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Volumn 288, Issue 28, 2013, Pages 20581-20591

AMP-dependent kinase inhibits oxidative stress-induced caveolin-1 phosphorylation and endocytosis by suppressing the dissociation between c-Abl and Prdx1 proteins in endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

CO-IMMUNOPRECIPITATION EXPERIMENTS; HUMAN UMBILICAL VEIN ENDOTHELIAL CELLS; PHARMACOLOGICAL ACTIVATOR; REGULATORY MECHANISM; SCAFFOLDING PROTEINS; SIGNALING MOLECULES; SPECIFIC INHIBITORS; STRUCTURAL COMPONENT;

EID: 84880057785     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.460832     Document Type: Article
Times cited : (40)

References (52)
  • 1
    • 33644839612 scopus 로고    scopus 로고
    • Signaling mechanisms regulating endothelial permeability
    • Mehta, D., and Malik, A. B. (2006) Signaling mechanisms regulating endothelial permeability. Physiol. Rev. 86, 279-367
    • (2006) Physiol. Rev. , vol.86 , pp. 279-367
    • Mehta, D.1    Malik, A.B.2
  • 2
    • 80054763779 scopus 로고    scopus 로고
    • Role of caveolin-1 in the regulation of pulmonary endothelial permeability
    • Sun, Y., Minshall, R. D., and Hu, G. (2011) Role of caveolin-1 in the regulation of pulmonary endothelial permeability. Methods Mol. Biol. 763, 303-317
    • (2011) Methods Mol. Biol. , vol.763 , pp. 303-317
    • Sun, Y.1    Minshall, R.D.2    Hu, G.3
  • 4
    • 77951697920 scopus 로고    scopus 로고
    • Regulation of endothelial permeability via paracellular and transcellular transport pathways
    • Komarova, Y., and Malik, A. B. (2010) Regulation of endothelial permeability via paracellular and transcellular transport pathways. Annu. Rev. Physiol. 72, 463-493
    • (2010) Annu. Rev. Physiol. , vol.72 , pp. 463-493
    • Komarova, Y.1    Malik, A.B.2
  • 7
    • 59849114434 scopus 로고    scopus 로고
    • Regulation of transendothelial permeability by Src kinase
    • Hu, G., and Minshall, R. D. (2009) Regulation of transendothelial permeability by Src kinase. Microvasc. Res. 77, 21-25
    • (2009) Microvasc. Res. , vol.77 , pp. 21-25
    • Hu, G.1    Minshall, R.D.2
  • 8
    • 0035542970 scopus 로고    scopus 로고
    • AMP-activated protein kinase. The energy charge hypothesis revisited
    • Hardie, D. G., and Hawley, S. A. (2001) AMP-activated protein kinase. The energy charge hypothesis revisited. Bioessays 23, 1112-1119
    • (2001) Bioessays , vol.23 , pp. 1112-1119
    • Hardie, D.G.1    Hawley, S.A.2
  • 10
    • 63849104290 scopus 로고    scopus 로고
    • AMP-activated protein kinase and cancer
    • Wang, W., and Guan, K. L. (2009) AMP-activated protein kinase and cancer. Acta Physiol (Oxf) 196, 55-63
    • (2009) Acta Physiol (Oxf) , vol.196 , pp. 55-63
    • Wang, W.1    Guan, K.L.2
  • 11
    • 77955818623 scopus 로고    scopus 로고
    • Retinoblastoma cells are inhibited by aminoimidazole carboxamide ribonucleotide (AICAR) partially through activation of AMP-dependent kinase
    • Theodoropoulou, S., Kolovou, P. E., Morizane, Y., Kayama, M., Nicolaou, F., Miller, J. W., Gragoudas, E., Ksander, B. R., and Vavvas, D. G. (2010) Retinoblastoma cells are inhibited by aminoimidazole carboxamide ribonucleotide (AICAR) partially through activation of AMP-dependent kinase. FASEB J. 24, 2620-2630
    • (2010) FASEB J. , vol.24 , pp. 2620-2630
    • Theodoropoulou, S.1    Kolovou, P.E.2    Morizane, Y.3    Kayama, M.4    Nicolaou, F.5    Miller, J.W.6    Gragoudas, E.7    Ksander, B.R.8    Vavvas, D.G.9
  • 12
    • 84871902020 scopus 로고    scopus 로고
    • Aminoimidazole carboxamide ribonucleotide (AICAR) inhibits the growth of retinoblastoma in vivo by decreasing angiogenesis and inducing apoptosis
    • Theodoropoulou, S., Brodowska, K., Kayama, M., Morizane, Y., Miller, J. W., Gragoudas, E. S., and Vavvas, D. G. (2013) Aminoimidazole carboxamide ribonucleotide (AICAR) inhibits the growth of retinoblastoma in vivo by decreasing angiogenesis and inducing apoptosis. PLoS ONE 8, e52852
    • (2013) PLoS ONE , vol.8
    • Theodoropoulou, S.1    Brodowska, K.2    Kayama, M.3    Morizane, Y.4    Miller, J.W.5    Gragoudas, E.S.6    Vavvas, D.G.7
  • 16
    • 80053927985 scopus 로고    scopus 로고
    • Adenosine monophosphate-activated kinase α1 promotes endothelial barrier repair
    • Creighton, J., Jian, M., Sayner, S., Alexeyev, M., and Insel, P. A. (2011) Adenosine monophosphate-activated kinase α1 promotes endothelial barrier repair. FASEB J. 25, 3356-3365
    • (2011) FASEB J. , vol.25 , pp. 3356-3365
    • Creighton, J.1    Jian, M.2    Sayner, S.3    Alexeyev, M.4    Insel, P.A.5
  • 17
    • 0035896560 scopus 로고    scopus 로고
    • Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr-14) via activation of p38 mitogen-activated protein kinase and c-Src kinase. Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress
    • Volonté, D., Galbiati, F., Pestell, R. G., and Lisanti, M. P. (2001) Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr-14) via activation of p38 mitogen-activated protein kinase and c-Src kinase. Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress. J. Biol. Chem. 276, 8094-8103
    • (2001) J. Biol. Chem. , vol.276 , pp. 8094-8103
    • Volonté, D.1    Galbiati, F.2    Pestell, R.G.3    Lisanti, M.P.4
  • 18
    • 0033573098 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of caveolin-1 in the endothelium
    • DOI 10.1006/excr.1999.4652
    • Aoki, T., Nomura, R., and Fujimoto, T. (1999) Tyrosine phosphorylation of caveolin-1 in the endothelium. Exp. Cell Res. 253, 629-636 (Pubitemid 30003124)
    • (1999) Experimental Cell Research , vol.253 , Issue.2 , pp. 629-636
    • Aoki, T.1    Nomura, R.2    Fujimoto, T.3
  • 19
    • 0037341849 scopus 로고    scopus 로고
    • C-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14
    • DOI 10.1016/S0898-6568(02)00090-6, PII S0898656802000906
    • Sanguinetti, A. R., and Mastick, C. C. (2003) c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14. Cell. Signal. 15, 289-298 (Pubitemid 36071673)
    • (2003) Cellular Signalling , vol.15 , Issue.3 , pp. 289-298
    • Sanguinetti, A.R.1    Mastick, C.C.2
  • 20
    • 70349705635 scopus 로고    scopus 로고
    • Phosphorylation of caveolin-1 regulates oxidant-induced pulmonary vascular permeability via paracellular and transcellular pathways
    • Sun, Y., Hu, G., Zhang, X., and Minshall, R. D. (2009) Phosphorylation of caveolin-1 regulates oxidant-induced pulmonary vascular permeability via paracellular and transcellular pathways. Circ. Res. 105, 676-685
    • (2009) Circ. Res. , vol.105 , pp. 676-685
    • Sun, Y.1    Hu, G.2    Zhang, X.3    Minshall, R.D.4
  • 21
    • 33745218224 scopus 로고    scopus 로고
    • 5-Aminoimidazole-4-carboxamide-1-β-D-ribofuranoside and metformin inhibit hepatic glucose phosphorylation by an AMP-activated protein kinase - Independent effect on glucokinase translocation
    • DOI 10.2337/diabetes.55.04.06.db05-1178
    • Guigas, B., Bertrand, L., Taleux, N., Foretz, M., Wiernsperger, N., Vertommen, D., Andreelli, F., Viollet, B., and Hue, L. (2006) 5-Aminoimidazole- 4-carboxamide-1-β-D-ribofuranoside and metformin inhibit hepatic glucose phosphorylation by an AMP-activated protein kinase-independent effect on glucokinase translocation. Diabetes 55, 865-874 (Pubitemid 44100158)
    • (2006) Diabetes , vol.55 , Issue.4 , pp. 865-874
    • Guigas, B.1    Bertrand, L.2    Taleux, N.3    Foretz, M.4    Wiernsperger, N.5    Vertommen, D.6    Andreelli, F.7    Viollet, B.8    Hue, L.9
  • 22
    • 34250751754 scopus 로고    scopus 로고
    • AMP-activated protein kinase-independent inhibition of hepatic mitochondrial oxidative phosphorylation by AICA riboside
    • DOI 10.1042/BJ20070105
    • Guigas, B., Taleux, N., Foretz, M., Detaille, D., Andreelli, F., Viollet, B., and Hue, L. (2007) AMP-activated protein kinase-independent inhibition of hepatic mitochondrial oxidative phosphorylation by AICA riboside. Biochem. J. 404, 499-507 (Pubitemid 46953924)
    • (2007) Biochemical Journal , vol.404 , Issue.3 , pp. 499-507
    • Guigas, B.1    Taleux, N.2    Foretz, M.3    Detaille, D.4    Andreelli, F.5    Viollet, B.6    Hue, L.7
  • 25
    • 55949132861 scopus 로고    scopus 로고
    • AMP-activated protein kinase. Structure and regulation
    • Sanz, P. (2008) AMP-activated protein kinase. Structure and regulation. Curr. Protein Pept. Sci. 9, 478-492
    • (2008) Curr. Protein Pept. Sci. , vol.9 , pp. 478-492
    • Sanz, P.1
  • 26
    • 61549138378 scopus 로고    scopus 로고
    • Imatinib and its successors. How modern chemistry has changed drug development
    • Müller, B. A. (2009) Imatinib and its successors. How modern chemistry has changed drug development. Curr. Pharm. Des. 15, 120-133
    • (2009) Curr. Pharm. Des. , vol.15 , pp. 120-133
    • Müller, B.A.1
  • 27
    • 58149398623 scopus 로고    scopus 로고
    • Translation of the Philadelphia chromosome into therapy for CML
    • Druker, B. J. (2008) Translation of the Philadelphia chromosome into therapy for CML. Blood 112, 4808-4817
    • (2008) Blood , vol.112 , pp. 4808-4817
    • Druker, B.J.1
  • 28
    • 0030803669 scopus 로고    scopus 로고
    • The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity
    • Wen, S. T., and Van Etten, R. A. (1997) The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity. Genes Dev. 11, 2456-2467
    • (1997) Genes Dev. , vol.11 , pp. 2456-2467
    • Wen, S.T.1    Van Etten, R.A.2
  • 29
    • 0345647078 scopus 로고    scopus 로고
    • The pag gene product, a physiological inhibitor of c-abl tyrosine kinase, is overexpressed in cells entering S phase and by contact with agents inducing oxidative stress
    • DOI 10.1016/S0014-5793(98)00057-X, PII S001457939800057X
    • Prospéri, M. T., Ferbus, D., Rouillard, D., and Goubin, G. (1998) The pag gene product, a physiological inhibitor of c-abl tyrosine kinase, is overexpressed in cells entering S phase and by contact with agents inducing oxidative stress. FEBS Lett. 423, 39-44 (Pubitemid 28098575)
    • (1998) FEBS Letters , vol.423 , Issue.1 , pp. 39-44
    • Prosperi, M.-T.1    Ferbus, D.2    Rouillard, D.3    Goubin, G.4
  • 31
    • 34247525991 scopus 로고    scopus 로고
    • Detection of transient protein-protein interactions by bimolecular fluorescence complementation: The Abl-SH3 case
    • DOI 10.1002/pmic.200600966
    • Morell, M., Espargaró, A., Avilés, F. X., and Ventura, S. (2007) Detection of transient protein-protein interactions by bimolecular fluorescence complementation. The Abl-SH3 case. Proteomics 7, 1023-1036 (Pubitemid 46649152)
    • (2007) Proteomics , vol.7 , Issue.7 , pp. 1023-1036
    • Morell, M.1    Espargaro, A.2    Aviles, F.X.3    Ventura, S.4
  • 32
    • 0037085384 scopus 로고    scopus 로고
    • Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress
    • DOI 10.1074/jbc.M106846200
    • Wong, C. M., Zhou, Y., Ng, R. W., Kung Hf, H. F., and Jin, D. Y. (2002) Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress. J. Biol. Chem. 277, 5385-5394 (Pubitemid 34968585)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 5385-5394
    • Wong, C.-M.1    Zhou, Y.2    Ng, R.W.M.3    Kung, H.-F.4    Jin, D.-Y.5
  • 33
    • 34547124878 scopus 로고    scopus 로고
    • Agonist-modulated regulation of AMP-activated protein kinase (AMPK) in endothelial cells: Evidence for an AMPK 3 Rac1 3 Akt 3 endothelial nitric-oxide synthase pathway
    • DOI 10.1074/jbc.M702182200
    • Levine, Y. C., Li, G. K., and Michel, T. (2007) Agonist-modulated regulation of AMP-activated protein kinase (AMPK) in endothelial cells. Evidence for an AMPK 3 Rac1 3 Akt 3 endothelial nitric-oxide synthase pathway. J. Biol. Chem. 282, 20351-20364 (Pubitemid 47100039)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.28 , pp. 20351-20364
    • Levine, Y.C.1    Li, G.K.2    Michel, T.3
  • 34
    • 84873274096 scopus 로고    scopus 로고
    • Wogonin inhibits H2O2-induced vascular permeability through suppressing the phosphorylation of caveolin-1
    • Wang, F., Song, X., Zhou, M., Wei, L., Dai, Q., Li, Z., Lu, N., and Guo, Q. (2013) Wogonin inhibits H2O2-induced vascular permeability through suppressing the phosphorylation of caveolin-1. Toxicology 305, 10-19
    • (2013) Toxicology , vol.305 , pp. 10-19
    • Wang, F.1    Song, X.2    Zhou, M.3    Wei, L.4    Dai, Q.5    Li, Z.6    Lu, N.7    Guo, Q.8
  • 36
    • 0026454933 scopus 로고
    • Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts
    • Glenney, J. R., Jr., and Soppet, D. (1992) Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts. Proc. Natl. Acad. Sci. U.S.A. 89, 10517-10521
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10517-10521
    • Glenney Jr., J.R.1    Soppet, D.2
  • 37
  • 38
    • 77957745942 scopus 로고    scopus 로고
    • Caveolae and caveolin-1 mediate endocytosis and transcytosis of oxidized low density lipoprotein in endothelial cells
    • Sun, S. W., Zu, X. Y., Tuo, Q. H., Chen, L. X., Lei, X. Y., Li, K., Tang, C. K., and Liao, D. F. (2010) Caveolae and caveolin-1 mediate endocytosis and transcytosis of oxidized low density lipoprotein in endothelial cells. Acta Pharmacol. Sin. 31, 1336-1342
    • (2010) Acta Pharmacol. Sin. , vol.31 , pp. 1336-1342
    • Sun, S.W.1    Zu, X.Y.2    Tuo, Q.H.3    Chen, L.X.4    Lei, X.Y.5    Li, K.6    Tang, C.K.7    Liao, D.F.8
  • 39
    • 0037309894 scopus 로고    scopus 로고
    • Abrogation of the cell death response to oxidative stress by the c-Abl tyrosine kinase inhibitor STI571
    • DOI 10.1124/mol.63.2.276
    • Kumar, S., Mishra, N., Raina, D., Saxena, S., and Kufe, D. (2003) Abrogation of the cell death response to oxidative stress by the c-Abl tyrosine kinase inhibitor STI571. Mol. Pharmacol. 63, 276-282 (Pubitemid 36158362)
    • (2003) Molecular Pharmacology , vol.63 , Issue.2 , pp. 276-282
    • Kumar, S.1    Mishra, N.2    Raina, D.3    Saxena, S.4    Kufe, D.5
  • 40
    • 0037088672 scopus 로고    scopus 로고
    • A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14. Recruitment of C-terminal Src kinase
    • DOI 10.1074/jbc.C100661200
    • Cao, H., Courchesne, W. E., and Mastick, C. C. (2002) A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14. Recruitment of C-terminal Src kinase. J. Biol. Chem. 277, 8771-8774 (Pubitemid 34952941)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.11 , pp. 8771-8774
    • Cao, H.1    Courchesne, W.E.2    Mastick, C.C.3
  • 42
    • 74249096153 scopus 로고    scopus 로고
    • Adiponectin directly improves endothelial dysfunction in obese rats through the AMPK-eNOS Pathway
    • Deng, G., Long, Y., Yu, Y. R., and Li, M. R. (2010) Adiponectin directly improves endothelial dysfunction in obese rats through the AMPK-eNOS Pathway. Int. J. Obes. (Lond.) 34, 165-171
    • (2010) Int. J. Obes. (Lond.) , vol.34 , pp. 165-171
    • Deng, G.1    Long, Y.2    Yu, Y.R.3    Li, M.R.4
  • 44
    • 33751220209 scopus 로고    scopus 로고
    • Imatinib mesylate (Gleevec) protects against streptozotocin-induced diabetes and islet cell death in vitro
    • DOI 10.1016/j.cellbi.2006.08.006, PII S1065699506001880
    • Hägerkvist, R., Makeeva, N., Elliman, S., and Welsh, N. (2006) Imatinib mesylate (Gleevec) protects against streptozotocin-induced diabetes and islet cell death in vitro. Cell Biol. Int. 30, 1013-1017 (Pubitemid 44781307)
    • (2006) Cell Biology International , vol.30 , Issue.12 , pp. 1013-1017
    • Hagerkvist, R.1    Makeeva, N.2    Elliman, S.3    Welsh, N.4
  • 45
    • 33846842100 scopus 로고    scopus 로고
    • Amelioration of diabetes by imatinib mesylate (Gleevec): Role of β-cell NF-κB activation and anti-apoptotic preconditioning
    • DOI 10.1096/fj.06-6910com
    • Hägerkvist, R., Sandler, S., Mokhtari, D., and Welsh, N. (2007) Amelioration of diabetes by imatinib mesylate (Gleevec). Role of β-cell NF-κB activation and anti-apoptotic preconditioning. FASEB J. 21, 618-628 (Pubitemid 46213508)
    • (2007) FASEB Journal , vol.21 , Issue.2 , pp. 618-628
    • Hagerkvist, R.1    Sandler, S.2    Mokhtari, D.3    Welsh, N.4
  • 47
    • 84857826929 scopus 로고    scopus 로고
    • AMP-activated protein kinase pathway and bone metabolism
    • Jeyabalan, J., Shah, M., Viollet, B., and Chenu, C. (2012) AMP-activated protein kinase pathway and bone metabolism. J. Endocrinol. 212, 277-290
    • (2012) J. Endocrinol. , vol.212 , pp. 277-290
    • Jeyabalan, J.1    Shah, M.2    Viollet, B.3    Chenu, C.4
  • 50
    • 79958078455 scopus 로고    scopus 로고
    • Nitric oxide-induced activation of the AMP-activated protein kinase α2 subunit attenuates IκB kinase activity and inflammatory responses in endothelial cells
    • Bess, E., Fisslthaler, B., Frömel, T., and Fleming, I. (2011) Nitric oxide-induced activation of the AMP-activated protein kinase α2 subunit attenuates IκB kinase activity and inflammatory responses in endothelial cells. PLoS ONE 6, e20848
    • (2011) PLoS ONE , vol.6
    • Bess, E.1    Fisslthaler, B.2    Frömel, T.3    Fleming, I.4
  • 51
    • 84874544167 scopus 로고    scopus 로고
    • Inhibition of AMP-activated protein kinase accentuates lipopolysaccharide-induced lung endothelial barrier dysfunction and lung injury in vivo
    • Xing, J., Wang, Q., Coughlan, K., Viollet, B., Moriasi, C., and Zou, M. H. (2013) Inhibition of AMP-activated protein kinase accentuates lipopolysaccharide-induced lung endothelial barrier dysfunction and lung injury in vivo. Am. J. Pathol. 182, 1021-1030
    • (2013) Am. J. Pathol. , vol.182 , pp. 1021-1030
    • Xing, J.1    Wang, Q.2    Coughlan, K.3    Viollet, B.4    Moriasi, C.5    Zou, M.H.6
  • 52
    • 0035282062 scopus 로고    scopus 로고
    • Post-translational modifications of the β-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization
    • Warden, S. M., Richardson, C., O'Donnell, J., Jr., Stapleton, D., Kemp, B. E., and Witters, L. A. (2001) Post-translational modifications of the β-1 subunit of AMP-activated protein kinase affect enzyme activity and cellular localization. Biochem. J. 354, 275-283
    • (2001) Biochem. J. , vol.354 , pp. 275-283
    • Warden, S.M.1    Richardson, C.2    O'Donnell Jr., J.3    Stapleton, D.4    Kemp, B.E.5    Witters, L.A.6


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