고
    • Isolation of adenovirus type 5 host range deletion mutants defective for transformation in rat embryo cells
    • Jones, N., and T. Shenk. 1979. Isolation of adenovirus type 5 host range deletion mutants defective for transformation in rat embryo cells. Cell 17:683.
    • (1979) Cell , vol.17 , pp. 683
    • Jones, N.1    Shenk, T.2
  • 40
    • 0026733701 scopus 로고
    • Map of cis-acting sequences that determine alternative transcription unit of adenovirus
    • Brady, H. A., A. Scaria, and W. S. M. Wold. 1992. Map of cis-acting sequences that determine alternative transcription unit of adenovirus. J. Virol. 66:5914.
    • (1992) J. Virol. , vol.66 , pp. 5914
    • Brady, H.A.1    Scaria, A.2    Wold, W.S.M.3
  • 43
    • 0028930542 scopus 로고
    • 2 by basic fibroblast growth factor via a p42 mitogen-activated protein kinase-dependent phosphorylation pathway in endolhelial cells
    • 2 by basic fibroblast growth factor via a p42 mitogen-activated protein kinase-dependent phosphorylation pathway in endolhelial cells. J. Biol. Chem. 270:2360.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2360
    • Sa, G.1    Murugesan, G.2    Jaye, M.3    Ivashchenko, Y.4    Fox, P.L.5
  • 45
    • 0028935270 scopus 로고
    • Pro-inflammatory cytokines and environmental stress cause p38 MAP kinase activation by dual phosphorylation on tyrosine and threonine
    • Raingeaud, J., S. Gupta, J. Rogers, M. Dickens, J. Han, R. J. Ulevitch, and R. J. Davis. 1995. Pro-inflammatory cytokines and environmental stress cause p38 MAP kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem. 270:7420.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7420
    • Raingeaud, J.1    Gupta, S.2    Rogers, J.3    Dickens, M.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 46
    • 0025220501 scopus 로고
    • 2 with membrane in the macrophage cell line RAW 264.7
    • 2 with membrane in the macrophage cell line RAW 264.7. J. Biol. Chem. 265:5409.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5409
    • Channon, J.Y.1    Leslie, C.C.2
  • 47
    • 0031060481 scopus 로고    scopus 로고
    • Slow increase in intranuclear and cytosolic free calcium concentrations in L929 cells is important in tumour necrosis factor-α-mediated cell death
    • Kong, S. K., K. P. Fung, Y. M. Choy, and C. Y. Lee. 1997. Slow increase in intranuclear and cytosolic free calcium concentrations in L929 cells is important in tumour necrosis factor-α-mediated cell death. Oncology 54:55.
    • (1997) Oncology , vol.54 , pp. 55
    • Kong, S.K.1    Fung, K.P.2    Choy, Y.M.3    Lee, C.Y.4
  • 52
    • 0030794511 scopus 로고    scopus 로고
    • Conditional expression of the mitogen-activated protein kinase (MAPK) phosphatase MKP-1 preferentially inhibits p38 MAPK and stress-activated protein kinase in U937 cells
    • Franklin, C. C., and A. S. Kraft. 1997. Conditional expression of the mitogen-activated protein kinase (MAPK) phosphatase MKP-1 preferentially inhibits p38 MAPK and stress-activated protein kinase in U937 cells. J. Biol. Chem. 272: 16917.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16917
    • Franklin, C.C.1    Kraft, A.S.2
  • 53
    • 0030046479 scopus 로고    scopus 로고
    • Induction of mitogen-activated protein kinase phosphatase 1 by the stress-activated protein kinase signaling pathway but not by extracellular signal-regulated kinase in fibroblasts
    • Bokemeyer, D., A. Sorokin, M. Yan, N. G. Ahn, D. J. Templeton, and M. J. Dunn. 1996. Induction of mitogen-activated protein kinase phosphatase 1 by the stress-activated protein kinase signaling pathway but not by extracellular signal-regulated kinase in fibroblasts. J. Biol. Chem. 271:639.
    • (1996) J. Biol. Chem. , vol.271 , pp. 639
    • Bokemeyer, D.1    Sorokin, A.2    Yan, M.3    Ahn, N.G.4    Templeton, D.J.5    Dunn, M.J.6
  • 54
    • 0027358722 scopus 로고
    • MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo
    • Sun, H., C. H. Charles, L. F. Lau, and N. K. Tonks. 1993. MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 75:487.
    • (1993) Cell , vol.75 , pp. 487
    • Sun, H.1    Charles, C.H.2    Lau, L.F.3    Tonks, N.K.4
  • 55
    • 0030738282 scopus 로고    scopus 로고
    • Inhibition of protein tyrosine phosphatases causes phosphorylation of tyrosine-331 in the p60 TNF receptor and inactivates the receptor-associated kinase
    • Damay, B. G., and B. B. Aggarwal. 1997. Inhibition of protein tyrosine phosphatases causes phosphorylation of tyrosine-331 in the p60 TNF receptor and inactivates the receptor-associated kinase. FEBS Lett. 410:361.
    • (1997) FEBS Lett. , vol.410 , pp. 361
    • Damay, B.G.1    Aggarwal, B.B.2
  • 56
    • 0030832148 scopus 로고    scopus 로고
    • Induction of endothelial cell surface adhesion molecules by TNF is blocked by protein tyrosine phosphatase inhibitors: Role of the nuclear transcription factor NF-κB
    • Dhawan, S., S. Singh, and B. B. Aggarwal. 1997. Induction of endothelial cell surface adhesion molecules by TNF is blocked by protein tyrosine phosphatase inhibitors: role of the nuclear transcription factor NF-κB. Eur. J. Immunol. 27: 2172.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 2172
    • Dhawan, S.1    Singh, S.2    Aggarwal, B.B.3
  • 57
    • 0027383499 scopus 로고
    • Role of protein phosphorylation in TNF-induced apoptosis: Phosphatase inhibitors synergize with TNF to activate DNA fragmentation in normal as well as TNF-resistant U937 variants
    • Wright, S. C., Zheng, H., Zhong, J., Torti, F. M., and J. W. Larrick. 1993. Role of protein phosphorylation in TNF-induced apoptosis: phosphatase inhibitors synergize with TNF to activate DNA fragmentation in normal as well as TNF-resistant U937 variants. J. Cell. Biochem. 53:222.
    • (1993) J. Cell. Biochem. , vol.53 , pp. 222
    • Wright, S.C.1    Zheng, H.2    Zhong, J.3    Torti, F.M.4    Larrick, J.W.5
  • 59
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda, A., J. Rouse, Y. N. Doza, R. Meier, P. Cohen, T. F. Gallagher, P. R. Young, and J. C. Lee. 1995. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett. 364:229.
    • (1995) FEBS Lett. , vol.364 , pp. 229
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 60
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death
    • Liu, Z.-G., H. Hsu, D. V. Goeddel, and M. Karin. 1996. Dissection of TNF receptor 1 effector functions: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death. Cell 87:565.
    • (1996) Cell , vol.87 , pp. 565
    • Liu, Z.-G.1    Hsu, H.2    Goeddel, D.V.3    Karin, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.