메뉴 건너뛰기




Volumn 1803, Issue 7, 2010, Pages 872-880

Gp-91 mediates histone deacetylase inhibition-induced cardioprotection

Author keywords

Gp 91; Histone deacetylase; Ischemia; Myocardial infarction; NADPH oxidase

Indexed keywords

CASPASE 3; GLYCOPROTEIN GP 91; HISTONE DEACETYLASE; REACTIVE OXYGEN METABOLITE; SMALL INTERFERING RNA; TRICHOSTATIN A;

EID: 77953363510     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2010.04.007     Document Type: Article
Times cited : (28)

References (46)
  • 1
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P., Allis C.D., Sassone-Corsi P. Signaling to chromatin through histone modifications. Cell 2000, 103:263-267.
    • (2000) Cell , vol.103 , pp. 263-267
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 2
    • 0032558998 scopus 로고    scopus 로고
    • Structure and function of the core histone N-termini: more than meets the eye
    • Hansen J.C., Tse C., Wolffe A.P. Structure and function of the core histone N-termini: more than meets the eye. Biochemistry 1998, 37:17637-17641.
    • (1998) Biochemistry , vol.37 , pp. 17637-17641
    • Hansen, J.C.1    Tse, C.2    Wolffe, A.P.3
  • 3
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8A resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8A resolution. Nature 1997, 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 4
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., Allis C.D. The language of covalent histone modifications. Nature 2000, 403:41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 5
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner B.M. Histone acetylation and an epigenetic code. Bioessays 2000, 22:836-845.
    • (2000) Bioessays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 7
    • 0037406061 scopus 로고    scopus 로고
    • Class II histone deacetylases: versatile regulators
    • Verdin E., Dequiedt F., Kasler H.G. Class II histone deacetylases: versatile regulators. Trends Genet. 2003, 19:286-293.
    • (2003) Trends Genet. , vol.19 , pp. 286-293
    • Verdin, E.1    Dequiedt, F.2    Kasler, H.G.3
  • 9
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • Grozinger C.M., Hassig C.A., Schreiber S.L. Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc. Natl Acad. Sci. USA 1999, 96:4868-4873.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 11
    • 1542514783 scopus 로고    scopus 로고
    • Targeted histone deacetylase inhibition for cancer therapy
    • Vigushi D.M., Coombes R.C. Targeted histone deacetylase inhibition for cancer therapy. Curr. Cancer Target 2004, 4:205-218.
    • (2004) Curr. Cancer Target , vol.4 , pp. 205-218
    • Vigushi, D.M.1    Coombes, R.C.2
  • 12
    • 35548942629 scopus 로고    scopus 로고
    • Inhibition of histone deacetylases triggers pharmacologic preconditioning effects against myocardial ischemic injury
    • Zhao T.C., Cheng G., Zhang L.X., Tseng Y.T., Padbury J.F. Inhibition of histone deacetylases triggers pharmacologic preconditioning effects against myocardial ischemic injury. Cardiovasc. Res. 2007, 76:473-481.
    • (2007) Cardiovasc. Res. , vol.76 , pp. 473-481
    • Zhao, T.C.1    Cheng, G.2    Zhang, L.X.3    Tseng, Y.T.4    Padbury, J.F.5
  • 15
    • 33745173485 scopus 로고    scopus 로고
    • Suppression of class I and II histone deacetylases blunts pressure-overload cardiac hypertrophy
    • Kong Y., Tannous P., Lu G., Berenji K., Rothermel B.A., Olson E.N., Hill J.A. Suppression of class I and II histone deacetylases blunts pressure-overload cardiac hypertrophy. Circulation 2006, 113:2579-2588.
    • (2006) Circulation , vol.113 , pp. 2579-2588
    • Kong, Y.1    Tannous, P.2    Lu, G.3    Berenji, K.4    Rothermel, B.A.5    Olson, E.N.6    Hill, J.A.7
  • 16
    • 3042651448 scopus 로고    scopus 로고
    • Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: potential roles of histone deacetylase inhibition and heat shock protein induction
    • Ren M., Leng Y., Jeong M., Leeds P.R., Chuang D.M. Valproic acid reduces brain damage induced by transient focal cerebral ischemia in rats: potential roles of histone deacetylase inhibition and heat shock protein induction. J. Neurochem. 2004, 89:1358-1367.
    • (2004) J. Neurochem. , vol.89 , pp. 1358-1367
    • Ren, M.1    Leng, Y.2    Jeong, M.3    Leeds, P.R.4    Chuang, D.M.5
  • 17
    • 0002626215 scopus 로고    scopus 로고
    • Lippincott, Wilkins, Philadelphia, J.I. Gallin, R. Snyderman (Eds.)
    • Leto T.L. Inflammation Basic and Clinical Correlates 1999, 769-787. Lippincott, Wilkins, Philadelphia. J.I. Gallin, R. Snyderman (Eds.).
    • (1999) Inflammation Basic and Clinical Correlates , pp. 769-787
    • Leto, T.L.1
  • 18
    • 0033230607 scopus 로고    scopus 로고
    • Role of redox potential and reactive oxygen species in stress signaling
    • dler V., Yin Z., Tew K.D., Ronai Z. Role of redox potential and reactive oxygen species in stress signaling. Oncogene 1999, 18:6104-6111.
    • (1999) Oncogene , vol.18 , pp. 6104-6111
    • dler, V.1    Yin, Z.2    Tew, K.D.3    Ronai, Z.4
  • 19
    • 0033568576 scopus 로고    scopus 로고
    • Regulation of the erythropoietin gene
    • Ebert B.L., Bunn H.F. Regulation of the erythropoietin gene. Blood 1999, 94:1864-1877.
    • (1999) Blood , vol.94 , pp. 1864-1877
    • Ebert, B.L.1    Bunn, H.F.2
  • 20
    • 24444437757 scopus 로고    scopus 로고
    • 3 receptor induced delayed cardioprotection in mouse heart: essential role of gp91 subunit of NADPH oxidase
    • 3 receptor induced delayed cardioprotection in mouse heart: essential role of gp91 subunit of NADPH oxidase. Circulation 2002, 106(Supplement II):II-314.
    • (2002) Circulation , vol.106 , Issue.SUPPL. 2
    • Zhao, T.C.1    Kukreja, R.C.2
  • 21
    • 0034617071 scopus 로고    scopus 로고
    • phox-containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall
    • phox-containing NADPH oxidase selectively expressed in endothelial cells is a major source of oxygen radical generation in the arterial wall. Circ. Res. 2000, 87:26-32.
    • (2000) Circ. Res. , vol.87 , pp. 26-32
    • Gorlach, A.1    Brandes, R.P.2    Nguyen, K.3    Amidi, M.4    Dehghani, F.5    Busse, R.6
  • 22
    • 0033897196 scopus 로고    scopus 로고
    • Molecular characterization and localization of the NAD(P)H oxidase components gp91-phox and p22-phox in endothelial cells
    • Bayraktutan U., Blayney L., Shah A.M. Molecular characterization and localization of the NAD(P)H oxidase components gp91-phox and p22-phox in endothelial cells. Arterioscler. Thromb. Vasc. Biol. 2000, 20:1903-1911.
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 1903-1911
    • Bayraktutan, U.1    Blayney, L.2    Shah, A.M.3
  • 23
    • 0029661428 scopus 로고    scopus 로고
    • phox Is a critical component of the superoxide-generating NADH/NADPH oxidase system and regulates angiotensin II-induced hypertrophy in vascular smooth muscle cells
    • phox Is a critical component of the superoxide-generating NADH/NADPH oxidase system and regulates angiotensin II-induced hypertrophy in vascular smooth muscle cells. J. Biol. Chem. 1996, 271:23317-23321.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23317-23321
    • Ushio-Fukai, M.1    Zafari, A.M.2    Fukui, T.3    Ishizaka, N.4    Griendling, K.K.5
  • 24
    • 0029665121 scopus 로고    scopus 로고
    • phox cDNA and functional analysis in a human X-linked chronic granulomatous disease cell line
    • phox cDNA and functional analysis in a human X-linked chronic granulomatous disease cell line. Blood 1996, 87:2005-2010.
    • (1996) Blood , vol.87 , pp. 2005-2010
    • Bjorgvinsdottir, H.1    Zhen, L.2    Dinauer, M.3
  • 25
    • 20744449274 scopus 로고    scopus 로고
    • Blockade of histone deacetylase inhibitor-induced RelA/p65 acetylation and NF-kappaB activation potentiates apoptosis in leukemia cells through a process mediated by oxidative damage, XIAP downregulation, and c-Jun N-terminal kinase 1 activation
    • Dai Y., Rahmani M., Dent P., Grant S. Blockade of histone deacetylase inhibitor-induced RelA/p65 acetylation and NF-kappaB activation potentiates apoptosis in leukemia cells through a process mediated by oxidative damage, XIAP downregulation, and c-Jun N-terminal kinase 1 activation. Mol. Cell Biol. 2005, 25:5429-5444.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 5429-5444
    • Dai, Y.1    Rahmani, M.2    Dent, P.3    Grant, S.4
  • 26
    • 33646795007 scopus 로고    scopus 로고
    • Direct effects of glucagon-like peptide-1 on myocardial contractility and glucose uptake in normal and postischemic isolated rat hearts
    • Zhao T., Parikh P., Bhashyam S., Bolukoglu H., Poornima I., Shen Y.T., Shannon R.P. Direct effects of glucagon-like peptide-1 on myocardial contractility and glucose uptake in normal and postischemic isolated rat hearts. J. Pharmacol. Exp. Ther. 2006, 317:1106-1113.
    • (2006) J. Pharmacol. Exp. Ther. , vol.317 , pp. 1106-1113
    • Zhao, T.1    Parikh, P.2    Bhashyam, S.3    Bolukoglu, H.4    Poornima, I.5    Shen, Y.T.6    Shannon, R.P.7
  • 27
    • 0036516501 scopus 로고    scopus 로고
    • Late preconditioning elicited by activation of adenosine A(3) receptor in heart: role of NF-kappa B, iNOS and mitochondrial K(ATP) channel
    • Zhao T.C., Kukreja R.C. Late preconditioning elicited by activation of adenosine A(3) receptor in heart: role of NF-kappa B, iNOS and mitochondrial K(ATP) channel. J. Mol. Cell Cardiol. 2002, 34:263-277.
    • (2002) J. Mol. Cell Cardiol. , vol.34 , pp. 263-277
    • Zhao, T.C.1    Kukreja, R.C.2
  • 29
    • 0035834815 scopus 로고    scopus 로고
    • P38 Triggers late preconditioning elicited by anisomycin in heart: involvement of NF-kappaB and iNOS
    • Zhao T.C., Taher M.M., Valerie K.C., Kukreja R.C. p38 Triggers late preconditioning elicited by anisomycin in heart: involvement of NF-kappaB and iNOS. Circ. Res. 2001, 89:915-922.
    • (2001) Circ. Res. , vol.89 , pp. 915-922
    • Zhao, T.C.1    Taher, M.M.2    Valerie, K.C.3    Kukreja, R.C.4
  • 31
    • 4544256691 scopus 로고    scopus 로고
    • P38 and JNK have distinct regulatory functions on the development of apoptosis during simulated ischaemia and reperfusion in neonatal cardiomyocytes
    • Engelbrecht A.M., Niesler C., Page C., Lochner A. p38 and JNK have distinct regulatory functions on the development of apoptosis during simulated ischaemia and reperfusion in neonatal cardiomyocytes. Basic Res. Cardiol. 2004, 99:338-350.
    • (2004) Basic Res. Cardiol. , vol.99 , pp. 338-350
    • Engelbrecht, A.M.1    Niesler, C.2    Page, C.3    Lochner, A.4
  • 33
    • 57349200484 scopus 로고    scopus 로고
    • Increased superoxide levels in ganglia and sympathoexcitation are involved in sarafotoxin 6c-induced hypertension
    • Li M., Dai X., Watts S., Kreulen D., Fink G. Increased superoxide levels in ganglia and sympathoexcitation are involved in sarafotoxin 6c-induced hypertension. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2008, 295:R1546-R1554.
    • (2008) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.295
    • Li, M.1    Dai, X.2    Watts, S.3    Kreulen, D.4    Fink, G.5
  • 34
    • 0024996768 scopus 로고
    • Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A
    • Yoshida M., Kijima M., Akita M., Beppu T. Potent and specific inhibition of mammalian histone deacetylase both in vivo and in vitro by trichostatin A. J. Biol. Chem. 1990, 265:17174-17179.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17174-17179
    • Yoshida, M.1    Kijima, M.2    Akita, M.3    Beppu, T.4
  • 38
    • 0035843914 scopus 로고    scopus 로고
    • Role of NADPH oxidase in the vascular hypertrophic and oxidative stress response to angiotensin II in mice
    • Wang H.D., Xu S., Johns D.G., Du Y., Quinn M.T., Cayatte A.J., Cohen R.A. Role of NADPH oxidase in the vascular hypertrophic and oxidative stress response to angiotensin II in mice. Circ. Res. 2001, 88:947-953.
    • (2001) Circ. Res. , vol.88 , pp. 947-953
    • Wang, H.D.1    Xu, S.2    Johns, D.G.3    Du, Y.4    Quinn, M.T.5    Cayatte, A.J.6    Cohen, R.A.7
  • 39
    • 22144454977 scopus 로고    scopus 로고
    • Cardioprotection following adenosine kinase inhibition in rat hearts
    • Peart J.N., Gross G.J. Cardioprotection following adenosine kinase inhibition in rat hearts. Basic Res. Cardiol. 2005, 100:328-336.
    • (2005) Basic Res. Cardiol. , vol.100 , pp. 328-336
    • Peart, J.N.1    Gross, G.J.2
  • 40
    • 0030026058 scopus 로고    scopus 로고
    • Evidence for an essential role of reactive oxygen species in the genesis of late preconditioning against myocardial stunning in conscious pigs
    • Sun J.Z., Tang X.L., Park S.W., Qiu Y., Turrens J.F., Bolli R. Evidence for an essential role of reactive oxygen species in the genesis of late preconditioning against myocardial stunning in conscious pigs. J. Clin. Invest. 1996, 97:562-576.
    • (1996) J. Clin. Invest. , vol.97 , pp. 562-576
    • Sun, J.Z.1    Tang, X.L.2    Park, S.W.3    Qiu, Y.4    Turrens, J.F.5    Bolli, R.6
  • 42
    • 25444512382 scopus 로고    scopus 로고
    • Impairment of diazoxide-induced formation of reactive oxygen species and loss of cardioprotection in connexin 43 deficient mice
    • Heinzel F.R., Luo Y., Li X., Boengler K., Buechert A., García-Dorado D., Di Lisa F., Schulz R., Heusch G. Impairment of diazoxide-induced formation of reactive oxygen species and loss of cardioprotection in connexin 43 deficient mice. Circ. Res. 2005, 97:583-586.
    • (2005) Circ. Res. , vol.97 , pp. 583-586
    • Heinzel, F.R.1    Luo, Y.2    Li, X.3    Boengler, K.4    Buechert, A.5    García-Dorado, D.6    Di Lisa, F.7    Schulz, R.8    Heusch, G.9
  • 45
    • 0037646962 scopus 로고    scopus 로고
    • Overexpression of the stress protein Grp94 reduces cardiomyocyte necrosis due to calcium overload and simulated ischemia
    • Vitadello M., Penzo D., Petronilli V., Michieli G., Gomirato S., Menabò R., Di Lisa F., Gorza L. Overexpression of the stress protein Grp94 reduces cardiomyocyte necrosis due to calcium overload and simulated ischemia. FASEB J. 2003, 17:923-925.
    • (2003) FASEB J. , vol.17 , pp. 923-925
    • Vitadello, M.1    Penzo, D.2    Petronilli, V.3    Michieli, G.4    Gomirato, S.5    Menabò, R.6    Di Lisa, F.7    Gorza, L.8
  • 46
    • 0037154308 scopus 로고    scopus 로고
    • Pivotal role of a gp91(phox)-containing NADPH oxidase in angiotensin II-induced cardiac hypertrophy in mice
    • Bendall J.K., Cave A.C., Heymes C., Gall N., Shah A.M. Pivotal role of a gp91(phox)-containing NADPH oxidase in angiotensin II-induced cardiac hypertrophy in mice. Circulation 2002, 105:293-296.
    • (2002) Circulation , vol.105 , pp. 293-296
    • Bendall, J.K.1    Cave, A.C.2    Heymes, C.3    Gall, N.4    Shah, A.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.