메뉴 건너뛰기




Volumn , Issue , 2012, Pages

The myocardial unfolded protein response during ischemic cardiovascular disease

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84859713589     PISSN: 20902247     EISSN: 20902255     Source Type: Journal    
DOI: 10.1155/2012/583170     Document Type: Review
Times cited : (17)

References (59)
  • 1
    • 19744378213 scopus 로고    scopus 로고
    • Heart failure
    • DOI 10.1016/S0140-6736(05)66621-4, PII S0140673605666214
    • McMurray J. J. V., Pfeffer M. A., Heart failure The Lancet 2005 365 9474 1877 1889 (Pubitemid 40744967)
    • (2005) Lancet , vol.365 , Issue.9474 , pp. 1877-1889
    • McMurray, J.J.V.1    Pfeffer, M.A.2
  • 2
    • 77955716725 scopus 로고    scopus 로고
    • The epidemiology and management of elderly patients with myocardial infarction or heart failure
    • Ezekowitz J. A., Kaul P., The epidemiology and management of elderly patients with myocardial infarction or heart failure Heart Failure Reviews 2010 15 5 407 413
    • (2010) Heart Failure Reviews , vol.15 , Issue.5 , pp. 407-413
    • Ezekowitz, J.A.1    Kaul, P.2
  • 6
    • 59449098471 scopus 로고    scopus 로고
    • Apoptotic and non-apoptotic programmed cardiomyocyte death in ventricular remodelling
    • Dorn G. W., Apoptotic and non-apoptotic programmed cardiomyocyte death in ventricular remodelling Cardiovascular Research 2009 81 3 465 473
    • (2009) Cardiovascular Research , vol.81 , Issue.3 , pp. 465-473
    • Dorn, G.W.1
  • 8
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • Ron D., Walter P., Signal integration in the endoplasmic reticulum unfolded protein response Nature Reviews Molecular Cell Biology 2007 8 7 519 529 (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 10
    • 0035966320 scopus 로고    scopus 로고
    • The unfolding tale of the unfolded protein response
    • DOI 10.1016/S0092-8674(01)00623-7
    • Ma Y., Hendershot L. M., The unfolding tale of the unfolded protein response Cell 2001 107 7 827 830 (Pubitemid 34084974)
    • (2001) Cell , vol.107 , Issue.7 , pp. 827-830
    • Ma, Y.1    Hendershot, L.M.2
  • 11
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • DOI 10.1016/0092-8674(93)90648-A
    • Cox J. S., Shamu C. E., Walter P., Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase Cell 1993 73 6 1197 1206 (Pubitemid 23180493)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 12
    • 0032509216 scopus 로고    scopus 로고
    • Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors
    • Yoshida H., Haze K., Yanagi H., Yura T., Mori K., Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins. Involvement of basic leucine zipper transcription factors The Journal of Biological Chemistry 1998 273 50 33741 33749
    • (1998) The Journal of Biological Chemistry , vol.273 , Issue.50 , pp. 33741-33749
    • Yoshida, H.1    Haze, K.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 13
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic- reticulum-resident kinase
    • DOI 10.1038/16729
    • Harding H. P., Zhang Y., Ron D., Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase Nature 1999 397 6716 271 274 (Pubitemid 29051178)
    • (1999) Nature , vol.397 , Issue.6716 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 14
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander R., Jarosch E., Urban J., Volkwein C., Sommer T., A regulatory link between ER-associated protein degradation and the unfolded-protein response Nature Cell Biology 2000 2 7 379 384
    • (2000) Nature Cell Biology , vol.2 , Issue.7 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 15
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers K. J., Patil C. K., Wodicka L., Lockhart D. J., Weissman J. S., Walter P., Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation Cell 2000 101 3 249 258
    • (2000) Cell , vol.101 , Issue.3 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 16
    • 0033634641 scopus 로고    scopus 로고
    • Perk is essential for translational regulation and cell survival during the unfolded protein response
    • Harding H. P., Zhang Y., Bertolotti A., Zeng H., Ron D., Perk is essential for translational regulation and cell survival during the unfolded protein response Molecular Cell 2000 5 5 897 904
    • (2000) Molecular Cell , vol.5 , Issue.5 , pp. 897-904
    • Harding, H.P.1    Zhang, Y.2    Bertolotti, A.3    Zeng, H.4    Ron, D.5
  • 17
    • 56349087407 scopus 로고    scopus 로고
    • Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions
    • Merksamer P. I., Trusina A., Papa F. R., Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions Cell 2008 135 5 933 947
    • (2008) Cell , vol.135 , Issue.5 , pp. 933-947
    • Merksamer, P.I.1    Trusina, A.2    Papa, F.R.3
  • 18
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • Tabas I., Ron D., Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress Nature Cell Biology 2011 13 3 184 190
    • (2011) Nature Cell Biology , vol.13 , Issue.3 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 19
    • 0016681491 scopus 로고
    • Ultrastructural features of degenerated cardiac muscle cells in patients with cardiac hypertrophy
    • Maron B. J., Ferrans V. J., Roberts W. C., Ultrastructural features of degenerated cardiac muscle cells in patients with cardiac hypertrophy American Journal of Pathology 1975 79 3 387 434
    • (1975) American Journal of Pathology , vol.79 , Issue.3 , pp. 387-434
    • Maron, B.J.1    Ferrans, V.J.2    Roberts, W.C.3
  • 21
    • 0027398879 scopus 로고
    • Purification of a 90-kDa protein (band VII) from cardiac sarcoplasmic reticulum. Identification as calnexin and localization of casein kinase II phosphorylation sites
    • Cala S. E., Ulbright C., Kelley J. S., Jones L. R., Purification of a 90-kDa protein (band VII) from cardiac sarcoplasmic reticulum. Identification as calnexin and localization of casein kinase II phosphorylation sites Journal of Biological Chemistry 1993 268 4 2969 2975 (Pubitemid 23057936)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.4 , pp. 2969-2975
    • Cala, S.E.1    Ulbright, C.2    Kelley, J.S.3    Jones, L.R.4
  • 22
    • 0030697901 scopus 로고    scopus 로고
    • Immunolocalization and heart levels of GRP94 in the mouse during post-implantation development
    • DOI 10.1007/s004290050102
    • Barnes J. A., Smoak I. W., Immunolocalization and heart levels of GRP94 in the mouse during post-implantation development Anatomy and Embryology 1997 196 4 335 341 (Pubitemid 27464174)
    • (1997) Anatomy and Embryology , vol.196 , Issue.4 , pp. 335-341
    • Barnes, J.A.1    Smoak, I.W.2
  • 24
    • 44449104300 scopus 로고    scopus 로고
    • Cardiomyocyte expression of a polyglutamine preamyloid oligomer causes heart failure
    • DOI 10.1161/CIRCULATIONAHA.107.750232, PII 0000301720080527000007
    • Pattison J. S., Sanbe A., Maloyan A., Osinska H., Klevitsky R., Robbins J., Cardiomyocyte expression of a polyglutamine preamyloid oligomer causes heart failure Circulation 2008 117 21 2743 2751 (Pubitemid 351770455)
    • (2008) Circulation , vol.117 , Issue.21 , pp. 2743-2751
    • Pattison, J.S.1    Sanbe, A.2    Maloyan, A.3    Osinska, H.4    Klevitsky, R.5    Robbins, J.6
  • 25
    • 0035816115 scopus 로고    scopus 로고
    • Expression of R120G-αB-crystallin causes aberrant desmin and αB-crystallin aggregation and cardiomyopathy in mice
    • Wang X., Osinska H., Klevitsky R., Gerdes A. M., Nieman M., Lorenz J., Hewett T., Robbins J., Expression of R120G- B-crystallin causes aberrant desmin and B-crystallin aggregation and cardiomyopathy in mice Circulation Research 2001 89 1 84 91 (Pubitemid 34135496)
    • (2001) Circulation Research , vol.89 , Issue.1 , pp. 84-91
    • Wang, X.1    Osinska, H.2    Klevitsky, R.3    Gerdes, A.M.4    Nieman, M.5    Lorenz, J.6    Hewett, T.7    Robbins, J.8
  • 26
    • 79952758037 scopus 로고    scopus 로고
    • Interrelationship between cardiac hypertrophy, heart failure, and chronic kidney disease: Endoplasmic reticulum stress as a mediator of pathogenesis
    • Dickhout J. G., Carlisle R. E., Austin R. C., Interrelationship between cardiac hypertrophy, heart failure, and chronic kidney disease: endoplasmic reticulum stress as a mediator of pathogenesis Circulation Research 2011 108 5 629 642
    • (2011) Circulation Research , vol.108 , Issue.5 , pp. 629-642
    • Dickhout, J.G.1    Carlisle, R.E.2    Austin, R.C.3
  • 27
    • 0034751674 scopus 로고    scopus 로고
    • Endoplasmic reticulum in the heart, a forgotten organelle?
    • DOI 10.1023/A:1012209923231
    • Mesaeli N., Nakamura K., Opas M., Michalak M., Endoplasmic reticulum in the heart, a forgotten organelle? Molecular and Cellular Biochemistry 2001 225 1-2 1 6 (Pubitemid 33014627)
    • (2001) Molecular and Cellular Biochemistry , vol.225 , Issue.1-2 , pp. 1-6
    • Mesaeli, N.1    Nakamura, K.2    Opas, M.3    Michalak, M.4
  • 28
    • 66349100683 scopus 로고    scopus 로고
    • Endoplasmic and sarcoplasmic reticulum in the heart
    • Michalak M., Opas M., Endoplasmic and sarcoplasmic reticulum in the heart Trends in Cell Biology 2009 19 6 253 259
    • (2009) Trends in Cell Biology , vol.19 , Issue.6 , pp. 253-259
    • Michalak, M.1    Opas, M.2
  • 30
    • 0016288626 scopus 로고
    • Salient biochemical features in ischemic myocardium
    • Sobel B. E., Salient biochemical features in ischemic myocardium Circulation Research 1974 35 3 173 181
    • (1974) Circulation Research , vol.35 , Issue.3 , pp. 173-181
    • Sobel, B.E.1
  • 32
    • 0036660827 scopus 로고    scopus 로고
    • Mitochondrial damage during ischemia determines post-ischemic contractile dysfunction in perfused rat heart
    • DOI 10.1006/jmcc.2002.2002
    • Iwai T., Tanonaka K., Inoue R., Kasahara S., Kamo N., Takeo S., Mitochondrial damage during ischemia determines post-ischemic contractile dysfunction in perfused rat heart Journal of Molecular and Cellular Cardiology 2002 34 7 725 738 (Pubitemid 35205176)
    • (2002) Journal of Molecular and Cellular Cardiology , vol.34 , Issue.7 , pp. 725-738
    • Iwai, T.1    Tanonaka, K.2    Inoue, R.3    Kasahara, S.4    Kamo, N.5    Takeo, S.6
  • 33
    • 68949196897 scopus 로고    scopus 로고
    • Oxidative folding: Cellular strategies for dealing with the resultant equimolar production of reactive oxygen species
    • Shimizu Y., Hendershot L. M., Oxidative folding: cellular strategies for dealing with the resultant equimolar production of reactive oxygen species Antioxidants and Redox Signaling 2009 11 9 2317 2331
    • (2009) Antioxidants and Redox Signaling , vol.11 , Issue.9 , pp. 2317-2331
    • Shimizu, Y.1    Hendershot, L.M.2
  • 34
    • 33745019669 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress gene induction and protection from ischemia/reperfusion injury in the hearts of transgenic mice with a tamoxifen-regulated form of ATF6
    • DOI 10.1161/01.RES.0000220643.65941.8d, PII 0000301220060512000014
    • Martindale J. J., Fernandez R., Thuerauf D., Whittaker R., Gude N., Sussman M. A., Glembotski C. C., Endoplasmic reticulum stress gene induction and protection from ischemia/reperfusion injury in the hearts of transgenic mice with a tamoxifen-regulated form of ATF6 Circulation Research 2006 98 9 1186 1193 (Pubitemid 43948105)
    • (2006) Circulation Research , vol.98 , Issue.9 , pp. 1186-1193
    • Martindale, J.J.1    Fernandez, R.2    Thuerauf, D.3    Whittaker, R.4    Gude, N.5    Sussman, M.A.6    Glembotski, C.C.7
  • 35
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • DOI 10.1146/annurev.biochem.73.011303.074134
    • Schrder M., Kaufman R. J., The mammalian unfolded protein response Annual Review of Biochemistry 2005 74 739 789 (Pubitemid 40995523)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 36
    • 0030954870 scopus 로고    scopus 로고
    • The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response
    • DOI 10.1016/S0092-8674(00)80369-4
    • Sidrauski C., Walter P., The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response Cell 1997 90 6 1031 1039 (Pubitemid 27408517)
    • (1997) Cell , vol.90 , Issue.6 , pp. 1031-1039
    • Sidrauski, C.1    Walter, P.2
  • 37
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • DOI 10.1038/415092a
    • Calfon M., Zeng H., Urano F., Till J. H., Hubbard S. R., Harding H. P., Clark S. G., Ron D., IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA Nature 2002 415 6867 92 96 (Pubitemid 34062456)
    • (2002) Nature , vol.415 , Issue.6867 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 38
    • 0033516930 scopus 로고    scopus 로고
    • Targeted disruption of CRE-Binding factor TREB5 gene leads to cellular necrosis in cardiac myocytes at the embryonic stage
    • DOI 10.1006/bbrc.1999.0972
    • Masaki T., Yoshida M., Noguchi S., Targeted disruption of CRE-Binding factor TREB5 gene leads to cellular necrosis in cardiac myocytes at the embryonic stage Biochemical and Biophysical Research Communications 1999 261 2 350 356 (Pubitemid 29392480)
    • (1999) Biochemical and Biophysical Research Communications , vol.261 , Issue.2 , pp. 350-356
    • Masaki, T.1    Yoshida, M.2    Noguchi, S.3
  • 39
    • 76549115938 scopus 로고    scopus 로고
    • MCP-1 causes cardiomyoblast death via autophagy resulting from ER stress caused by oxidative stress generated by inducing a novel zinc-finger protein, MCPIP
    • Younce C. W., Kolattukudy P. E., MCP-1 causes cardiomyoblast death via autophagy resulting from ER stress caused by oxidative stress generated by inducing a novel zinc-finger protein, MCPIP Biochemical Journal 2010 426 1 43 53
    • (2010) Biochemical Journal , vol.426 , Issue.1 , pp. 43-53
    • Younce, C.W.1    Kolattukudy, P.E.2
  • 40
    • 33746788477 scopus 로고    scopus 로고
    • Activation of the unfolded protein response in infarcted mouse heart and hypoxic cultured cardiac myocytes
    • DOI 10.1161/01.RES.0000233317.70421.03, PII 0000301220060804000011
    • Thuerauf D. J., Marcinko M., Gude N., Rubio M., Sussman M. A., Glembotski C. C., Activation of the unfolded protein response in infarcted mouse heart and hypoxic cultured cardiac myocytes Circulation Research 2006 99 3 275 282 (Pubitemid 44174935)
    • (2006) Circulation Research , vol.99 , Issue.3 , pp. 275-282
    • Thuerauf, D.J.1    Marcinko, M.2    Gude, N.3    Rubio, M.4    Sussman, M.A.5    Glembotski, C.C.6
  • 41
    • 34548829885 scopus 로고    scopus 로고
    • δPKC participates in the endoplasmic reticulum stress-induced response in cultured cardiac myocytes and ischemic heart
    • DOI 10.1016/j.yjmcc.2007.07.061, PII S0022282807011698
    • Qi X., Vallentin A., Churchill E., Mochly-Rosen D., PKC participates in the endoplasmic reticulum stress-induced response in cultured cardiac myocytes and ischemic heart Journal of Molecular and Cellular Cardiology 2007 43 4 420 428 (Pubitemid 47451430)
    • (2007) Journal of Molecular and Cellular Cardiology , vol.43 , Issue.4 , pp. 420-428
    • Qi, X.1    Vallentin, A.2    Churchill, E.3    Mochly-Rosen, D.4
  • 43
    • 0034723235 scopus 로고    scopus 로고
    • Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1
    • DOI 10.1126/science.287.5453.664
    • Urano F., Wang X., Bertolotti A., Zhang Y., Chung P., Harding H. P., Ron D., Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1 Science 2000 287 5453 664 666 (Pubitemid 30070916)
    • (2000) Science , vol.287 , Issue.5453 , pp. 664-666
    • Urano, F.1    Wang, X.2    Bertolotti, A.3    Zhang, Y.4    Chung, P.5    Harding, H.P.6    Ron, D.7
  • 44
    • 58749099435 scopus 로고    scopus 로고
    • Compartmentalized expression of three novel sarco/endoplasmic reticulum Ca2+ATPase 3 isoforms including the switch to ER stress, SERCA3f, in non-failing and failing human heart
    • Dally S., Monceau V., Corvazier E., Bredoux R., Raies A., Bobe R., del Monte F., Enouf J., Compartmentalized expression of three novel sarco/endoplasmic reticulum Ca2+ATPase 3 isoforms including the switch to ER stress, SERCA3f, in non-failing and failing human heart Cell Calcium 2009 45 2 144 154
    • (2009) Cell Calcium , vol.45 , Issue.2 , pp. 144-154
    • Dally, S.1    Monceau, V.2    Corvazier, E.3    Bredoux, R.4    Raies, A.5    Bobe, R.6    Del Monte, F.7    Enouf, J.8
  • 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., Menab R., Di Lisa F., Gorza L., Overexpression of the stress protein Grp94 reduces cardiomyocyte necrosis due to calcium overload and simulated ischemia The FASEB Journal 2003 17 8 923 925
    • (2003) The FASEB Journal , vol.17 , Issue.8 , pp. 923-925
    • Vitadello, M.1    Penzo, D.2    Petronilli, V.3    Michieli, G.4    Gomirato, S.5    Menab, R.6    Di Lisa, F.7    Gorza, L.8
  • 50
    • 40649112123 scopus 로고    scopus 로고
    • The role of the unfolded protein response in the heart
    • DOI 10.1016/j.yjmcc.2007.10.017, PII S0022282807012837
    • Glembotski C. C., The role of the unfolded protein response in the heart Journal of Molecular and Cellular Cardiology 2008 44 3 453 459 (Pubitemid 351374700)
    • (2008) Journal of Molecular and Cellular Cardiology , vol.44 , Issue.3 , pp. 453-459
    • Glembotski, C.C.1
  • 53
    • 0033830234 scopus 로고    scopus 로고
    • Amino acids control mammalian gene transcription: Activating transcription factor 2 is essential for the amino acid responsiveness of the CHOP promoter
    • Bruhat A., Jousse C., Carraro V., Reimold A. M., Ferrara M., Fafournoux P., Amino acids control mammalian gene transcription: activating transcription factor 2 is essential for the amino acid responsiveness of the CHOP promoter Molecular and Cellular Biology 2000 20 19 7192 7204
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.19 , pp. 7192-7204
    • Bruhat, A.1    Jousse, C.2    Carraro, V.3    Reimold, A.M.4    Ferrara, M.5    Fafournoux, P.6
  • 54
    • 70450196548 scopus 로고    scopus 로고
    • Activating transcription factor 2 increases transactivation and protein stability of hypoxia-inducible factor 1 in hepatocytes
    • Choi J. H., Cho H. K., Choi Y. H., Cheong J. H., Activating transcription factor 2 increases transactivation and protein stability of hypoxia-inducible factor 1 in hepatocytes Biochemical Journal 2009 424 2 285 296
    • (2009) Biochemical Journal , vol.424 , Issue.2 , pp. 285-296
    • Choi, J.H.1    Cho, H.K.2    Choi, Y.H.3    Cheong, J.H.4
  • 55
    • 78349290664 scopus 로고    scopus 로고
    • PARM-1 is an endoplasmic reticulum molecule involved in endoplasmic reticulum stress-induced apoptosis in rat cardiac myocytes
    • ARTICLE E9746
    • Isodono K., Takahashi T., Imoto H., Nakanishi N., Ogata T., Asada S., Adachi A., Ueyama T., Oh H., Matsubara H., PARM-1 is an endoplasmic reticulum molecule involved in endoplasmic reticulum stress-induced apoptosis in rat cardiac myocytes PloS One 2010 5 3, article e9746
    • (2010) PloS One , vol.5 , pp. 3
    • Isodono, K.1    Takahashi, T.2    Imoto, H.3    Nakanishi, N.4    Ogata, T.5    Asada, S.6    Adachi, A.7    Ueyama, T.8    Oh, H.9    Matsubara, H.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.