메뉴 건너뛰기




Volumn 14, Issue 11, 2013, Pages 22678-22696

Membrane signaling induced by high doses of ionizing radiation in the endothelial compartment. Relevance in radiation toxicity

Author keywords

Acid sphingomyelinase; Ceramide; Endothelium; Plasma membrane; Radiation toxicity; Radiotherapy

Indexed keywords

CASPASE 7; CD40 ANTIGEN; CERAMIDE; DYSFERLIN; FAS ANTIGEN; GLUTATHIONE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SNARE PROTEIN; SPHINGOMYELIN PHOSPHODIESTERASE; SPHINGOSINE 1 PHOSPHATE; SYNTAXIN 4; TUMOR NECROSIS FACTOR ALPHA;

EID: 84887907614     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms141122678     Document Type: Review
Times cited : (58)

References (103)
  • 1
    • 0141653957 scopus 로고    scopus 로고
    • Effects of radiation on normal tissue: Consequences and mechanisms
    • Stone, H. B.; Coleman, C. N.; Anscher, M. S.; McBride, W. H. Effects of radiation on normal tissue: Consequences and mechanisms. Lancet Oncol. 2003, 4, 529-536.
    • (2003) Lancet Oncol , vol.4 , pp. 529-536
    • Stone, H.B.1    Coleman, C.N.2    Anscher, M.S.3    McBride, W.H.4
  • 2
    • 77951540327 scopus 로고    scopus 로고
    • Recent advances in radiotherapy
    • Bhide, S. A.; Nutting, C. M. Recent advances in radiotherapy. BMC Med. 2010, 8, 25.
    • (2010) BMC Med , vol.8 , pp. 25
    • Bhide, S.A.1    Nutting, C.M.2
  • 3
    • 84864409104 scopus 로고    scopus 로고
    • Stereotactic body radiation therapy for abdominal oligometastases: A biological and clinical review
    • doi: 10. 1186/1748-717X-7-126
    • Almaghrabi, M. Y.; Supiot, S.; Paris, F.; Mahe, M. A.; Rio, E. Stereotactic body radiation therapy for abdominal oligometastases: A biological and clinical review. Radiat. Oncol. 2012, 7, doi: 10. 1186/1748-717X-7-126.
    • (2012) Radiat. Oncol , vol.7
    • Almaghrabi, M.Y.1    Supiot, S.2    Paris, F.3    Mahe, M.A.4    Rio, E.5
  • 5
    • 57649244044 scopus 로고    scopus 로고
    • Normal tissue toxicity after small field hypofractionated stereotactic body radiation
    • Milano, M. T.; Constine, L. S.; Okunieff, P. Normal tissue toxicity after small field hypofractionated stereotactic body radiation. Radiat. Oncol. 2008, 3, 36.
    • (2008) Radiat. Oncol , vol.3 , pp. 36
    • Milano, M.T.1    Constine, L.S.2    Okunieff, P.3
  • 6
    • 43049167071 scopus 로고    scopus 로고
    • High-dose single-fraction radiotherapy: Exploiting a new biology?
    • Brown, J. M.; Koong, A. C. High-dose single-fraction radiotherapy: Exploiting a new biology? Int. J. Radiat. Oncol. Biol. Phys. 2008, 71, 324-325.
    • (2008) Int. J. Radiat. Oncol. Biol. Phys , vol.71 , pp. 324-325
    • Brown, J.M.1    Koong, A.C.2
  • 7
    • 0342545909 scopus 로고    scopus 로고
    • Radiation-induced apoptosis of endothelial cells in the murine central nervous system: Protection by fibroblast growth factor and sphingomyelinase deficiency
    • Pena, L. A.; Fuks, Z.; Kolesnick, R. N. Radiation-induced apoptosis of endothelial cells in the murine central nervous system: Protection by fibroblast growth factor and sphingomyelinase deficiency. Cancer Res. 2000, 60, 321-327.
    • (2000) Cancer Res , vol.60 , pp. 321-327
    • Pena, L.A.1    Fuks, Z.2    Kolesnick, R.N.3
  • 9
    • 33947536682 scopus 로고    scopus 로고
    • Responses of normal cells to ionizing radiation
    • Rodemann, H. P.; Blaese, M. A. Responses of normal cells to ionizing radiation. Semin. Radiat. Oncol. 2007, 17, 81-88.
    • (2007) Semin. Radiat. Oncol , vol.17 , pp. 81-88
    • Rodemann, H.P.1    Blaese, M.A.2
  • 10
    • 33645013491 scopus 로고    scopus 로고
    • A unifying system: Does the vascular endothelium have a role to play in multi-organ failure following radiation exposure?
    • Gaugler, M. H. A unifying system: Does the vascular endothelium have a role to play in multi-organ failure following radiation exposure? BJR Suppl. 2005, 27, 100-105.
    • (2005) BJR Suppl , vol.27 , pp. 100-105
    • Gaugler, M.H.1
  • 12
    • 0034877938 scopus 로고    scopus 로고
    • Induction of a senescence-like phenotype in bovine aortic endothelial cells by ionizing radiation
    • Oh, C. W.; Bump, E. A.; Kim, J. S.; Janigro, D.; Mayberg, M. R. Induction of a senescence-like phenotype in bovine aortic endothelial cells by ionizing radiation. Radiat. Res. 2001, 156, 232-240.
    • (2001) Radiat. Res , vol.156 , pp. 232-240
    • Oh, C.W.1    Bump, E.A.2    Kim, J.S.3    Janigro, D.4    Mayberg, M.R.5
  • 13
    • 84857448727 scopus 로고    scopus 로고
    • Radiobiology dedicated to endothelium
    • Supiot, S.; Paris, F. Radiobiology dedicated to endothelium. Cancer Radiother. 2012, 16, 11-15.
    • (2012) Cancer Radiother , vol.16 , pp. 11-15
    • Supiot, S.1    Paris, F.2
  • 15
    • 23644445797 scopus 로고    scopus 로고
    • Engaging the vascular component of the tumor response
    • Fuks, Z.; Kolesnick, R. Engaging the vascular component of the tumor response. Cancer Cell 2005, 8, 89-91.
    • (2005) Cancer Cell , vol.8 , pp. 89-91
    • Fuks, Z.1    Kolesnick, R.2
  • 19
    • 77951889353 scopus 로고    scopus 로고
    • Sphingomyelin metabolism at the plasma membrane: Implications for bioactive sphingolipids
    • Milhas, D.; Clarke, C. J.; Hannun, Y. A. Sphingomyelin metabolism at the plasma membrane: implications for bioactive sphingolipids. FEBS Lett. 2010, 584, 1887-1894.
    • (2010) FEBS Lett , vol.584 , pp. 1887-1894
    • Milhas, D.1    Clarke, C.J.2    Hannun, Y.A.3
  • 20
    • 0032579258 scopus 로고    scopus 로고
    • Secretory sphingomyelinase, a product of the acid sphingomyelinase gene, can hydrolyze atherogenic lipoproteins at neutral pH. Implications for atherosclerotic lesion development
    • Schissel, S. L.; Jiang, X.; Tweedie-Hardman, J.; Jeong, T.; Camejo, E. H.; Najib, J.; Rapp, J. H.; Williams, K. J.; Tabas, I. Secretory sphingomyelinase, a product of the acid sphingomyelinase gene, can hydrolyze atherogenic lipoproteins at neutral pH. Implications for atherosclerotic lesion development. J. Biol. Chem. 1998, 273, 2738-2746.
    • (1998) J. Biol. Chem , vol.273 , pp. 2738-2746
    • Schissel, S.L.1    Jiang, X.2    Tweedie-Hardman, J.3    Jeong, T.4    Camejo, E.H.5    Najib, J.6    Rapp, J.H.7    Williams, K.J.8    Tabas, I.9
  • 21
    • 84859726313 scopus 로고    scopus 로고
    • Requirement of translocated lysosomal V1 H(+)-ATPase for activation of membrane acid sphingomyelinase and raft clustering in coronary endothelial cells
    • Xu, M.; Xia, M.; Li, X. X.; Han, W. Q.; Boini, K. M.; Zhang, F.; Zhang, Y.; Ritter, J. K.; Li, P. L. Requirement of translocated lysosomal V1 H(+)-ATPase for activation of membrane acid sphingomyelinase and raft clustering in coronary endothelial cells. Mol. Biol. Cell 2012, 23, 1546-1557.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 1546-1557
    • Xu, M.1    Xia, M.2    Li, X.X.3    Han, W.Q.4    Boini, K.M.5    Zhang, F.6    Zhang, Y.7    Ritter, J.K.8    Li, P.L.9
  • 22
    • 21444434296 scopus 로고    scopus 로고
    • UV-C light induces raft-associated acid sphingomyelinase and JNK activation and translocation independently on a nuclear signal
    • Charruyer, A.; Grazide, S.; Bezombes, C.; Muller, S.; Laurent, G.; Jaffrezou, J. P. UV-C light induces raft-associated acid sphingomyelinase and JNK activation and translocation independently on a nuclear signal. J. Biol. Chem. 2005, 280, 19196-19204.
    • (2005) J. Biol. Chem , vol.280 , pp. 19196-19204
    • Charruyer, A.1    Grazide, S.2    Bezombes, C.3    Muller, S.4    Laurent, G.5    Jaffrezou, J.P.6
  • 23
    • 33748664357 scopus 로고    scopus 로고
    • TRAIL activates acid sphingomyelinase via a redox mechanism and releases ceramide to trigger apoptosis
    • Dumitru, C. A.; Gulbins, E. TRAIL activates acid sphingomyelinase via a redox mechanism and releases ceramide to trigger apoptosis. Oncogene 2006, 25, 5612-5625.
    • (2006) Oncogene , vol.25 , pp. 5612-5625
    • Dumitru, C.A.1    Gulbins, E.2
  • 24
    • 0042335762 scopus 로고    scopus 로고
    • Ceramide-mediated clustering is required for CD95-DISC formation
    • Grassme, H.; Cremesti, A.; Kolesnick, R.; Gulbins, E. Ceramide-mediated clustering is required for CD95-DISC formation. Oncogene 2003, 22, 5457-5470.
    • (2003) Oncogene , vol.22 , pp. 5457-5470
    • Grassme, H.1    Cremesti, A.2    Kolesnick, R.3    Gulbins, E.4
  • 27
    • 84861364532 scopus 로고    scopus 로고
    • Lysosome fusion to the cell membrane is mediated by the dysferlin C2A domain in coronary arterial endothelial cells
    • Han, W. Q.; Xia, M.; Xu, M.; Boini, K. M.; Ritter, J. K.; Li, N. J.; Li, P. L. Lysosome fusion to the cell membrane is mediated by the dysferlin C2A domain in coronary arterial endothelial cells. J. Cell Sci. 2012, 125, 1225-1234.
    • (2012) J. Cell Sci , vol.125 , pp. 1225-1234
    • Han, W.Q.1    Xia, M.2    Xu, M.3    Boini, K.M.4    Ritter, J.K.5    Li, N.J.6    Li, P.L.7
  • 29
    • 38049098527 scopus 로고    scopus 로고
    • A novel role for protein kinase Cdelta-mediated phosphorylation of acid sphingomyelinase in UV light-induced mitochondrial injury
    • Zeidan, Y. H.; Wu, B. X.; Jenkins, R. W.; Obeid, L. M.; Hannun, Y. A. A novel role for protein kinase Cdelta-mediated phosphorylation of acid sphingomyelinase in UV light-induced mitochondrial injury. FASEB J. 2008, 22, 183-193.
    • (2008) FASEB J , vol.22 , pp. 183-193
    • Zeidan, Y.H.1    Wu, B.X.2    Jenkins, R.W.3    Obeid, L.M.4    Hannun, Y.A.5
  • 32
    • 34250799092 scopus 로고    scopus 로고
    • Reactive nitrogen and oxygen species activate different sphingomyelinases to induce apoptosis in airway epithelial cells
    • Castillo, S. S.; Levy, M.; Thaikoottathil, J. V.; Goldkorn, T. Reactive nitrogen and oxygen species activate different sphingomyelinases to induce apoptosis in airway epithelial cells. Exp. Cell Res. 2007, 313, 2680-2686.
    • (2007) Exp. Cell Res , vol.313 , pp. 2680-2686
    • Castillo, S.S.1    Levy, M.2    Thaikoottathil, J.V.3    Goldkorn, T.4
  • 33
    • 34250315352 scopus 로고    scopus 로고
    • Acid sphingomyelinase and its redox amplification in formation of lipid raft redox signaling platforms in endothelial cells
    • Zhang, A. Y.; Yi, F.; Jin, S.; Xia, M.; Chen, Q. Z.; Gulbins, E.; Li, P. L. Acid sphingomyelinase and its redox amplification in formation of lipid raft redox signaling platforms in endothelial cells. Antioxid. Redox Signal. 2007, 9, 817-828.
    • (2007) Antioxid. Redox Signal , vol.9 , pp. 817-828
    • Zhang, A.Y.1    Yi, F.2    Jin, S.3    Xia, M.4    Chen, Q.Z.5    Gulbins, E.6    Li, P.L.7
  • 34
    • 84867483822 scopus 로고    scopus 로고
    • Ionizing radiation-induced metabolic oxidative stress and prolonged cell injury
    • Azzam, E. I.; Jay-Gerin, J. P.; Pain, D. Ionizing radiation-induced metabolic oxidative stress and prolonged cell injury. Cancer Lett. 2012, 327, 48-60.
    • (2012) Cancer Lett , vol.327 , pp. 48-60
    • Azzam, E.I.1    Jay-Gerin, J.P.2    Pain, D.3
  • 36
    • 0033884050 scopus 로고    scopus 로고
    • Compartmentalization of ceramide signaling: Physical foundations and biological effects
    • Kolesnick, R. N.; Goni, F. M.; Alonso, A. Compartmentalization of ceramide signaling: Physical foundations and biological effects. J. Cell Physiol. 2000, 184, 285-300.
    • (2000) J. Cell Physiol , vol.184 , pp. 285-300
    • Kolesnick, R.N.1    Goni, F.M.2    Alonso, A.3
  • 37
    • 0032535156 scopus 로고    scopus 로고
    • Sphingomyelinase induces lipid microdomain formation in a fluid phosphatidylcholine/sphingomyelin membrane
    • Holopainen, J. M.; Subramanian, M.; Kinnunen, P. K. Sphingomyelinase induces lipid microdomain formation in a fluid phosphatidylcholine/sphingomyelin membrane. Biochemistry 1998, 37, 17562-17570.
    • (1998) Biochemistry , vol.37 , pp. 17562-17570
    • Holopainen, J.M.1    Subramanian, M.2    Kinnunen, P.K.3
  • 38
    • 0037120891 scopus 로고    scopus 로고
    • Observation of topical catalysis by sphingomyelinase coupled to microspheres
    • Nurminen, T. A.; Holopainen, J. M.; Zhao, H.; Kinnunen, P. K. Observation of topical catalysis by sphingomyelinase coupled to microspheres. J. Am. Chem. Soc. 2002, 124, 12129-12134.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 12129-12134
    • Nurminen, T.A.1    Holopainen, J.M.2    Zhao, H.3    Kinnunen, P.K.4
  • 39
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K.; Ikonen, E. Functional rafts in cell membranes. Nature 1997, 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 40
    • 58149204290 scopus 로고    scopus 로고
    • Ceramide-enriched membrane domains-Structure and function
    • Zhang, Y.; Li, X.; Becker, K. A.; Gulbins, E. Ceramide-enriched membrane domains-Structure and function. Biochim. Biophys. Acta 2009, 1788, 178-183.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 178-183
    • Zhang, Y.1    Li, X.2    Becker, K.A.3    Gulbins, E.4
  • 41
    • 77951910348 scopus 로고    scopus 로고
    • Ceramide-rich platforms in transmembrane signaling
    • Stancevic, B.; Kolesnick, R. Ceramide-rich platforms in transmembrane signaling. FEBS Lett. 2010, 584, 1728-1740.
    • (2010) FEBS Lett , vol.584 , pp. 1728-1740
    • Stancevic, B.1    Kolesnick, R.2
  • 44
    • 0242574357 scopus 로고    scopus 로고
    • Raft ceramide in molecular medicine
    • Gulbins, E.; Kolesnick, R. Raft ceramide in molecular medicine. Oncogene 2003, 22, 7070-7077.
    • (2003) Oncogene , vol.22 , pp. 7070-7077
    • Gulbins, E.1    Kolesnick, R.2
  • 45
    • 0141757451 scopus 로고    scopus 로고
    • Radiation and ceramide-induced apoptosis
    • Kolesnick, R.; Fuks, Z. Radiation and ceramide-induced apoptosis. Oncogene 2003, 22, 5897-5906.
    • (2003) Oncogene , vol.22 , pp. 5897-5906
    • Kolesnick, R.1    Fuks, Z.2
  • 46
    • 77649247134 scopus 로고    scopus 로고
    • Activation of membrane NADPH oxidase associated with lysosome-targeted acid sphingomyelinase in coronary endothelial cells
    • Bao, J. X.; Jin, S.; Zhang, F.; Wang, Z. C.; Li, N.; Li, P. L. Activation of membrane NADPH oxidase associated with lysosome-targeted acid sphingomyelinase in coronary endothelial cells. Antioxid. Redox Signal. 2010, 12, 703-712.
    • (2010) Antioxid. Redox Signal , vol.12 , pp. 703-712
    • Bao, J.X.1    Jin, S.2    Zhang, F.3    Wang, Z.C.4    Li, N.5    Li, P.L.6
  • 47
    • 31744443116 scopus 로고    scopus 로고
    • Lipid raft clustering and redox signaling platform formation in coronary arterial endothelial cells
    • Zhang, A. Y.; Yi, F.; Zhang, G.; Gulbins, E.; Li, P. L. Lipid raft clustering and redox signaling platform formation in coronary arterial endothelial cells. Hypertension 2006, 47, 74-80.
    • (2006) Hypertension , vol.47 , pp. 74-80
    • Zhang, A.Y.1    Yi, F.2    Zhang, G.3    Gulbins, E.4    Li, P.L.5
  • 48
    • 0034924486 scopus 로고    scopus 로고
    • The amplification of TCR signaling by dynamic membrane microdomains
    • Viola, A. The amplification of TCR signaling by dynamic membrane microdomains. Trends Immunol. 2001, 22, 322-327.
    • (2001) Trends Immunol , vol.22 , pp. 322-327
    • Viola, A.1
  • 49
    • 84872316510 scopus 로고    scopus 로고
    • TRAIL death receptor 4 signaling via lysosome fusion and membrane raft clustering in coronary arterial endothelial cells: Evidence from ASM knockout mice
    • Li, X.; Han, W. Q.; Boini, K. M.; Xia, M.; Zhang, Y.; Li, P. L. TRAIL death receptor 4 signaling via lysosome fusion and membrane raft clustering in coronary arterial endothelial cells: Evidence from ASM knockout mice. J. Mol. Med. 2013, 91, 25-36.
    • (2013) J. Mol. Med , vol.91 , pp. 25-36
    • Li, X.1    Han, W.Q.2    Boini, K.M.3    Xia, M.4    Zhang, Y.5    Li, P.L.6
  • 50
    • 40749145747 scopus 로고    scopus 로고
    • Critical role of lipid raft redox signaling platforms in endostatin-induced coronary endothelial dysfunction
    • Jin, S.; Zhang, Y.; Yi, F.; Li, P. L. Critical role of lipid raft redox signaling platforms in endostatin-induced coronary endothelial dysfunction. Arterioscler. Thromb. Vasc. Biol. 2008, 28, 485-490.
    • (2008) Arterioscler. Thromb. Vasc. Biol , vol.28 , pp. 485-490
    • Jin, S.1    Zhang, Y.2    Yi, F.3    Li, P.L.4
  • 51
    • 54949089213 scopus 로고    scopus 로고
    • NADPH oxidase mediates radiation-induced oxidative stress in rat brain microvascular endothelial cells
    • Collins-Underwood, J. R.; Zhao, W.; Sharpe, J. G.; Robbins, M. E. NADPH oxidase mediates radiation-induced oxidative stress in rat brain microvascular endothelial cells. Free Radic. Biol. Med. 2008, 45, 929-938.
    • (2008) Free Radic. Biol. Med , vol.45 , pp. 929-938
    • Collins-Underwood, J.R.1    Zhao, W.2    Sharpe, J.G.3    Robbins, M.E.4
  • 52
    • 0141510031 scopus 로고    scopus 로고
    • Sphingomyelinase activity causes transbilayer lipid translocation in model and cell membranes
    • Contreras, F. X.; Villar, A. V.; Alonso, A.; Kolesnick, R. N.; Goni, F. M. Sphingomyelinase activity causes transbilayer lipid translocation in model and cell membranes. J. Biol. Chem. 2003, 278, 37169-37174.
    • (2003) J. Biol. Chem , vol.278 , pp. 37169-37174
    • Contreras, F.X.1    Villar, A.V.2    Alonso, A.3    Kolesnick, R.N.4    Goni, F.M.5
  • 53
    • 0033575310 scopus 로고    scopus 로고
    • Long chain ceramides activate protein phosphatase-1 and protein phosphatase-2A. Activation is stereospecific and regulated by phosphatidic acid
    • Chalfant, C. E.; Kishikawa, K.; Mumby, M. C.; Kamibayashi, C.; Bielawska, A.; Hannun, Y. A. Long chain ceramides activate protein phosphatase-1 and protein phosphatase-2A. Activation is stereospecific and regulated by phosphatidic acid. J. Biol. Chem. 1999, 274, 20313-20317.
    • (1999) J. Biol. Chem , vol.274 , pp. 20313-20317
    • Chalfant, C.E.1    Kishikawa, K.2    Mumby, M.C.3    Kamibayashi, C.4    Bielawska, A.5    Hannun, Y.A.6
  • 54
    • 1542723736 scopus 로고    scopus 로고
    • The structural requirements for ceramide activation of serine-threonine protein phosphatases
    • Chalfant, C. E.; Szulc, Z.; Roddy, P.; Bielawska, A.; Hannun, Y. A. The structural requirements for ceramide activation of serine-threonine protein phosphatases. J. Lipid Res. 2004, 45, 496-506.
    • (2004) J. Lipid Res , vol.45 , pp. 496-506
    • Chalfant, C.E.1    Szulc, Z.2    Roddy, P.3    Bielawska, A.4    Hannun, Y.A.5
  • 55
    • 0035893385 scopus 로고    scopus 로고
    • Kinase suppressor of Ras determines survival of intestinal epithelial cells exposed to tumor necrosis factor
    • Yan, F.; John, S. K.; Polk, D. B. Kinase suppressor of Ras determines survival of intestinal epithelial cells exposed to tumor necrosis factor. Cancer Res. 2001, 61, 8668-8675.
    • (2001) Cancer Res , vol.61 , pp. 8668-8675
    • Yan, F.1    John, S.K.2    Polk, D.B.3
  • 58
    • 0034634596 scopus 로고    scopus 로고
    • Ceramide directly activates protein kinase C zeta to regulate a stress-activated protein kinase signaling complex
    • Bourbon, N. A.; Yun, J.; Kester, M. Ceramide directly activates protein kinase C zeta to regulate a stress-activated protein kinase signaling complex. J. Biol. Chem. 2000, 275, 35617-35623.
    • (2000) J. Biol. Chem , vol.275 , pp. 35617-35623
    • Bourbon, N.A.1    Yun, J.2    Kester, M.3
  • 59
    • 0027965006 scopus 로고
    • Protein kinase C zeta isoform is critical for kappa B-dependent promoter activation by sphingomyelinase
    • Lozano, J.; Berra, E.; Municio, M. M.; Diaz-Meco, M. T.; Dominguez, I.; Sanz, L.; Moscat, J. Protein kinase C zeta isoform is critical for kappa B-dependent promoter activation by sphingomyelinase. J. Biol. Chem. 1994, 269, 19200-19202.
    • (1994) J. Biol. Chem , vol.269 , pp. 19200-19202
    • Lozano, J.1    Berra, E.2    Municio, M.M.3    Diaz-Meco, M.T.4    Dominguez, I.5    Sanz, L.6    Moscat, J.7
  • 60
    • 0029003788 scopus 로고
    • PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid
    • Muller, G.; Ayoub, M.; Storz, P.; Rennecke, J.; Fabbro, D.; Pfizenmaier, K. PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid. EMBO J. 1995, 14, 1961-1969.
    • (1995) EMBO J , vol.14 , pp. 1961-1969
    • Muller, G.1    Ayoub, M.2    Storz, P.3    Rennecke, J.4    Fabbro, D.5    Pfizenmaier, K.6
  • 64
    • 0029810967 scopus 로고    scopus 로고
    • Tyrosine phosphorylation-dependent suppression of a voltage-gated K+ channel in T lymphocytes upon Fas stimulation
    • Szabo, I.; Gulbins, E.; Apfel, H.; Zhang, X.; Barth, P.; Busch, A. E.; Schlottmann, K.; Pongs, O.; Lang, F. Tyrosine phosphorylation-dependent suppression of a voltage-gated K+ channel in T lymphocytes upon Fas stimulation. J. Biol. Chem. 1996, 271, 20465-20469.
    • (1996) J. Biol. Chem , vol.271 , pp. 20465-20469
    • Szabo, I.1    Gulbins, E.2    Apfel, H.3    Zhang, X.4    Barth, P.5    Busch, A.E.6    Schlottmann, K.7    Pongs, O.8    Lang, F.9
  • 65
    • 57749176350 scopus 로고    scopus 로고
    • Peroxynitrite-dependent activation of protein phosphatase type 2A mediates microvascular endothelial barrier dysfunction
    • Wu, F.; Wilson, J. X. Peroxynitrite-dependent activation of protein phosphatase type 2A mediates microvascular endothelial barrier dysfunction. Cardiovasc. Res. 2009, 81, 38-45.
    • (2009) Cardiovasc. Res , vol.81 , pp. 38-45
    • Wu, F.1    Wilson, J.X.2
  • 66
    • 30044436438 scopus 로고    scopus 로고
    • Cathepsin D and H2O2 stimulate degradation of thioredoxin-1: Implication for endothelial cell apoptosis
    • Haendeler, J.; Popp, R.; Goy, C.; Tischler, V.; Zeiher, A. M.; Dimmeler, S. Cathepsin D and H2O2 stimulate degradation of thioredoxin-1: Implication for endothelial cell apoptosis. J. Biol. Chem. 2005, 280, 42945-42951.
    • (2005) J. Biol. Chem , vol.280 , pp. 42945-42951
    • Haendeler, J.1    Popp, R.2    Goy, C.3    Tischler, V.4    Zeiher, A.M.5    Dimmeler, S.6
  • 67
    • 70350455599 scopus 로고    scopus 로고
    • Phosphorylation of endothelial nitric oxide synthase by atypical PKC zeta contributes to angiopoietin-1-dependent inhibition of VEGF-induced endothelial permeability in vitro
    • Oubaha, M.; Gratton, J. P. Phosphorylation of endothelial nitric oxide synthase by atypical PKC zeta contributes to angiopoietin-1-dependent inhibition of VEGF-induced endothelial permeability in vitro. Blood 2009, 114, 3343-3351.
    • (2009) Blood , vol.114 , pp. 3343-3351
    • Oubaha, M.1    Gratton, J.P.2
  • 68
    • 0023022340 scopus 로고
    • Reversible alterations in cultured pulmonary artery endothelial cell monolayer morphology and albumin permeability induced by ionizing radiation
    • Friedman, M.; Ryan, U. S.; Davenport, W. C.; Chaney, E. L.; Strickland, D. L.; Kwock, L. Reversible alterations in cultured pulmonary artery endothelial cell monolayer morphology and albumin permeability induced by ionizing radiation. J. Cell Physiol. 1986, 129, 237-249.
    • (1986) J. Cell Physiol , vol.129 , pp. 237-249
    • Friedman, M.1    Ryan, U.S.2    Davenport, W.C.3    Chaney, E.L.4    Strickland, D.L.5    Kwock, L.6
  • 69
    • 36148979672 scopus 로고    scopus 로고
    • Radiation effects on the cytoskeleton of endothelial cells and endothelial monolayer permeability
    • Gabrys, D.; Greco, O.; Patel, G.; Prise, K. M.; Tozer, G. M.; Kanthou, C. Radiation effects on the cytoskeleton of endothelial cells and endothelial monolayer permeability. Int. J. Radiat. Oncol. Biol. Phys. 2007, 69, 1553-1562.
    • (2007) Int. J. Radiat. Oncol. Biol. Phys , vol.69 , pp. 1553-1562
    • Gabrys, D.1    Greco, O.2    Patel, G.3    Prise, K.M.4    Tozer, G.M.5    Kanthou, C.6
  • 71
    • 0033103156 scopus 로고    scopus 로고
    • Radiation induced endothelial cell retraction in vitro: Correlation with acute pulmonary edema
    • Onoda, J. M.; Kantak, S. S.; Diglio, C. A. Radiation induced endothelial cell retraction in vitro: Correlation with acute pulmonary edema. Pathol. Oncol. Res. 1999, 5, 49-55.
    • (1999) Pathol. Oncol. Res , vol.5 , pp. 49-55
    • Onoda, J.M.1    Kantak, S.S.2    Diglio, C.A.3
  • 72
    • 84870209800 scopus 로고    scopus 로고
    • Rho family GTPases
    • Hall, A. Rho family GTPases. Biochem. Soc. Trans. 2012, 40, 1378-1382.
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 1378-1382
    • Hall, A.1
  • 73
    • 84870914919 scopus 로고    scopus 로고
    • Mast cells and ionizing radiation induce a synergistic expression of inflammatory genes in endothelial cells by a mechanism involving p38alpha MAP kinase and (p65) NF-kappaB activation
    • Blirando, K.; Hneino, M.; Martelly, I.; Benderitter, M.; Milliat, F.; Francois, A. Mast cells and ionizing radiation induce a synergistic expression of inflammatory genes in endothelial cells by a mechanism involving p38alpha MAP kinase and (p65) NF-kappaB activation. Radiat. Res. 2012, 178, 556-567.
    • (2012) Radiat. Res , vol.178 , pp. 556-567
    • Blirando, K.1    Hneino, M.2    Martelly, I.3    Benderitter, M.4    Milliat, F.5    Francois, A.6
  • 75
    • 0030803278 scopus 로고    scopus 로고
    • Fas-or ceramide-induced apoptosis is mediated by a Rac1-regulated activation of Jun N-terminal kinase/p38 kinases and GADD153
    • Brenner, B.; Koppenhoefer, U.; Weinstock, C.; Linderkamp, O.; Lang, F.; Gulbins, E. Fas-or ceramide-induced apoptosis is mediated by a Rac1-regulated activation of Jun N-terminal kinase/p38 kinases and GADD153. J. Biol. Chem. 1997, 272, 22173-22181.
    • (1997) J. Biol. Chem , vol.272 , pp. 22173-22181
    • Brenner, B.1    Koppenhoefer, U.2    Weinstock, C.3    Linderkamp, O.4    Lang, F.5    Gulbins, E.6
  • 77
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • Plowman, S. J.; Muncke, C.; Parton, R. G.; Hancock, J. F. H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc. Natl. Acad. Sci. USA 2005, 102, 15500-15505.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 78
    • 33747826874 scopus 로고    scopus 로고
    • Preventing or reducing late side effects of radiation therapy: Radiobiology meets molecular pathology
    • Bentzen, S. M. Preventing or reducing late side effects of radiation therapy: Radiobiology meets molecular pathology. Nat. Rev. Cancer 2006, 6, 702-713.
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 702-713
    • Bentzen, S.M.1
  • 80
    • 77952943373 scopus 로고    scopus 로고
    • Small molecule inhibitors of acid sphingomyelinase
    • Arenz, C. Small molecule inhibitors of acid sphingomyelinase. Cell Physiol. Biochem. 2010, 26, 1-8.
    • (2010) Cell Physiol. Biochem , vol.26 , pp. 1-8
    • Arenz, C.1
  • 81
    • 77952908473 scopus 로고    scopus 로고
    • Functional Inhibitors of Acid Sphingomyelinase (FIASMAs): A novel pharmacological group of drugs with broad clinical applications
    • Kornhuber, J.; Tripal, P.; Reichel, M.; Muhle, C.; Rhein, C.; Muehlbacher, M.; Groemer, T. W.; Gulbins, E. Functional Inhibitors of Acid Sphingomyelinase (FIASMAs): A novel pharmacological group of drugs with broad clinical applications. Cell Physiol. Biochem. 2010, 26, 9-20.
    • (2010) Cell Physiol. Biochem , vol.26 , pp. 9-20
    • Kornhuber, J.1    Tripal, P.2    Reichel, M.3    Muhle, C.4    Rhein, C.5    Muehlbacher, M.6    Groemer, T.W.7    Gulbins, E.8
  • 83
    • 84875869921 scopus 로고    scopus 로고
    • Therapy of CF-patients with amitriptyline and placebo-A randomised, double-blind, placebo-controlled phase IIb multicenter, cohort-study
    • Nahrlich, L.; Mainz, J. G.; Adams, C.; Engel, C.; Herrmann, G.; Icheva, V.; Lauer, J.; Deppisch, C.; Wirth, A.; Unger, K.; et al. Therapy of CF-patients with amitriptyline and placebo-A randomised, double-blind, placebo-controlled phase IIb multicenter, cohort-study. Cell Physiol. Biochem. 2013, 31, 505-512.
    • (2013) Cell Physiol. Biochem , vol.31 , pp. 505-512
    • Nahrlich, L.1    Mainz, J.G.2    Adams, C.3    Engel, C.4    Herrmann, G.5    Icheva, V.6    Lauer, J.7    Deppisch, C.8    Wirth, A.9    Unger, K.10
  • 85
    • 0037133306 scopus 로고    scopus 로고
    • Pharmacological treatment of coronary artery disease with recombinant fibroblast growth factor-2: Double-blind, randomized, controlled clinical trial
    • Simons, M.; Annex, B. H.; Laham, R. J.; Kleiman, N.; Henry, T.; Dauerman, H.; Udelson, J. E.; Gervino, E. V.; Pike, M.; Whitehouse, M. J.; et al. Pharmacological treatment of coronary artery disease with recombinant fibroblast growth factor-2: Double-blind, randomized, controlled clinical trial. Circulation 2002, 105, 788-793.
    • (2002) Circulation , vol.105 , pp. 788-793
    • Simons, M.1    Annex, B.H.2    Laham, R.J.3    Kleiman, N.4    Henry, T.5    Dauerman, H.6    Udelson, J.E.7    Gervino, E.V.8    Pike, M.9    Whitehouse, M.J.10
  • 94
    • 33847793485 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate protects proliferating endothelial cells from ceramide-induced apoptosis but not from DNA damage-induced mitotic death
    • Bonnaud, S.; Niaudet, C.; Pottier, G.; Gaugler, M. H.; Millour, J.; Barbet, J.; Sabatier, L.; Paris, F. Sphingosine-1-phosphate protects proliferating endothelial cells from ceramide-induced apoptosis but not from DNA damage-induced mitotic death. Cancer Res. 2007, 67, 1803-1811.
    • (2007) Cancer Res , vol.67 , pp. 1803-1811
    • Bonnaud, S.1    Niaudet, C.2    Pottier, G.3    Gaugler, M.H.4    Millour, J.5    Barbet, J.6    Sabatier, L.7    Paris, F.8
  • 95
  • 96
    • 84863911000 scopus 로고    scopus 로고
    • Cholesterol-lowering drugs inhibit lectin-like oxidized low-density lipoprotein-1 receptor function by membrane raft disruption
    • Matarazzo, S.; Quitadamo, M. C.; Mango, R.; Ciccone, S.; Novelli, G.; Biocca, S. Cholesterol-lowering drugs inhibit lectin-like oxidized low-density lipoprotein-1 receptor function by membrane raft disruption. Mol. Pharmacol. 2012, 82, 246-254.
    • (2012) Mol. Pharmacol , vol.82 , pp. 246-254
    • Matarazzo, S.1    Quitadamo, M.C.2    Mango, R.3    Ciccone, S.4    Novelli, G.5    Biocca, S.6
  • 98
    • 19444379395 scopus 로고    scopus 로고
    • Pravastatin limits endothelial activation after irradiation and decreases the resulting inflammatory and thrombotic responses
    • Gaugler, M. H.; Vereycken-Holler, V.; Squiban, C.; Vandamme, M.; Vozenin-Brotons, M. C.; Benderitter, M. Pravastatin limits endothelial activation after irradiation and decreases the resulting inflammatory and thrombotic responses. Radiat. Res. 2005, 163, 479-487.
    • (2005) Radiat. Res , vol.163 , pp. 479-487
    • Gaugler, M.H.1    Vereycken-Holler, V.2    Squiban, C.3    Vandamme, M.4    Vozenin-Brotons, M.C.5    Benderitter, M.6
  • 100
    • 31844451010 scopus 로고    scopus 로고
    • Anti-inflammatory effects of statins: Clinical evidence and basic mechanisms
    • Jain, M. K.; Ridker, P. M. Anti-inflammatory effects of statins: Clinical evidence and basic mechanisms. Nat. Rev. Drug Discov. 2005, 4, 977-987.
    • (2005) Nat. Rev. Drug Discov , vol.4 , pp. 977-987
    • Jain, M.K.1    Ridker, P.M.2
  • 101
    • 14544278377 scopus 로고    scopus 로고
    • Inhibition of Rho kinase modulates radiation induced fibrogenic phenotype in intestinal smooth muscle cells through alteration of the cytoskeleton and connective tissue growth factor expression
    • Bourgier, C.; Haydont, V.; Milliat, F.; Francois, A.; Holler, V.; Lasser, P.; Bourhis, J.; Mathe, D.; Vozenin-Brotons, M. C. Inhibition of Rho kinase modulates radiation induced fibrogenic phenotype in intestinal smooth muscle cells through alteration of the cytoskeleton and connective tissue growth factor expression. Gut 2005, 54, 336-343.
    • (2005) Gut , vol.54 , pp. 336-343
    • Bourgier, C.1    Haydont, V.2    Milliat, F.3    Francois, A.4    Holler, V.5    Lasser, P.6    Bourhis, J.7    Mathe, D.8    Vozenin-Brotons, M.C.9
  • 102
    • 34848906040 scopus 로고    scopus 로고
    • Pravastatin Inhibits the Rho/CCN2/extracellular matrix cascade in human fibrosis explants and improves radiation-induced intestinal fibrosis in rats
    • Haydont, V.; Bourgier, C.; Pocard, M.; Lusinchi, A.; Aigueperse, J.; Mathe, D.; Bourhis, J.; Vozenin-Brotons, M. C. Pravastatin Inhibits the Rho/CCN2/extracellular matrix cascade in human fibrosis explants and improves radiation-induced intestinal fibrosis in rats. Clin. Cancer Res. 2007, 13, 5331-5340.
    • (2007) Clin. Cancer Res , vol.13 , pp. 5331-5340
    • Haydont, V.1    Bourgier, C.2    Pocard, M.3    Lusinchi, A.4    Aigueperse, J.5    Mathe, D.6    Bourhis, J.7    Vozenin-Brotons, M.C.8
  • 103
    • 84879636711 scopus 로고    scopus 로고
    • Strategies for optimizing the response of cancer and normal tissues to radiation
    • Moding, E. J.; Kastan, M. B.; Kirsch, D. G. Strategies for optimizing the response of cancer and normal tissues to radiation. Nat. Rev. Drug Discov. 2013, 12, 526-542.
    • (2013) Nat. Rev. Drug Discov , vol.12 , pp. 526-542
    • Moding, E.J.1    Kastan, M.B.2    Kirsch, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.