메뉴 건너뛰기




Volumn 441, Issue 4, 2013, Pages 891-896

FERM domain promotes resveratrol-induced apoptosis in endothelial cells via inhibition of NO production

Author keywords

Apoptosis; Endothelial cells; FAK; FERM; Resveratrol

Indexed keywords

ENDOTHELIAL NITRIC OXIDE SYNTHASE; EZRIN; FOCAL ADHESION KINASE; MOESIN; NITRIC OXIDE; RADIXIN; RESVERATROL; TUMOR NECROSIS FACTOR ALPHA;

EID: 84888820840     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.10.154     Document Type: Article
Times cited : (9)

References (27)
  • 1
    • 82955233363 scopus 로고    scopus 로고
    • Focal adhesion kinase and endothelial cell apoptosis
    • Lu Q., Rounds S. Focal adhesion kinase and endothelial cell apoptosis. Microvasc. Res. 2012, 83(1):56-63.
    • (2012) Microvasc. Res. , vol.83 , Issue.1 , pp. 56-63
    • Lu, Q.1    Rounds, S.2
  • 2
    • 82955248167 scopus 로고    scopus 로고
    • How focal adhesion kinase achieves regulation by linking ligand binding, localization and action
    • Arold S.T. How focal adhesion kinase achieves regulation by linking ligand binding, localization and action. Curr. Opin. Struct. Biol. 2011, 21:808-813.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 808-813
    • Arold, S.T.1
  • 3
    • 0029055784 scopus 로고
    • Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase
    • Hildebrand J.D., Schaller M.D., Parsons J.T. Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol. Biol. Cell 1995, 6:637-647.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 637-647
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 4
    • 0029046858 scopus 로고
    • Interaction of focal adhesion kinase with cytoskeletal protein talin
    • Chen H.C., Appeddu P.A., Parsons J.T., et al. Interaction of focal adhesion kinase with cytoskeletal protein talin. J. Biol. Chem. 1995, 270:16995-16999.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16995-16999
    • Chen, H.C.1    Appeddu, P.A.2    Parsons, J.T.3
  • 5
    • 77955843731 scopus 로고    scopus 로고
    • XIAP is essential for shear stress-enhanced Tyr-576 phosphorylation of FAK
    • Ahn S., Park H. XIAP is essential for shear stress-enhanced Tyr-576 phosphorylation of FAK. Biochem. Biophys. Res. Commun. 2010, 399:256-261.
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , pp. 256-261
    • Ahn, S.1    Park, H.2
  • 6
    • 0036798144 scopus 로고    scopus 로고
    • Staurosporine induces endothelial cell apoptosis via focal adhesion kinase dephosphorylation and focal adhesion disassembly independent of focal adhesion kinase proteolysis
    • Kabir J., Lobo M., Zachary I. Staurosporine induces endothelial cell apoptosis via focal adhesion kinase dephosphorylation and focal adhesion disassembly independent of focal adhesion kinase proteolysis. Biochem. J. 2002, 367:145-155.
    • (2002) Biochem. J. , vol.367 , pp. 145-155
    • Kabir, J.1    Lobo, M.2    Zachary, I.3
  • 7
    • 77956626576 scopus 로고    scopus 로고
    • Focal adhesion kinase and p53 signal transduction pathways in cancer
    • Golubovskaya V.M., Cance W. Focal adhesion kinase and p53 signal transduction pathways in cancer. Front Biosci. 2010, 15:901-912.
    • (2010) Front Biosci. , vol.15 , pp. 901-912
    • Golubovskaya, V.M.1    Cance, W.2
  • 8
    • 38149070791 scopus 로고    scopus 로고
    • Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation
    • Lim S.T., Chen X.L., Lim Y., et al. Nuclear FAK promotes cell proliferation and survival through FERM-enhanced p53 degradation. Mol. Cell 2008, 29:9-22.
    • (2008) Mol. Cell , vol.29 , pp. 9-22
    • Lim, S.T.1    Chen, X.L.2    Lim, Y.3
  • 9
    • 0032536543 scopus 로고    scopus 로고
    • FAK and disassembly of focal adhesions in human endothelial cell apoptosis
    • FAK and disassembly of focal adhesions in human endothelial cell apoptosis. J. Exp. Med. 1998, 187(4):579-586.
    • (1998) J. Exp. Med. , vol.187 , Issue.4 , pp. 579-586
    • Levkau, B.1    Herren, B.2    Koyam, H.3
  • 10
    • 77955454919 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein controls integrin alpha5-mediated cell adhesion and migration
    • Kim J., Ahn S., Ko Y.G., et al. X-linked inhibitor of apoptosis protein controls integrin alpha5-mediated cell adhesion and migration. Am. J. Physiol. Heart Circ. Physiol. 2010, 299:H300-H309.
    • (2010) Am. J. Physiol. Heart Circ. Physiol. , vol.299
    • Kim, J.1    Ahn, S.2    Ko, Y.G.3
  • 11
    • 0034644712 scopus 로고    scopus 로고
    • XIAP regulates DNA damage-induced apoptosis downstream of caspase-9 cleavage
    • Datta R., Oki E., Endo K., et al. XIAP regulates DNA damage-induced apoptosis downstream of caspase-9 cleavage. J. Biol. Chem. 2000, 275:31733-31738.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31733-31738
    • Datta, R.1    Oki, E.2    Endo, K.3
  • 12
    • 42549170543 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein is an important regulator of vascular endothelial growth factor-dependent bovine aortic endothelial cell survival
    • Kim J., Park J., Choi S., et al. X-linked inhibitor of apoptosis protein is an important regulator of vascular endothelial growth factor-dependent bovine aortic endothelial cell survival. Circ. Res. 2008, 102:896-904.
    • (2008) Circ. Res. , vol.102 , pp. 896-904
    • Kim, J.1    Park, J.2    Choi, S.3
  • 13
    • 46749116365 scopus 로고    scopus 로고
    • Resveratrol stimulates nitric oxide production by increasing estrogen receptor α-Src-caveolin-1 interaction and phosphorylation in human umbilical vein endothelial cells
    • Klinge C.M., Wickramasinghe N.S., Ivanova M.M., et al. Resveratrol stimulates nitric oxide production by increasing estrogen receptor α-Src-caveolin-1 interaction and phosphorylation in human umbilical vein endothelial cells. FASEB J. 2008, 22(7):2185-2197.
    • (2008) FASEB J. , vol.22 , Issue.7 , pp. 2185-2197
    • Klinge, C.M.1    Wickramasinghe, N.S.2    Ivanova, M.M.3
  • 14
    • 0034610067 scopus 로고    scopus 로고
    • Nuclear localization and apoptotic regulation of an amino-terminal domain focal adhesion kinase fragment in endothelial cells
    • Lobo M., Zachary I. Nuclear localization and apoptotic regulation of an amino-terminal domain focal adhesion kinase fragment in endothelial cells. Biochem. Biophys. Res. Commun. 2000, 276:1068-1074.
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 1068-1074
    • Lobo, M.1    Zachary, I.2
  • 15
    • 79955677125 scopus 로고    scopus 로고
    • The reduction of water-soluble tetrazolium salt reagent on the plasma membrane of epidermal keratinocytes is oxygen dependent
    • Weir L., Robertson D., Leigh I.M., et al. The reduction of water-soluble tetrazolium salt reagent on the plasma membrane of epidermal keratinocytes is oxygen dependent. Anal. Biochem. 2011, 411:31-37.
    • (2011) Anal. Biochem. , vol.411 , pp. 31-37
    • Weir, L.1    Robertson, D.2    Leigh, I.M.3
  • 16
    • 84862829624 scopus 로고    scopus 로고
    • XIAP reverses various functional activities of FRNK in endothelial cells
    • Ahn S., Kim H.J., Chi S.G., et al. XIAP reverses various functional activities of FRNK in endothelial cells. Biochem. Biophys. Res. Commun. 2012, 419(2):419-424.
    • (2012) Biochem. Biophys. Res. Commun. , vol.419 , Issue.2 , pp. 419-424
    • Ahn, S.1    Kim, H.J.2    Chi, S.G.3
  • 17
    • 84861517212 scopus 로고    scopus 로고
    • Tumor necrosis factor α decreases nitric oxide synthase Type 3 expression primarily via Rho/Rho kinase in the thick ascending limb
    • Ramseyer V.D., Hong N.J., Garvin J.L. Tumor necrosis factor α decreases nitric oxide synthase Type 3 expression primarily via Rho/Rho kinase in the thick ascending limb. Hypertension 2012, 59(6):1145-1150.
    • (2012) Hypertension , vol.59 , Issue.6 , pp. 1145-1150
    • Ramseyer, V.D.1    Hong, N.J.2    Garvin, J.L.3
  • 18
    • 34547912897 scopus 로고    scopus 로고
    • Tumor necrosis factor-α reduces argininosuccinate synthase expression and nitric oxide production in aortic endothelial cells
    • Goodwin B.L., Pendleton L.C., Levy M.M., et al. Tumor necrosis factor-α reduces argininosuccinate synthase expression and nitric oxide production in aortic endothelial cells. Am. J. Physiol. Heart Circ. Physiol. 2007, 293:H1115-H1121.
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.293
    • Goodwin, B.L.1    Pendleton, L.C.2    Levy, M.M.3
  • 19
    • 69249216358 scopus 로고    scopus 로고
    • Resveratrol prevents hyperglycemia-induced endothelial dysfunction via activation of adenosine monophosphate-activated protein kinase
    • Xu Q., Hao X., Yang Q., et al. Resveratrol prevents hyperglycemia-induced endothelial dysfunction via activation of adenosine monophosphate-activated protein kinase. Biochem. Biophys. Res. Commun. 2009, 388:389-394.
    • (2009) Biochem. Biophys. Res. Commun. , vol.388 , pp. 389-394
    • Xu, Q.1    Hao, X.2    Yang, Q.3
  • 20
    • 0034905394 scopus 로고    scopus 로고
    • XIAP: apoptotic brake and promising therapeutic target
    • Holcik M., Gibson H., Korneluk R.G. XIAP: apoptotic brake and promising therapeutic target. Apoptosis 2001, 6(4):253-261.
    • (2001) Apoptosis , vol.6 , Issue.4 , pp. 253-261
    • Holcik, M.1    Gibson, H.2    Korneluk, R.G.3
  • 21
    • 44349136151 scopus 로고    scopus 로고
    • Cardiac developmental defects and eccentric right ventricular hypertrophy in cardiomyocyte focal adhesion kinase (FAK) conditional knockout mice
    • Peng X., Wu X., Druso J.E., et al. Cardiac developmental defects and eccentric right ventricular hypertrophy in cardiomyocyte focal adhesion kinase (FAK) conditional knockout mice. Proc. Natl. Acad. Sci. USA 2009, 105:6638-6643.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6638-6643
    • Peng, X.1    Wu, X.2    Druso, J.E.3
  • 22
    • 0030669961 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates
    • Tachibana K., Urano T., Fujita H., et al. Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates. J. Biol. Chem. 1997, 272:29083-29090.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29083-29090
    • Tachibana, K.1    Urano, T.2    Fujita, H.3
  • 23
    • 0028986116 scopus 로고
    • Pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • Schaller M.D., Parsons J.T. Pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol. Cell Biol. 1992, 15:2635-2645.
    • (1992) Mol. Cell Biol. , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 24
    • 82955207200 scopus 로고    scopus 로고
    • Cross talk between focal adhesion kinase and cadherins: role in regulating endothelial barrier function
    • Quadri S.K. Cross talk between focal adhesion kinase and cadherins: role in regulating endothelial barrier function. Microvasc. Res. 2012, 83:3-11.
    • (2012) Microvasc. Res. , vol.83 , pp. 3-11
    • Quadri, S.K.1
  • 25
    • 0035003136 scopus 로고    scopus 로고
    • Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain
    • Chen R., Kim O., Li M., et al. Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain. Nat. Cell Biol. 2001, 3(5):439-444.
    • (2001) Nat. Cell Biol. , vol.3 , Issue.5 , pp. 439-444
    • Chen, R.1    Kim, O.2    Li, M.3
  • 26
    • 84863753056 scopus 로고    scopus 로고
    • Nuclear-localized focal adhesion kinase regulates inflammatory VCAM-1 expression
    • Lim S.T., Miller N.L.G., Chen X.L., et al. Nuclear-localized focal adhesion kinase regulates inflammatory VCAM-1 expression. J. Cell Biol. 2012, 197(7):907-919.
    • (2012) J. Cell Biol. , vol.197 , Issue.7 , pp. 907-919
    • Lim, S.T.1    Miller, N.L.G.2    Chen, X.L.3
  • 27
    • 48849089827 scopus 로고    scopus 로고
    • FERM control of FAK function: implications for cancer therapy
    • Lim S.T., Mikolon D., Stupack D.G., et al. FERM control of FAK function: implications for cancer therapy. Cell Cycle 2008, 7(15):2306-2314.
    • (2008) Cell Cycle , vol.7 , Issue.15 , pp. 2306-2314
    • Lim, S.T.1    Mikolon, D.2    Stupack, D.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.