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Volumn 7, Issue 10, 2011, Pages

Chlamydia trachomatis co-opts the FGF2 signaling pathway to enhance infection

Author keywords

[No Author keywords available]

Indexed keywords

FIBROBLAST GROWTH FACTOR 2; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEASOME; PROTEOHEPARAN SULFATE; INTERLEUKIN 1BETA CONVERTING ENZYME; PLATELET DERIVED GROWTH FACTOR RECEPTOR; SMALL INTERFERING RNA;

EID: 80055088874     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002285     Document Type: Article
Times cited : (54)

References (73)
  • 2
    • 0025979037 scopus 로고
    • Interaction of chlamydiae and host cells in vitro
    • Moulder JW, (1991) Interaction of chlamydiae and host cells in vitro. Microbiol Rev 55: 143-190.
    • (1991) Microbiol Rev , vol.55 , pp. 143-190
    • Moulder, J.W.1
  • 3
    • 28044453071 scopus 로고    scopus 로고
    • Recent insights into the mechanisms of Chlamydia entry
    • Dautry-Varsat A, Subtil A, Hackstadt T, (2005) Recent insights into the mechanisms of Chlamydia entry. Cell Microbiol 7: 1714-1722.
    • (2005) Cell Microbiol , vol.7 , pp. 1714-1722
    • Dautry-Varsat, A.1    Subtil, A.2    Hackstadt, T.3
  • 4
    • 72749123375 scopus 로고    scopus 로고
    • New insights into Chlamydia intracellular survival mechanisms
    • Cocchiaro JL, Valdivia RH, (2009) New insights into Chlamydia intracellular survival mechanisms. Cell Microbiol 11: 1571-1578.
    • (2009) Cell Microbiol , vol.11 , pp. 1571-1578
    • Cocchiaro, J.L.1    Valdivia, R.H.2
  • 5
    • 42949086499 scopus 로고    scopus 로고
    • RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry
    • Elwell CA, Ceesay A, Kim JH, Kalman D, Engel JN, (2008) RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry. PLoS Pathog 4: e1000021.
    • (2008) PLoS Pathog , vol.4
    • Elwell, C.A.1    Ceesay, A.2    Kim, J.H.3    Kalman, D.4    Engel, J.N.5
  • 6
    • 3042707297 scopus 로고    scopus 로고
    • A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin
    • Clifton DR, Fields KA, Grieshaber SS, Dooley CA, Fischer ER, et al. (2004) A chlamydial type III translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin. Proc Natl Acad Sci U S A 101: 10166-10171.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10166-10171
    • Clifton, D.R.1    Fields, K.A.2    Grieshaber, S.S.3    Dooley, C.A.4    Fischer, E.R.5
  • 7
    • 77957686132 scopus 로고    scopus 로고
    • The conserved Tarp actin binding domain is important for chlamydial invasion
    • Jewett TJ, Miller NJ, Dooley CA, Hackstadt T, (2010) The conserved Tarp actin binding domain is important for chlamydial invasion. PLoS Pathog 6: e1000997.
    • (2010) PLoS Pathog , vol.6
    • Jewett, T.J.1    Miller, N.J.2    Dooley, C.A.3    Hackstadt, T.4
  • 8
    • 0034139491 scopus 로고    scopus 로고
    • Redirection of host vesicle trafficking pathways by intracellular parasites
    • Hackstadt T, (2000) Redirection of host vesicle trafficking pathways by intracellular parasites. Traffic 1: 93-99.
    • (2000) Traffic , vol.1 , pp. 93-99
    • Hackstadt, T.1
  • 9
    • 34547397847 scopus 로고    scopus 로고
    • Mechanisms of host cell exit by the intracellular bacterium Chlamydia
    • Hybiske K, Stephens RS, (2007) Mechanisms of host cell exit by the intracellular bacterium Chlamydia. Proc Natl Acad Sci U S A 104: 11430-11435.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 11430-11435
    • Hybiske, K.1    Stephens, R.S.2
  • 10
    • 0037312521 scopus 로고    scopus 로고
    • Chlamydia trachomatis infection alters host cell transcription in diverse cellular pathways
    • Xia M, Bumgarner RE, Lampe MF, Stamm WE, (2003) Chlamydia trachomatis infection alters host cell transcription in diverse cellular pathways. J Infect Dis 187: 424-434.
    • (2003) J Infect Dis , vol.187 , pp. 424-434
    • Xia, M.1    Bumgarner, R.E.2    Lampe, M.F.3    Stamm, W.E.4
  • 11
    • 18944374182 scopus 로고    scopus 로고
    • Activation of lipid metabolism contributes to interleukin-8 production during Chlamydia trachomatis infection of cervical epithelial cells
    • Fukuda EY, Lad SP, Mikolon DP, Iacobelli-Martinez M, Li E, (2005) Activation of lipid metabolism contributes to interleukin-8 production during Chlamydia trachomatis infection of cervical epithelial cells. Infect Immun 73: 4017-4024.
    • (2005) Infect Immun , vol.73 , pp. 4017-4024
    • Fukuda, E.Y.1    Lad, S.P.2    Mikolon, D.P.3    Iacobelli-Martinez, M.4    Li, E.5
  • 12
    • 35948943102 scopus 로고    scopus 로고
    • Interleukin-1 is the initiator of Fallopian tube destruction during Chlamydia trachomatis infection
    • Hvid M, Baczynska A, Deleuran B, Fedder J, Knudsen HJ, et al. (2007) Interleukin-1 is the initiator of Fallopian tube destruction during Chlamydia trachomatis infection. Cell Microbiol 9: 2795-2803.
    • (2007) Cell Microbiol , vol.9 , pp. 2795-2803
    • Hvid, M.1    Baczynska, A.2    Deleuran, B.3    Fedder, J.4    Knudsen, H.J.5
  • 13
    • 15844391177 scopus 로고    scopus 로고
    • Structural requirements of heparin binding to Chlamydia trachomatis
    • Chen JC, Zhang JP, Stephens RS, (1996) Structural requirements of heparin binding to Chlamydia trachomatis. J Biol Chem 271: 11134-11140.
    • (1996) J Biol Chem , vol.271 , pp. 11134-11140
    • Chen, J.C.1    Zhang, J.P.2    Stephens, R.S.3
  • 14
    • 0028306744 scopus 로고
    • Trachoma and LGV biovars of Chlamydia trachomatis share the same glycosaminoglycan-dependent mechanism for infection of eukaryotic cells
    • Chen JC, Stephens RS, (1994) Trachoma and LGV biovars of Chlamydia trachomatis share the same glycosaminoglycan-dependent mechanism for infection of eukaryotic cells. Mol Microbiol 11: 501-507.
    • (1994) Mol Microbiol , vol.11 , pp. 501-507
    • Chen, J.C.1    Stephens, R.S.2
  • 15
    • 0031017697 scopus 로고    scopus 로고
    • Chlamydia trachomatis glycosaminoglycan-dependent and independent attachment to eukaryotic cells
    • Chen JC, Stephens RS, (1997) Chlamydia trachomatis glycosaminoglycan-dependent and independent attachment to eukaryotic cells. Microb Pathog 22: 23-30.
    • (1997) Microb Pathog , vol.22 , pp. 23-30
    • Chen, J.C.1    Stephens, R.S.2
  • 16
    • 0034947648 scopus 로고    scopus 로고
    • Molecular diversity of heparan sulfate
    • Esko JD, Lindahl U, (2001) Molecular diversity of heparan sulfate. J Clin Invest 108: 169-173.
    • (2001) J Clin Invest , vol.108 , pp. 169-173
    • Esko, J.D.1    Lindahl, U.2
  • 17
    • 34247610845 scopus 로고    scopus 로고
    • Heparan sulphate proteoglycans fine-tune mammalian physiology
    • Bishop JR, Schuksz M, Esko JD, (2007) Heparan sulphate proteoglycans fine-tune mammalian physiology. Nature 446: 1030.
    • (2007) Nature , vol.446 , pp. 1030
    • Bishop, J.R.1    Schuksz, M.2    Esko, J.D.3
  • 18
    • 33947578471 scopus 로고    scopus 로고
    • Basic fibroblast growth factor (FGF-2): the high molecular weight forms come of age
    • Yu PJ, Ferrari G, Galloway AC, Mignatti P, Pintucci G, (2007) Basic fibroblast growth factor (FGF-2): the high molecular weight forms come of age. J Cell Biochem 100: 1100-1108.
    • (2007) J Cell Biochem , vol.100 , pp. 1100-1108
    • Yu, P.J.1    Ferrari, G.2    Galloway, A.C.3    Mignatti, P.4    Pintucci, G.5
  • 19
    • 0011832027 scopus 로고
    • Multiple forms of basic fibroblast growth factor: amino-terminal cleavages by tumor cell- and brain cell-derived acid proteinases
    • Klagsbrun M, Smith S, Sullivan R, Shing Y, Davidson S, et al. (1987) Multiple forms of basic fibroblast growth factor: amino-terminal cleavages by tumor cell- and brain cell-derived acid proteinases. Proc Natl Acad Sci U S A 84: 1839-1843.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 1839-1843
    • Klagsbrun, M.1    Smith, S.2    Sullivan, R.3    Shing, Y.4    Davidson, S.5
  • 20
    • 1342325441 scopus 로고    scopus 로고
    • Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells
    • Schafer T, Zentgraf H, Zehe C, Brugger B, Bernhagen J, et al. (2004) Unconventional secretion of fibroblast growth factor 2 is mediated by direct translocation across the plasma membrane of mammalian cells. J Biol Chem 279: 6244-6251.
    • (2004) J Biol Chem , vol.279 , pp. 6244-6251
    • Schafer, T.1    Zentgraf, H.2    Zehe, C.3    Brugger, B.4    Bernhagen, J.5
  • 21
    • 46349098379 scopus 로고    scopus 로고
    • A direct role for phosphatidylinositol-4,5-bisphosphate in unconventional secretion of fibroblast growth factor 2
    • Temmerman K, Ebert AD, Muller HM, Sinning I, Tews I, et al. (2008) A direct role for phosphatidylinositol-4,5-bisphosphate in unconventional secretion of fibroblast growth factor 2. Traffic 9: 1204-1217.
    • (2008) Traffic , vol.9 , pp. 1204-1217
    • Temmerman, K.1    Ebert, A.D.2    Muller, H.M.3    Sinning, I.4    Tews, I.5
  • 22
    • 0032850597 scopus 로고    scopus 로고
    • FGF-2/fibroblast growth factor receptor/heparin-like glycosaminoglycan interactions: a compensation model for FGF-2 signaling
    • Padera R, Venkataraman G, Berry D, Godavarti R, Sasisekharan R, (1999) FGF-2/fibroblast growth factor receptor/heparin-like glycosaminoglycan interactions: a compensation model for FGF-2 signaling. FASEB J 13: 1677-1687.
    • (1999) FASEB J , vol.13 , pp. 1677-1687
    • Padera, R.1    Venkataraman, G.2    Berry, D.3    Godavarti, R.4    Sasisekharan, R.5
  • 23
    • 0028023801 scopus 로고
    • Heparin increases the affinity of basic fibroblast growth factor for its receptor but is not required for binding
    • Roghan M, Mansukhani A, Dell'Era P, Bellosta P, Basilico C, et al. (1994) Heparin increases the affinity of basic fibroblast growth factor for its receptor but is not required for binding. J Biol Chem 269: 3976-3984.
    • (1994) J Biol Chem , vol.269 , pp. 3976-3984
    • Roghan, M.1    Mansukhani, A.2    Dell'Era, P.3    Bellosta, P.4    Basilico, C.5
  • 24
    • 0028608075 scopus 로고
    • Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation
    • Spivack-Kroizman T, Lemmon MA, Dikic I, Ladbury JE, Pinchasi D, et al. (1994) Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation. Cell 79: 1015-1024.
    • (1994) Cell , vol.79 , pp. 1015-1024
    • Spivack-Kroizman, T.1    Lemmon, M.A.2    Dikic, I.3    Ladbury, J.E.4    Pinchasi, D.5
  • 25
    • 38049064482 scopus 로고    scopus 로고
    • Fibroblast growth factor receptor 1 (FGFR1) tyrosine phosphorylation regulates binding of FGFR substrate 2alpha (FRS2alpha) but not FRS2 to the receptor
    • Zhang Y, McKeehan K, Lin Y, Zhang J, Wang F, (2008) Fibroblast growth factor receptor 1 (FGFR1) tyrosine phosphorylation regulates binding of FGFR substrate 2alpha (FRS2alpha) but not FRS2 to the receptor. Mol Endocrinol 22: 167-175.
    • (2008) Mol Endocrinol , vol.22 , pp. 167-175
    • Zhang, Y.1    McKeehan, K.2    Lin, Y.3    Zhang, J.4    Wang, F.5
  • 26
    • 44449108785 scopus 로고    scopus 로고
    • Regulation of growth factor signaling by FRS2 family docking/scaffold adaptor proteins
    • Gotoh N, (2008) Regulation of growth factor signaling by FRS2 family docking/scaffold adaptor proteins. Cancer Sci 99: 1319-1325.
    • (2008) Cancer Sci , vol.99 , pp. 1319-1325
    • Gotoh, N.1
  • 27
    • 0035142611 scopus 로고    scopus 로고
    • Infectivity of Chlamydia trachomatis serovar LGV but not E is dependent on host cell heparan sulfate
    • Taraktchoglou M, Pacey AA, Turnbull JE, Eley A, (2001) Infectivity of Chlamydia trachomatis serovar LGV but not E is dependent on host cell heparan sulfate. Infect Immun 69: 968-976.
    • (2001) Infect Immun , vol.69 , pp. 968-976
    • Taraktchoglou, M.1    Pacey, A.A.2    Turnbull, J.E.3    Eley, A.4
  • 28
    • 0035377577 scopus 로고    scopus 로고
    • Distinct heparan sulfate glycosaminoglycans are responsible for mediating fibroblast growth factor-2 biological activity through different fibroblast growth factor receptors
    • Berry D, Kwan CP, Shriver Z, Venkataraman G, Sasisekharan R, (2001) Distinct heparan sulfate glycosaminoglycans are responsible for mediating fibroblast growth factor-2 biological activity through different fibroblast growth factor receptors. FASEB J 15: 1422-1424.
    • (2001) FASEB J , vol.15 , pp. 1422-1424
    • Berry, D.1    Kwan, C.P.2    Shriver, Z.3    Venkataraman, G.4    Sasisekharan, R.5
  • 29
    • 77956208869 scopus 로고    scopus 로고
    • Influence of heparin mimetics on the assembly of the FGF - FGFR4 signaling complex
    • Saxena K, Schieborr U, Anderka O, Duchardt-Ferner E, Elshorst B, et al. (2010) Influence of heparin mimetics on the assembly of the FGF- FGFR4 signaling complex. J Biol Chem 285: 26628-26640.
    • (2010) J Biol Chem , vol.285 , pp. 26628-26640
    • Saxena, K.1    Schieborr, U.2    Anderka, O.3    Duchardt-Ferner, E.4    Elshorst, B.5
  • 30
    • 0032985184 scopus 로고    scopus 로고
    • Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase
    • Kan M, Wu X, Wang F, McKeehan WL, (1999) Specificity for fibroblast growth factors determined by heparan sulfate in a binary complex with the receptor kinase. J Biol Chem 274: 15947-15952.
    • (1999) J Biol Chem , vol.274 , pp. 15947-15952
    • Kan, M.1    Wu, X.2    Wang, F.3    McKeehan, W.L.4
  • 31
    • 67650100411 scopus 로고    scopus 로고
    • FRS2 via fibroblast growth factor receptor 1 is required for platelet-derived growth factor receptor beta-mediated regulation of vascular smooth muscle marker gene expression
    • Chen PY, Simons M, Friesel R, (2009) FRS2 via fibroblast growth factor receptor 1 is required for platelet-derived growth factor receptor beta-mediated regulation of vascular smooth muscle marker gene expression. J Biol Chem 284: 15980-15992.
    • (2009) J Biol Chem , vol.284 , pp. 15980-15992
    • Chen, P.Y.1    Simons, M.2    Friesel, R.3
  • 32
    • 0141624402 scopus 로고    scopus 로고
    • Production of basic fibroblast growth factor and interleukin 6 by human smooth muscle cells following infection with Chlamydia pneumoniae
    • Rodel J, Woytas M, Groh A, Schmidt KH, Hartmann M, et al. (2000) Production of basic fibroblast growth factor and interleukin 6 by human smooth muscle cells following infection with Chlamydia pneumoniae. Infect Immun 68: 3635-3641.
    • (2000) Infect Immun , vol.68 , pp. 3635-3641
    • Rodel, J.1    Woytas, M.2    Groh, A.3    Schmidt, K.H.4    Hartmann, M.5
  • 33
    • 3142704258 scopus 로고    scopus 로고
    • Growth factor production in human endothelial cells after Chlamydia pneumoniae infection
    • Prochnau D, Rodel J, Hartmann M, Straube E, Figulla HR, (2004) Growth factor production in human endothelial cells after Chlamydia pneumoniae infection. Int J Med Microbiol 294: 53-57.
    • (2004) Int J Med Microbiol , vol.294 , pp. 53-57
    • Prochnau, D.1    Rodel, J.2    Hartmann, M.3    Straube, E.4    Figulla, H.R.5
  • 34
    • 67649771727 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 autofeedback regulation in pituitary folliculostellate TtT/GF cells
    • Vlotides G, Chen YH, Eigler T, Ren SG, Melmed S, (2009) Fibroblast growth factor-2 autofeedback regulation in pituitary folliculostellate TtT/GF cells. Endocrinology 150: 3252-3258.
    • (2009) Endocrinology , vol.150 , pp. 3252-3258
    • Vlotides, G.1    Chen, Y.H.2    Eigler, T.3    Ren, S.G.4    Melmed, S.5
  • 35
    • 58149499166 scopus 로고    scopus 로고
    • Upregulation of fibroblast growth factor-2 by visfatin that promotes endothelial angiogenesis
    • Bae YH, Bae MK, Kim SR, Lee JH, Wee HJ, et al. (2009) Upregulation of fibroblast growth factor-2 by visfatin that promotes endothelial angiogenesis. Biochem Biophys Res Commun 379: 206-211.
    • (2009) Biochem Biophys Res Commun , vol.379 , pp. 206-211
    • Bae, Y.H.1    Bae, M.K.2    Kim, S.R.3    Lee, J.H.4    Wee, H.J.5
  • 36
    • 1542334775 scopus 로고    scopus 로고
    • Activation of Raf/MEK/ERK/cPLA2 signaling pathway is essential for chlamydial acquisition of host glycerophospholipids
    • Su H, McClarty G, Dong F, Hatch GM, Pan ZK, et al. (2004) Activation of Raf/MEK/ERK/cPLA2 signaling pathway is essential for chlamydial acquisition of host glycerophospholipids. J Biol Chem 279: 9409-9416.
    • (2004) J Biol Chem , vol.279 , pp. 9409-9416
    • Su, H.1    McClarty, G.2    Dong, F.3    Hatch, G.M.4    Pan, Z.K.5
  • 37
    • 0036326980 scopus 로고    scopus 로고
    • Identification of MEK- and phosphoinositide 3-kinase-dependent signalling as essential events during Chlamydia pneumoniae invasion of HEp2 cells
    • Coombes BK, Mahony JB, (2002) Identification of MEK- and phosphoinositide 3-kinase-dependent signalling as essential events during Chlamydia pneumoniae invasion of HEp2 cells. Cell Microbiol 4: 447-460.
    • (2002) Cell Microbiol , vol.4 , pp. 447-460
    • Coombes, B.K.1    Mahony, J.B.2
  • 38
    • 36749049173 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase/mitogen-activated protein kinase pathway induces the inflammatory factor interleukin-8 following Chlamydia trachomatis infection
    • Buchholz KR, Stephens RS, (2007) The extracellular signal-regulated kinase/mitogen-activated protein kinase pathway induces the inflammatory factor interleukin-8 following Chlamydia trachomatis infection. Infect Immun 75: 5924-5929.
    • (2007) Infect Immun , vol.75 , pp. 5924-5929
    • Buchholz, K.R.1    Stephens, R.S.2
  • 39
    • 46449093146 scopus 로고    scopus 로고
    • The cytosolic pattern recognition receptor NOD1 induces inflammatory interleukin-8 during Chlamydia trachomatis infection
    • Buchholz KR, Stephens RS, (2008) The cytosolic pattern recognition receptor NOD1 induces inflammatory interleukin-8 during Chlamydia trachomatis infection. Infect Immun 76: 3150-3155.
    • (2008) Infect Immun , vol.76 , pp. 3150-3155
    • Buchholz, K.R.1    Stephens, R.S.2
  • 40
    • 77954374184 scopus 로고    scopus 로고
    • cPLA2 regulates the expression of type I interferons and intracellular immunity to Chlamydia trachomatis
    • Vignola MJ, Kashatus DF, Taylor GA, Counter CM, Valdivia RH, (2010) cPLA2 regulates the expression of type I interferons and intracellular immunity to Chlamydia trachomatis. J Biol Chem 285: 21625-21635.
    • (2010) J Biol Chem , vol.285 , pp. 21625-21635
    • Vignola, M.J.1    Kashatus, D.F.2    Taylor, G.A.3    Counter, C.M.4    Valdivia, R.H.5
  • 41
    • 77953854520 scopus 로고    scopus 로고
    • A loss-of-function screen reveals Ras- and Raf-independent MEK-ERK signaling during Chlamydia trachomatis infection
    • Gurumurthy RK, Maurer AP, Machuy N, Hess S, Pleissner KP, et al. (2010) A loss-of-function screen reveals Ras- and Raf-independent MEK-ERK signaling during Chlamydia trachomatis infection. Sci Signal 3: ra21.
    • (2010) Sci Signal , vol.3
    • Gurumurthy, R.K.1    Maurer, A.P.2    Machuy, N.3    Hess, S.4    Pleissner, K.P.5
  • 42
    • 77954746346 scopus 로고    scopus 로고
    • Tarp regulates early Chlamydia-induced host cell survival through interactions with the human adaptor protein SHC1
    • Mehlitz A, Banhart S, Maurer AP, Kaushansky A, Gordus AG, et al. (2010) Tarp regulates early Chlamydia-induced host cell survival through interactions with the human adaptor protein SHC1. J Cell Biol 190: 143-157.
    • (2010) J Cell Biol , vol.190 , pp. 143-157
    • Mehlitz, A.1    Banhart, S.2    Maurer, A.P.3    Kaushansky, A.4    Gordus, A.G.5
  • 43
    • 52449108643 scopus 로고    scopus 로고
    • FGF2 translationally induced by hypoxia is involved in negative and positive feedback loops with HIF-1alpha
    • Conte C, Riant E, Toutain C, Pujol F, Arnal JF, et al. (2008) FGF2 translationally induced by hypoxia is involved in negative and positive feedback loops with HIF-1alpha. PLoS One 3: e3078.
    • (2008) PLoS One , vol.3
    • Conte, C.1    Riant, E.2    Toutain, C.3    Pujol, F.4    Arnal, J.F.5
  • 44
    • 0035797499 scopus 로고    scopus 로고
    • p53 directs conformational change and translation initiation blockade of human fibroblast growth factor 2 mRNA
    • Galy B, Creancier L, Prado-Lourenco L, Prats AC, Prats H, (2001) p53 directs conformational change and translation initiation blockade of human fibroblast growth factor 2 mRNA. Oncogene 20: 4613-4620.
    • (2001) Oncogene , vol.20 , pp. 4613-4620
    • Galy, B.1    Creancier, L.2    Prado-Lourenco, L.3    Prats, A.C.4    Prats, H.5
  • 45
    • 0035967104 scopus 로고    scopus 로고
    • Tumour suppressor p53 inhibits human fibroblast growth factor 2 expression by a post-transcriptional mechanism
    • Galy B, Creancier L, Zanibellato C, Prats AC, Prats H, (2001) Tumour suppressor p53 inhibits human fibroblast growth factor 2 expression by a post-transcriptional mechanism. Oncogene 20: 1669-1677.
    • (2001) Oncogene , vol.20 , pp. 1669-1677
    • Galy, B.1    Creancier, L.2    Zanibellato, C.3    Prats, A.C.4    Prats, H.5
  • 46
    • 77957341471 scopus 로고    scopus 로고
    • ERK activation of p21 activated kinase-1 (Pak1) is critical for medulloblastoma cell migration
    • Yuan L, Santi M, Rushing EJ, Cornelison R, MacDonald TJ, (2010) ERK activation of p21 activated kinase-1 (Pak1) is critical for medulloblastoma cell migration. Clin Exp Metastasis 27: 481-491.
    • (2010) Clin Exp Metastasis , vol.27 , pp. 481-491
    • Yuan, L.1    Santi, M.2    Rushing, E.J.3    Cornelison, R.4    MacDonald, T.J.5
  • 47
    • 78751569887 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases ERK 1/2- and p38-GATA4 pathways mediate the Ang II-induced activation of FGF2 gene in neonatal rat cardiomyocytes
    • Tang W, Wei Y, Le K, Li Z, Bao Y, et al. (2011) Mitogen-activated protein kinases ERK 1/2- and p38-GATA4 pathways mediate the Ang II-induced activation of FGF2 gene in neonatal rat cardiomyocytes. Biochem Pharmacol 81: 518-525.
    • (2011) Biochem Pharmacol , vol.81 , pp. 518-525
    • Tang, W.1    Wei, Y.2    Le, K.3    Li, Z.4    Bao, Y.5
  • 48
    • 62649084181 scopus 로고    scopus 로고
    • Activation of the FGF2/FGFR1 autocrine loop for cell proliferation and survival in uveal melanoma cells
    • Lefevre G, Babchia N, Calipel A, Mouriaux F, Faussat AM, et al. (2009) Activation of the FGF2/FGFR1 autocrine loop for cell proliferation and survival in uveal melanoma cells. Invest Ophthalmol Vis Sci 50: 1047-1057.
    • (2009) Invest Ophthalmol Vis Sci , vol.50 , pp. 1047-1057
    • Lefevre, G.1    Babchia, N.2    Calipel, A.3    Mouriaux, F.4    Faussat, A.M.5
  • 49
    • 0035896736 scopus 로고    scopus 로고
    • Identification of a chlamydial protease-like activity factor responsible for the degradation of host transcription factors
    • Zhong G, Fan P, Ji H, Dong F, Huang Y, (2001) Identification of a chlamydial protease-like activity factor responsible for the degradation of host transcription factors. J Exp Med 193: 935-942.
    • (2001) J Exp Med , vol.193 , pp. 935-942
    • Zhong, G.1    Fan, P.2    Ji, H.3    Dong, F.4    Huang, Y.5
  • 50
    • 48649108402 scopus 로고    scopus 로고
    • Actin and intermediate filaments stabilize the Chlamydia trachomatis vacuole by forming dynamic structural scaffolds
    • Kumar Y, Valdivia RH, (2008) Actin and intermediate filaments stabilize the Chlamydia trachomatis vacuole by forming dynamic structural scaffolds. Cell Host Microbe 4: 159-169.
    • (2008) Cell Host Microbe , vol.4 , pp. 159-169
    • Kumar, Y.1    Valdivia, R.H.2
  • 51
    • 0028939001 scopus 로고
    • Quantitative export of FGF-2 occurs through an alternative, energy-dependent, non-ER/Golgi pathway
    • Florkiewicz RZ, Majack RA, Buechler RD, Florkiewicz E, (1995) Quantitative export of FGF-2 occurs through an alternative, energy-dependent, non-ER/Golgi pathway. J Cell Physiol 162: 388-399.
    • (1995) J Cell Physiol , vol.162 , pp. 388-399
    • Florkiewicz, R.Z.1    Majack, R.A.2    Buechler, R.D.3    Florkiewicz, E.4
  • 52
    • 0026548976 scopus 로고
    • Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum-Golgi complex
    • Mignatti P, Morimoto T, Rifkin DB, (1992) Basic fibroblast growth factor, a protein devoid of secretory signal sequence, is released by cells via a pathway independent of the endoplasmic reticulum-Golgi complex. J Cell Physiol 151: 81-93.
    • (1992) J Cell Physiol , vol.151 , pp. 81-93
    • Mignatti, P.1    Morimoto, T.2    Rifkin, D.B.3
  • 53
    • 39749084641 scopus 로고    scopus 로고
    • Active caspase-1 is a regulator of unconventional protein secretion
    • Keller M, Ruegg A, Werner S, Beer HD, (2008) Active caspase-1 is a regulator of unconventional protein secretion. Cell 132: 818-831.
    • (2008) Cell , vol.132 , pp. 818-831
    • Keller, M.1    Ruegg, A.2    Werner, S.3    Beer, H.D.4
  • 54
    • 0034610312 scopus 로고    scopus 로고
    • Participation of Na,K-ATPase in FGF-2 secretion: rescue of ouabain-inhibitable FGF-2 secretion by ouabain-resistant Na,K-ATPase alpha subunits
    • Dahl JP, Binda A, Canfield VA, Levenson R, (2000) Participation of Na,K-ATPase in FGF-2 secretion: rescue of ouabain-inhibitable FGF-2 secretion by ouabain-resistant Na,K-ATPase alpha subunits. Biochemistry 39: 14877-14883.
    • (2000) Biochemistry , vol.39 , pp. 14877-14883
    • Dahl, J.P.1    Binda, A.2    Canfield, V.A.3    Levenson, R.4
  • 55
    • 9144247272 scopus 로고    scopus 로고
    • Shedding of membrane vesicles mediates fibroblast growth factor-2 release from cells
    • Taverna S, Ghersi G, Ginestra A, Rigogliuso S, Pecorella S, et al. (2003) Shedding of membrane vesicles mediates fibroblast growth factor-2 release from cells. J Biol Chem 278: 51911-51919.
    • (2003) J Biol Chem , vol.278 , pp. 51911-51919
    • Taverna, S.1    Ghersi, G.2    Ginestra, A.3    Rigogliuso, S.4    Pecorella, S.5
  • 56
    • 0034254559 scopus 로고    scopus 로고
    • Chlamydia trachomatis infection of epithelial cells induces the activation of caspase-1 and release of mature IL-18
    • Lu H, Shen C, Brunham RC, (2000) Chlamydia trachomatis infection of epithelial cells induces the activation of caspase-1 and release of mature IL-18. J Immunol 165: 1463-1469.
    • (2000) J Immunol , vol.165 , pp. 1463-1469
    • Lu, H.1    Shen, C.2    Brunham, R.C.3
  • 57
    • 0030978083 scopus 로고    scopus 로고
    • Differences in the association of Chlamydia trachomatis serovar E and serovar L2 with epithelial cells in vitro may reflect biological differences in vivo
    • Davis CH, Wyrick PB, (1997) Differences in the association of Chlamydia trachomatis serovar E and serovar L2 with epithelial cells in vitro may reflect biological differences in vivo. Infect Immun 65: 2914-2924.
    • (1997) Infect Immun , vol.65 , pp. 2914-2924
    • Davis, C.H.1    Wyrick, P.B.2
  • 58
    • 1242306650 scopus 로고    scopus 로고
    • Chlorate: a reversible inhibitor of proteoglycan sulphation in Chlamydia trachomatis-infected cells
    • Fadel S, Eley A, (2004) Chlorate: a reversible inhibitor of proteoglycan sulphation in Chlamydia trachomatis-infected cells. J Med Microbiol 53: 93-95.
    • (2004) J Med Microbiol , vol.53 , pp. 93-95
    • Fadel, S.1    Eley, A.2
  • 59
    • 37349053423 scopus 로고    scopus 로고
    • The Chlamydia outer membrane protein OmcB is required for adhesion and exhibits biovar-specific differences in glycosaminoglycan binding
    • Moelleken K, Hegemann JH, (2008) The Chlamydia outer membrane protein OmcB is required for adhesion and exhibits biovar-specific differences in glycosaminoglycan binding. Mol Microbiol 67: 403-419.
    • (2008) Mol Microbiol , vol.67 , pp. 403-419
    • Moelleken, K.1    Hegemann, J.H.2
  • 61
    • 0033575235 scopus 로고    scopus 로고
    • Shc regulates epidermal growth factor-induced activation of the JNK signaling pathway
    • Hashimoto A, Kurosaki M, Gotoh N, Shibuya M, Kurosaki T, (1999) Shc regulates epidermal growth factor-induced activation of the JNK signaling pathway. J Biol Chem 274: 20139-20143.
    • (1999) J Biol Chem , vol.274 , pp. 20139-20143
    • Hashimoto, A.1    Kurosaki, M.2    Gotoh, N.3    Shibuya, M.4    Kurosaki, T.5
  • 62
    • 0028817834 scopus 로고
    • Shc and a novel 89-kDa component couple to the Grb2-Sos complex in fibroblast growth factor-2-stimulated cells
    • Klint P, Kanda S, Claesson-Welsh L, (1995) Shc and a novel 89-kDa component couple to the Grb2-Sos complex in fibroblast growth factor-2-stimulated cells. J Biol Chem 270: 23337-23344.
    • (1995) J Biol Chem , vol.270 , pp. 23337-23344
    • Klint, P.1    Kanda, S.2    Claesson-Welsh, L.3
  • 63
    • 33644550021 scopus 로고    scopus 로고
    • Structural systems biology: modelling protein interactions
    • Aloy P, Russell RB, (2006) Structural systems biology: modelling protein interactions. Nat Rev Mol Cell Biol 7: 188-197.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 188-197
    • Aloy, P.1    Russell, R.B.2
  • 64
    • 42249099989 scopus 로고    scopus 로고
    • Thrombin cleaves the high molecular weight forms of basic fibroblast growth factor (FGF-2): a novel mechanism for the control of FGF-2 and thrombin activity
    • Yu PJ, Ferrari G, Pirelli L, Galloway AC, Mignatti P, et al. (2008) Thrombin cleaves the high molecular weight forms of basic fibroblast growth factor (FGF-2): a novel mechanism for the control of FGF-2 and thrombin activity. Oncogene 27: 2594-2601.
    • (2008) Oncogene , vol.27 , pp. 2594-2601
    • Yu, P.J.1    Ferrari, G.2    Pirelli, L.3    Galloway, A.C.4    Mignatti, P.5
  • 65
    • 79551512812 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae infection induces altered amphiregulin processing and release
    • Lofmark S, de Klerk N, Aro H, (2011) Neisseria gonorrhoeae infection induces altered amphiregulin processing and release. PLoS One 6: e16369.
    • (2011) PLoS One , vol.6
    • Lofmark, S.1    de Klerk, N.2    Aro, H.3
  • 66
    • 33747879124 scopus 로고    scopus 로고
    • Helicobacter pylori can induce heparin-binding epidermal growth factor expression via gastrin and its receptor
    • Dickson JH, Grabowska A, El-Zaatari M, Atherton J, Watson SA, (2006) Helicobacter pylori can induce heparin-binding epidermal growth factor expression via gastrin and its receptor. Cancer Res 66: 7524-7531.
    • (2006) Cancer Res , vol.66 , pp. 7524-7531
    • Dickson, J.H.1    Grabowska, A.2    El-Zaatari, M.3    Atherton, J.4    Watson, S.A.5
  • 67
    • 0036605508 scopus 로고    scopus 로고
    • Chlamydia pneumoniae infection of endothelial cells induces transcriptional activation of platelet-derived growth factor-B: a potential link to intimal thickening in a rabbit model of atherosclerosis
    • Coombes BK, Chiu B, Fong IW, Mahony JB, (2002) Chlamydia pneumoniae infection of endothelial cells induces transcriptional activation of platelet-derived growth factor-B: a potential link to intimal thickening in a rabbit model of atherosclerosis. J Infect Dis 185: 1621-1630.
    • (2002) J Infect Dis , vol.185 , pp. 1621-1630
    • Coombes, B.K.1    Chiu, B.2    Fong, I.W.3    Mahony, J.B.4
  • 68
    • 33644660157 scopus 로고    scopus 로고
    • Basic fibroblast growth factor (bFGF, FGF-2) potentiates leukocyte recruitment to inflammation by enhancing endothelial adhesion molecule expression
    • Zittermann SI, Issekutz AC, (2006) Basic fibroblast growth factor (bFGF, FGF-2) potentiates leukocyte recruitment to inflammation by enhancing endothelial adhesion molecule expression. Am J Pathol 168: 835-846.
    • (2006) Am J Pathol , vol.168 , pp. 835-846
    • Zittermann, S.I.1    Issekutz, A.C.2
  • 69
    • 33646362773 scopus 로고    scopus 로고
    • Functional diversity of FGF-2 isoforms by intracellular sorting
    • Sorensen V, Nilsen T, Wiedlocha A, (2006) Functional diversity of FGF-2 isoforms by intracellular sorting. Bioessays 28: 504-514.
    • (2006) Bioessays , vol.28 , pp. 504-514
    • Sorensen, V.1    Nilsen, T.2    Wiedlocha, A.3
  • 70
    • 33746306130 scopus 로고    scopus 로고
    • FGF-2 protects small cell lung cancer cells from apoptosis through a complex involving PKCepsilon, B-Raf and S6K2
    • Pardo OE, Wellbrock C, Khanzada UK, Aubert M, Arozarena I, et al. (2006) FGF-2 protects small cell lung cancer cells from apoptosis through a complex involving PKCepsilon, B-Raf and S6K2. EMBO J 25: 3078-3088.
    • (2006) EMBO J , vol.25 , pp. 3078-3088
    • Pardo, O.E.1    Wellbrock, C.2    Khanzada, U.K.3    Aubert, M.4    Arozarena, I.5
  • 71
    • 0031029325 scopus 로고    scopus 로고
    • Characterization of the Chlamydia trachomatis vacuole and its interaction with the host endocytic pathway in HeLa cells
    • van Ooij C, Apodaca G, Engel J, (1997) Characterization of the Chlamydia trachomatis vacuole and its interaction with the host endocytic pathway in HeLa cells. Infect Immun 65: 758-766.
    • (1997) Infect Immun , vol.65 , pp. 758-766
    • van Ooij, C.1    Apodaca, G.2    Engel, J.3
  • 72
    • 0019514724 scopus 로고
    • Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis
    • Caldwell HD, Kromhout J, Schachter J, (1981) Purification and partial characterization of the major outer membrane protein of Chlamydia trachomatis. Infect Immun 31: 1161-1176.
    • (1981) Infect Immun , vol.31 , pp. 1161-1176
    • Caldwell, H.D.1    Kromhout, J.2    Schachter, J.3
  • 73
    • 0033562350 scopus 로고    scopus 로고
    • Development and validation of real-time quantitative reverse transcriptase-polymerase chain reaction for monitoring gene expression in cardiac myocytes in vitro
    • Winer J, Jung CK, Shackel I, Williams PM, (1999) Development and validation of real-time quantitative reverse transcriptase-polymerase chain reaction for monitoring gene expression in cardiac myocytes in vitro. Anal Biochem 270: 41-49.
    • (1999) Anal Biochem , vol.270 , pp. 41-49
    • Winer, J.1    Jung, C.K.2    Shackel, I.3    Williams, P.M.4


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