메뉴 건너뛰기




Volumn 313, Issue 16, 2007, Pages 3421-3431

Fas ligand-induced apoptosis is regulated by nitric oxide through the inhibition of fas receptor clustering and the nitrosylation of protein kinase Cε

Author keywords

Apoptosis; Nitrosylation; Protein kinase C; Receptor clustering; Trophoblast

Indexed keywords

FAS LIGAND; NITRIC OXIDE; PROTEIN KINASE C ALPHA; PROTEIN KINASE C EPSILON; RECEPTOR; SMALL INTERFERING RNA;

EID: 34548610177     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2007.05.030     Document Type: Article
Times cited : (20)

References (43)
  • 1
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signaling pathway: more than a paradigm
    • Wajant H. The Fas signaling pathway: more than a paradigm. Science 296 (2002) 1635-1636
    • (2002) Science , vol.296 , pp. 1635-1636
    • Wajant, H.1
  • 2
    • 0033853079 scopus 로고    scopus 로고
    • TNF-alpha/TNFRI in primary and immortalized first trimester cytotrophoblasts
    • Knofler M., Mosl B., Bauer S., Griesinger G., and Husslein P. TNF-alpha/TNFRI in primary and immortalized first trimester cytotrophoblasts. Placenta 21 (2000) 525-535
    • (2000) Placenta , vol.21 , pp. 525-535
    • Knofler, M.1    Mosl, B.2    Bauer, S.3    Griesinger, G.4    Husslein, P.5
  • 3
    • 0031955360 scopus 로고    scopus 로고
    • Immunolocalization of tumour necrosis factor-alpha (TNF-alpha) in the placental bed of normotensive and hypertensive human pregnancies
    • Pijnenborg R., McLaughlin P.J., Vercruysse L., Hanssens M., Johnson P.M., Keith J.C., and Van Assche F.A. Immunolocalization of tumour necrosis factor-alpha (TNF-alpha) in the placental bed of normotensive and hypertensive human pregnancies. Placenta 19 (1998) 231-239
    • (1998) Placenta , vol.19 , pp. 231-239
    • Pijnenborg, R.1    McLaughlin, P.J.2    Vercruysse, L.3    Hanssens, M.4    Johnson, P.M.5    Keith, J.C.6    Van Assche, F.A.7
  • 6
    • 0030921819 scopus 로고    scopus 로고
    • Expression of the apoptosis-inducing Fas ligand (FasL) in human first and third trimester placenta and choriocarcinoma cells
    • Bamberger A.M., Schulte H.M., Thuneke I., Erdmann I., Bamberger C.M., and Asa S.L. Expression of the apoptosis-inducing Fas ligand (FasL) in human first and third trimester placenta and choriocarcinoma cells. J. Clin. Endocrinol. Metab. 82 (1997) 3173-3175
    • (1997) J. Clin. Endocrinol. Metab. , vol.82 , pp. 3173-3175
    • Bamberger, A.M.1    Schulte, H.M.2    Thuneke, I.3    Erdmann, I.4    Bamberger, C.M.5    Asa, S.L.6
  • 7
    • 0033563139 scopus 로고    scopus 로고
    • TRAIL (Apo-2L) and TRAIL receptors in human placentas: implications for immune privilege
    • Phillips T.A., Ni J., Pan G., Ruben S.M., Wei Y.F., Pace J.L., and Hunt J.S. TRAIL (Apo-2L) and TRAIL receptors in human placentas: implications for immune privilege. J. Immunol. 162 (1999) 6053-6059
    • (1999) J. Immunol. , vol.162 , pp. 6053-6059
    • Phillips, T.A.1    Ni, J.2    Pan, G.3    Ruben, S.M.4    Wei, Y.F.5    Pace, J.L.6    Hunt, J.S.7
  • 8
    • 0032920603 scopus 로고    scopus 로고
    • Death receptor Fas/Apo-1/CD95 expressed by human placental cytotrophoblasts does not mediate apoptosis
    • Payne S.G., Smith S.C., Davidge S.T., Baker P.N., and Guilbert L.J. Death receptor Fas/Apo-1/CD95 expressed by human placental cytotrophoblasts does not mediate apoptosis. Biol. Reprod. 60 (1999) 1144-1150
    • (1999) Biol. Reprod. , vol.60 , pp. 1144-1150
    • Payne, S.G.1    Smith, S.C.2    Davidge, S.T.3    Baker, P.N.4    Guilbert, L.J.5
  • 9
    • 0034883831 scopus 로고    scopus 로고
    • Macrophage-induced apoptosis limits endovascular trophoblast invasion in the uterine wall of preeclamptic women
    • Reister F., Frank H.G., Kingdom J.C., Heyl W., Kaufmann P., Rath W., and Huppertz B. Macrophage-induced apoptosis limits endovascular trophoblast invasion in the uterine wall of preeclamptic women. Lab. Invest. 81 (2001) 1143-1152
    • (2001) Lab. Invest. , vol.81 , pp. 1143-1152
    • Reister, F.1    Frank, H.G.2    Kingdom, J.C.3    Heyl, W.4    Kaufmann, P.5    Rath, W.6    Huppertz, B.7
  • 10
    • 0035988264 scopus 로고    scopus 로고
    • Differential regulation and function of the Fas/Fas ligand system in human trophoblast cells
    • Aschkenazi S., Straszewski S., Verwer K.M., Foellmer H., Rutherford T., and Mor G. Differential regulation and function of the Fas/Fas ligand system in human trophoblast cells. Biol. Reprod. 66 (2002) 1853-1861
    • (2002) Biol. Reprod. , vol.66 , pp. 1853-1861
    • Aschkenazi, S.1    Straszewski, S.2    Verwer, K.M.3    Foellmer, H.4    Rutherford, T.5    Mor, G.6
  • 12
    • 0032983892 scopus 로고    scopus 로고
    • Preeclampsia is associated with widespread apoptosis of placental cytotrophoblasts within the uterine wall
    • DiFederico E., Genbacev O., and Fisher S.J. Preeclampsia is associated with widespread apoptosis of placental cytotrophoblasts within the uterine wall. Am. J. Pathol. 155 (1999) 293-301
    • (1999) Am. J. Pathol. , vol.155 , pp. 293-301
    • DiFederico, E.1    Genbacev, O.2    Fisher, S.J.3
  • 14
    • 0043205903 scopus 로고    scopus 로고
    • Nitric oxide protects human extravillous trophoblast cells from apoptosis by a cyclic GMP-dependent mechanism and independently of caspase 3 nitrosylation
    • Dash P.R., Cartwright J.E., Baker P.N., Johnstone A.P., and Whitley G.S. Nitric oxide protects human extravillous trophoblast cells from apoptosis by a cyclic GMP-dependent mechanism and independently of caspase 3 nitrosylation. Exp. Cell Res. 287 (2003) 314-324
    • (2003) Exp. Cell Res. , vol.287 , pp. 314-324
    • Dash, P.R.1    Cartwright, J.E.2    Baker, P.N.3    Johnstone, A.P.4    Whitley, G.S.5
  • 15
    • 0038736870 scopus 로고    scopus 로고
    • Nitric oxide inhibits polyamine-induced apoptosis in the human extravillous trophoblast cell line SGHPL-4
    • Dash P.R., Cartwright J.E., and Whitely G.S. Nitric oxide inhibits polyamine-induced apoptosis in the human extravillous trophoblast cell line SGHPL-4. Hum. Reprod. 18 (2003) 959-968
    • (2003) Hum. Reprod. , vol.18 , pp. 959-968
    • Dash, P.R.1    Cartwright, J.E.2    Whitely, G.S.3
  • 16
    • 15944405002 scopus 로고    scopus 로고
    • Trophoblast apoptosis is inhibited by hepatocyte growth factor through the Akt and beta-catenin mediated up-regulation of inducible nitric oxide synthase
    • Dash P.R., Whitley G.S., Ayling L.J., Johnstone A.P., and Cartwright J.E. Trophoblast apoptosis is inhibited by hepatocyte growth factor through the Akt and beta-catenin mediated up-regulation of inducible nitric oxide synthase. Cell. Signal. 17 (2005) 571-580
    • (2005) Cell. Signal. , vol.17 , pp. 571-580
    • Dash, P.R.1    Whitley, G.S.2    Ayling, L.J.3    Johnstone, A.P.4    Cartwright, J.E.5
  • 17
    • 0031728394 scopus 로고    scopus 로고
    • The phagocytic activity of human first trimester extravillous trophoblast
    • Choy M.Y., and Manyonda I.T. The phagocytic activity of human first trimester extravillous trophoblast. Hum. Reprod. 13 (1998) 2941-2949
    • (1998) Hum. Reprod. , vol.13 , pp. 2941-2949
    • Choy, M.Y.1    Manyonda, I.T.2
  • 18
    • 0032881107 scopus 로고    scopus 로고
    • Hepatocyte growth factor regulates human trophoblast motility and invasion: a role for nitric oxide
    • Cartwright J.E., Holden D.P., and Whitley G.S. Hepatocyte growth factor regulates human trophoblast motility and invasion: a role for nitric oxide. Br. J. Pharmacol. 128 (1999) 181-189
    • (1999) Br. J. Pharmacol. , vol.128 , pp. 181-189
    • Cartwright, J.E.1    Holden, D.P.2    Whitley, G.S.3
  • 21
    • 0030458834 scopus 로고    scopus 로고
    • Protein kinase C in cultured human placental trophoblasts: identification of isoforms and role in cAMP signalling
    • Karl P.I., and Divald A. Protein kinase C in cultured human placental trophoblasts: identification of isoforms and role in cAMP signalling. Biochem. J. 320 Pt 3 (1996) 831-836
    • (1996) Biochem. J. , vol.320 , Issue.PART 3 , pp. 831-836
    • Karl, P.I.1    Divald, A.2
  • 22
    • 0141841765 scopus 로고    scopus 로고
    • Effect of selective PKC isoform activation and inhibition on TNF-alpha-induced injury and apoptosis in human intestinal epithelial cells
    • Chang Q., and Tepperman B.L. Effect of selective PKC isoform activation and inhibition on TNF-alpha-induced injury and apoptosis in human intestinal epithelial cells. Br. J. Pharmacol. 140 (2003) 41-52
    • (2003) Br. J. Pharmacol. , vol.140 , pp. 41-52
    • Chang, Q.1    Tepperman, B.L.2
  • 24
    • 0042335762 scopus 로고    scopus 로고
    • Ceramide-mediated clustering is required for CD95-DISC formation
    • Grassme H., Cremesti A., Kolesnick R., and Gulbins E. Ceramide-mediated clustering is required for CD95-DISC formation. Oncogene 22 (2003) 5457-5470
    • (2003) Oncogene , vol.22 , pp. 5457-5470
    • Grassme, H.1    Cremesti, A.2    Kolesnick, R.3    Gulbins, E.4
  • 25
    • 16844381848 scopus 로고    scopus 로고
    • The extracellular domains of FasL and Fas are sufficient for the formation of supramolecular FasL-Fas clusters of high stability
    • Henkler F., Behrle E., Dennehy K.M., Wicovsky A., Peters N., Warnke C., Pfizenmaier K., and Wajant H. The extracellular domains of FasL and Fas are sufficient for the formation of supramolecular FasL-Fas clusters of high stability. J. Cell Biol. 168 (2005) 1087-1098
    • (2005) J. Cell Biol. , vol.168 , pp. 1087-1098
    • Henkler, F.1    Behrle, E.2    Dennehy, K.M.3    Wicovsky, A.4    Peters, N.5    Warnke, C.6    Pfizenmaier, K.7    Wajant, H.8
  • 26
    • 19544382901 scopus 로고    scopus 로고
    • The caspase-8 modulator c-FLIP
    • Kataoka T. The caspase-8 modulator c-FLIP. Crit. Rev. Immunol. 25 (2005) 31-58
    • (2005) Crit. Rev. Immunol. , vol.25 , pp. 31-58
    • Kataoka, T.1
  • 30
    • 0036850413 scopus 로고    scopus 로고
    • Cyclic GMP-dependent inhibition of acid sphingomyelinase by nitric oxide: an early step in protection against apoptosis
    • Barsacchi R., Perrotta C., Sestili P., Cantoni O., Moncada S., and Clementi E. Cyclic GMP-dependent inhibition of acid sphingomyelinase by nitric oxide: an early step in protection against apoptosis. Cell Death Differ. 9 (2002) 1248-1255
    • (2002) Cell Death Differ. , vol.9 , pp. 1248-1255
    • Barsacchi, R.1    Perrotta, C.2    Sestili, P.3    Cantoni, O.4    Moncada, S.5    Clementi, E.6
  • 31
    • 29644432729 scopus 로고    scopus 로고
    • Nitric oxide negatively regulates Fas CD95-induced apoptosis through inhibition of ubiquitin-proteasome-mediated degradation of FLICE inhibitory protein
    • Chanvorachote P., Nimmannit U., Wang L., Stehlik C., Lu B., Azad N., and Rojanasakul Y. Nitric oxide negatively regulates Fas CD95-induced apoptosis through inhibition of ubiquitin-proteasome-mediated degradation of FLICE inhibitory protein. J. Biol. Chem. 280 (2005) 42044-42050
    • (2005) J. Biol. Chem. , vol.280 , pp. 42044-42050
    • Chanvorachote, P.1    Nimmannit, U.2    Wang, L.3    Stehlik, C.4    Lu, B.5    Azad, N.6    Rojanasakul, Y.7
  • 32
    • 0037710311 scopus 로고    scopus 로고
    • The isoform-specific regulation of apoptosis by protein kinase C
    • Gutcher I., Webb P.R., and Anderson N.G. The isoform-specific regulation of apoptosis by protein kinase C. Cell. Mol. Life Sci. 60 (2003) 1061-1070
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1061-1070
    • Gutcher, I.1    Webb, P.R.2    Anderson, N.G.3
  • 33
    • 21644447437 scopus 로고    scopus 로고
    • Protein kinase C zeta associates with death inducing signaling complex and regulates Fas ligand-induced apoptosis
    • Leroy I., de Thonel A., Laurent G., and Quillet-Mary A. Protein kinase C zeta associates with death inducing signaling complex and regulates Fas ligand-induced apoptosis. Cell. Signal. 17 (2005) 1149-1157
    • (2005) Cell. Signal. , vol.17 , pp. 1149-1157
    • Leroy, I.1    de Thonel, A.2    Laurent, G.3    Quillet-Mary, A.4
  • 34
    • 0039791449 scopus 로고    scopus 로고
    • Activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by conventional, novel, and atypical protein kinase C isotypes
    • Schonwasser D.C., Marais R.M., Marshall C.J., and Parker P.J. Activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by conventional, novel, and atypical protein kinase C isotypes. Mol. Cell. Biol. 18 (1998) 790-798
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 790-798
    • Schonwasser, D.C.1    Marais, R.M.2    Marshall, C.J.3    Parker, P.J.4
  • 35
    • 0027732536 scopus 로고
    • Nitric oxide and nitric oxide-generating agents induce a reversible inactivation of protein kinase C activity and phorbol ester binding
    • Gopalakrishna R., Chen Z.H., and Gundimeda U. Nitric oxide and nitric oxide-generating agents induce a reversible inactivation of protein kinase C activity and phorbol ester binding. J. Biol. Chem. 268 (1993) 27180-27185
    • (1993) J. Biol. Chem. , vol.268 , pp. 27180-27185
    • Gopalakrishna, R.1    Chen, Z.H.2    Gundimeda, U.3
  • 36
    • 0344034360 scopus 로고    scopus 로고
    • Thioredoxin restores nitric oxide-induced inhibition of protein kinase C activity in lung endothelial cells
    • Kahlos K., Zhang J., Block E.R., and Patel J.M. Thioredoxin restores nitric oxide-induced inhibition of protein kinase C activity in lung endothelial cells. Mol. Cell. Biochem. 254 (2003) 47-54
    • (2003) Mol. Cell. Biochem. , vol.254 , pp. 47-54
    • Kahlos, K.1    Zhang, J.2    Block, E.R.3    Patel, J.M.4
  • 37
    • 0033583131 scopus 로고    scopus 로고
    • Isoform-selective activation of protein kinase C by nitric oxide in the heart of conscious rabbits: a signaling mechanism for both nitric oxide-induced and ischemia-induced preconditioning
    • Ping P., Takano H., Zhang J., Tang X.L., Qiu Y., Li R.C., Banerjee S., Dawn B., Balafonova Z., and Bolli R. Isoform-selective activation of protein kinase C by nitric oxide in the heart of conscious rabbits: a signaling mechanism for both nitric oxide-induced and ischemia-induced preconditioning. Circ. Res. 84 (1999) 587-604
    • (1999) Circ. Res. , vol.84 , pp. 587-604
    • Ping, P.1    Takano, H.2    Zhang, J.3    Tang, X.L.4    Qiu, Y.5    Li, R.C.6    Banerjee, S.7    Dawn, B.8    Balafonova, Z.9    Bolli, R.10
  • 38
    • 0037177860 scopus 로고    scopus 로고
    • Nitric oxide (NO) induces nitration of protein kinase Cepsilon (PKCepsilon), facilitating PKCepsilon translocation via enhanced PKCepsilon-RACK2 interactions: a novel mechanism of no-triggered activation of PKCepsilon
    • Balafanova Z., Bolli R., Zhang J., Zheng Y., Pass J.M., Bhatnagar A., Tang X.L., Wang O., Cardwell E., and Ping P. Nitric oxide (NO) induces nitration of protein kinase Cepsilon (PKCepsilon), facilitating PKCepsilon translocation via enhanced PKCepsilon-RACK2 interactions: a novel mechanism of no-triggered activation of PKCepsilon. J. Biol. Chem. 277 (2002) 15021-15027
    • (2002) J. Biol. Chem. , vol.277 , pp. 15021-15027
    • Balafanova, Z.1    Bolli, R.2    Zhang, J.3    Zheng, Y.4    Pass, J.M.5    Bhatnagar, A.6    Tang, X.L.7    Wang, O.8    Cardwell, E.9    Ping, P.10
  • 41
    • 0035827569 scopus 로고    scopus 로고
    • Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex
    • Krueger A., Schmitz I., Baumann S., Krammer P.H., and Kirchhoff S. Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex. J. Biol. Chem. 276 (2001) 20633-20640
    • (2001) J. Biol. Chem. , vol.276 , pp. 20633-20640
    • Krueger, A.1    Schmitz, I.2    Baumann, S.3    Krammer, P.H.4    Kirchhoff, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.