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Volumn 38, Issue 5, 2005, Pages 723-733

Ischemia depletes dystrophin and inhibits protein synthesis in the canine heart: Mechanisms of myocardial ischemic injury

Author keywords

Dog heart; Dystrophin; Ischemia; Transcription; Translation

Indexed keywords

ALBUMIN; BETA DYSTROGLYCAN; BETA1 INTEGRIN; DYSTROPHIN; GAMMA SARCOGLYCAN; GLYCOPROTEIN; LAMININ; S6 KINASE; SPECTRIN; UNCLASSIFIED DRUG; VINCULIN;

EID: 17844363973     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2005.02.019     Document Type: Article
Times cited : (51)

References (35)
  • 2
    • 0023194839 scopus 로고
    • Cytoskeletal damage during myocardial ischemia: Changes in vinculin immunofluorescence staining during total in vitro ischemia in canine heart
    • C. Steenbergen, M.L. Hill, and R.B. Jennings Cytoskeletal damage during myocardial ischemia: changes in vinculin immunofluorescence staining during total in vitro ischemia in canine heart Circ. Res. 60 4 1987 478 486
    • (1987) Circ. Res. , vol.60 , Issue.4 , pp. 478-486
    • Steenbergen, C.1    Hill, M.L.2    Jennings, R.B.3
  • 3
    • 0031739677 scopus 로고    scopus 로고
    • The internal and external protein scaffold of the T-tubular system in cardiomyocytes
    • S. Kostin, D. Scholz, T. Shimada, Y. Maeno, H. Mollnau, and S. Hein The internal and external protein scaffold of the T-tubular system in cardiomyocytes Cell Tissue Res. 294 3 1998 449 460
    • (1998) Cell Tissue Res. , vol.294 , Issue.3 , pp. 449-460
    • Kostin, S.1    Scholz, D.2    Shimada, T.3    Maeno, Y.4    Mollnau, H.5    Hein, S.6
  • 4
    • 0023727505 scopus 로고
    • Irreversible injury of isolated adult rat myocytes. Osmotic fragility during metabolic inhibition
    • C.E. Ganote, and R.S. Vander Heide Irreversible injury of isolated adult rat myocytes. Osmotic fragility during metabolic inhibition Am. J. Pathol. 132 1988 212 222
    • (1988) Am. J. Pathol. , vol.132 , pp. 212-222
    • Ganote, C.E.1    Vander Heide, R.S.2
  • 5
    • 85047675697 scopus 로고
    • Ischemia and the myocyte cytoskeleton: Review and speculation
    • C.E. Ganote, and S.C. Armstrong Ischemia and the myocyte cytoskeleton: review and speculation Cardiovasc. Res. 27 1993 1387 1403
    • (1993) Cardiovasc. Res. , vol.27 , pp. 1387-1403
    • Ganote, C.E.1    Armstrong, S.C.2
  • 6
    • 0037284342 scopus 로고    scopus 로고
    • An ischemic beta-dystroglycan (betaDG) degradation product: Correlation with irreversible injury in adult rabbit cardiomyocytes
    • S.C. Armstrong, C.A. Latham, and C.E. Ganote An ischemic beta-dystroglycan (betaDG) degradation product: correlation with irreversible injury in adult rabbit cardiomyocytes Mol. Cell. Biochem. 242 1-2 2003 71 79
    • (2003) Mol. Cell. Biochem. , vol.242 , Issue.1-2 , pp. 71-79
    • Armstrong, S.C.1    Latham, C.A.2    Ganote, C.E.3
  • 7
    • 0034955468 scopus 로고    scopus 로고
    • Ischemic loss of sarcolemmal dystrophin and spectrin: Correlation with myocardial injury
    • S.C. Armstrong, C.A. Latham, C.L. Shivell, and C.E. Ganote Ischemic loss of sarcolemmal dystrophin and spectrin: correlation with myocardial injury J. Mol. Cell. Cardiol. 33 6 2001 1165 1179
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , Issue.6 , pp. 1165-1179
    • Armstrong, S.C.1    Latham, C.A.2    Shivell, C.L.3    Ganote, C.E.4
  • 8
    • 0035140850 scopus 로고    scopus 로고
    • Sarcolemmal blebs and osmotic fragility as correlates of irreversible ischemic injury in preconditioned isolated rabbit cardiomyocytes
    • S.C. Armstrong, L.C. Shivell, and C.E. Ganote Sarcolemmal blebs and osmotic fragility as correlates of irreversible ischemic injury in preconditioned isolated rabbit cardiomyocytes J. Mol. Cell. Cardiol. 33 1 2001 149 160
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , Issue.1 , pp. 149-160
    • Armstrong, S.C.1    Shivell, L.C.2    Ganote, C.E.3
  • 9
    • 0022329605 scopus 로고
    • Ultrastructural characteristics of regional ischaemia and infarction in the canine heart
    • J. Schaper, P. Alpers, M. Gottwik, and W. Schaper Ultrastructural characteristics of regional ischaemia and infarction in the canine heart Eur. Heart J. 6 Suppl E 1985 21 31
    • (1985) Eur. Heart J. , vol.6 , Issue.SUPPL. E , pp. 21-31
    • Schaper, J.1    Alpers, P.2    Gottwik, M.3    Schaper, W.4
  • 10
    • 0042671357 scopus 로고    scopus 로고
    • Pre-mRNA splicing: Awash in a sea of proteins
    • M.S. Jurica, and M.J. Moore Pre-mRNA splicing: awash in a sea of proteins Mol. Cell 12 1 2003 5 14
    • (2003) Mol. Cell , vol.12 , Issue.1 , pp. 5-14
    • Jurica, M.S.1    Moore, M.J.2
  • 11
    • 0025936626 scopus 로고
    • Associations between distinct pre-mRNA splicing components and the cell nucleus
    • D.L. Spector, X.D. Fu, and T. Maniatis Associations between distinct pre-mRNA splicing components and the cell nucleus EMBO J. 10 11 1991 3467 3481
    • (1991) EMBO J. , vol.10 , Issue.11 , pp. 3467-3481
    • Spector, D.L.1    Fu, X.D.2    Maniatis, T.3
  • 12
    • 0029915031 scopus 로고    scopus 로고
    • P70 S6 kinase: An enigma with variations
    • C.G. Proud p70 S6 kinase: an enigma with variations Trends Biochem. Sci. 21 5 1996 181 185
    • (1996) Trends Biochem. Sci. , vol.21 , Issue.5 , pp. 181-185
    • Proud, C.G.1
  • 13
    • 0026465921 scopus 로고
    • Protein phosphorylation in translational control
    • C.G. Proud Protein phosphorylation in translational control Curr. Top. Cell. Regul. 32 1992 243 369
    • (1992) Curr. Top. Cell. Regul. , vol.32 , pp. 243-369
    • Proud, C.G.1
  • 15
    • 0034605070 scopus 로고    scopus 로고
    • The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin
    • I.N. Rybakova, J.R. Patel, and J.M. Ervasti The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin J. Cell Biol. 150 5 2000 1209 1214
    • (2000) J. Cell Biol. , vol.150 , Issue.5 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 16
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function
    • D.E. Michele, and K.P. Campbell Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function J. Biol. Chem. 278 18 2003 15457 15460
    • (2003) J. Biol. Chem. , vol.278 , Issue.18 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 18
    • 0037117144 scopus 로고    scopus 로고
    • Molecular remodelling of dystrophin in patients with end-stage cardiomyopathies and reversal in patients on assistance-device therapy
    • M. Vatta, S. Stetson, A. Perez-Verdia, M.L. Entman, G.P. Noon, and G. Torre-Amione Molecular remodelling of dystrophin in patients with end-stage cardiomyopathies and reversal in patients on assistance-device therapy Lancet 359 2002 936 941
    • (2002) Lancet , vol.359 , pp. 936-941
    • Vatta, M.1    Stetson, S.2    Perez-Verdia, A.3    Entman, M.L.4    Noon, G.P.5    Torre-Amione, G.6
  • 19
    • 0142090574 scopus 로고    scopus 로고
    • Decrease in sarcoglycans and dystrophin in failing heart following acute myocardial infarction
    • H. Yoshida, M. Takahashi, M. Koshimizu, K. Tanonaka, R. Oikawa, and T. Toyo-oka Decrease in sarcoglycans and dystrophin in failing heart following acute myocardial infarction Cardiovasc. Res. 59 2003 419 427
    • (2003) Cardiovasc. Res. , vol.59 , pp. 419-427
    • Yoshida, H.1    Takahashi, M.2    Koshimizu, M.3    Tanonaka, K.4    Oikawa, R.5    Toyo-Oka, T.6
  • 20
    • 0035190381 scopus 로고    scopus 로고
    • The dystrophin-glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies
    • T.A. Rando The dystrophin-glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies Muscle Nerve 24 12 2001 1575 1594
    • (2001) Muscle Nerve , vol.24 , Issue.12 , pp. 1575-1594
    • Rando, T.A.1
  • 21
    • 0035403114 scopus 로고    scopus 로고
    • Dystrophin-deficient cardiomyocytes are abnormally vulnerable to mechanical stress-induced contractile failure and injury
    • G. Danialou, A.S. Comtois, R. Dudley, G. Karpati, G. Vincent, and C. Des Rosiers Dystrophin-deficient cardiomyocytes are abnormally vulnerable to mechanical stress-induced contractile failure and injury FASEB J. 15 9 2001 1655 1657
    • (2001) FASEB J. , vol.15 , Issue.9 , pp. 1655-1657
    • Danialou, G.1    Comtois, A.S.2    Dudley, R.3    Karpati, G.4    Vincent, G.5    Des Rosiers, C.6
  • 22
    • 0035878554 scopus 로고    scopus 로고
    • Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex
    • H. Yamada, F. Saito, H. Fukuta-Ohi, D. Zhong, A. Hase, and K. Arai Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex Hum. Mol. Genet. 10 15 2001 1563 1569
    • (2001) Hum. Mol. Genet. , vol.10 , Issue.15 , pp. 1563-1569
    • Yamada, H.1    Saito, F.2    Fukuta-Ohi, H.3    Zhong, D.4    Hase, A.5    Arai, K.6
  • 23
    • 0034725593 scopus 로고    scopus 로고
    • Integrins and actin filaments: Reciprocal regulation of cell adhesion and signaling
    • D.A. Calderwood, S.J. Shattil, and M.H. Ginsberg Integrins and actin filaments: reciprocal regulation of cell adhesion and signaling J. Biol. Chem. 275 30 2000 22607 22610
    • (2000) J. Biol. Chem. , vol.275 , Issue.30 , pp. 22607-22610
    • Calderwood, D.A.1    Shattil, S.J.2    Ginsberg, M.H.3
  • 24
    • 0033040088 scopus 로고    scopus 로고
    • Vinculin, Talin, Integrin alpha6beta1 and laminin can serve as components of attachment complex mediating contraction force transmission from cardiomyocytes to extracellular matrix
    • K. Imanaka-Yoshida, M. Enomoto-Iwamoto, T. Yoshida, and T. Sakakura Vinculin, Talin, Integrin alpha6beta1 and laminin can serve as components of attachment complex mediating contraction force transmission from cardiomyocytes to extracellular matrix Cell Motil. Cytoskeleton 42 1 1999 1 11
    • (1999) Cell Motil. Cytoskeleton , vol.42 , Issue.1 , pp. 1-11
    • Imanaka-Yoshida, K.1    Enomoto-Iwamoto, M.2    Yoshida, T.3    Sakakura, T.4
  • 25
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • E. Zamir, and B. Geiger Molecular complexity and dynamics of cell-matrix adhesions J. Cell Sci. 114 Pt 20 2001 3583 3590
    • (2001) J. Cell Sci. , vol.114 , Issue.20 PART , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 26
    • 0026559273 scopus 로고
    • Flow cytometric analysis of isolated adult cardiomyocytes: Vinculin and tubulin fluorescence during metabolic inhibition and ischemia
    • S.C. Armstrong, and C.E. Ganote Flow cytometric analysis of isolated adult cardiomyocytes: vinculin and tubulin fluorescence during metabolic inhibition and ischemia J. Mol. Cell. Cardiol. 24 2 1992 149 162
    • (1992) J. Mol. Cell. Cardiol. , vol.24 , Issue.2 , pp. 149-162
    • Armstrong, S.C.1    Ganote, C.E.2
  • 27
    • 0029020791 scopus 로고
    • Ischemia induces early changes to cytoskeletal and contractile proteins in diseased human myocardium
    • S. Hein, T. Scheffold, and J. Schaper Ischemia induces early changes to cytoskeletal and contractile proteins in diseased human myocardium J. Thorac. Cardiovasc. Surg. 110 1 1995 89 98
    • (1995) J. Thorac. Cardiovasc. Surg. , vol.110 , Issue.1 , pp. 89-98
    • Hein, S.1    Scheffold, T.2    Schaper, J.3
  • 28
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • M.A. De Matteis, and J.S. Morrow Spectrin tethers and mesh in the biosynthetic pathway J. Cell Sci. 113 Pt 13 2000 2331 2343
    • (2000) J. Cell Sci. , vol.113 , Issue.13 PART , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 29
    • 0035232894 scopus 로고    scopus 로고
    • Mechanoprotection of the plasma membrane in neurons and other non-erythroid cells by the spectrin-based membrane skeleton
    • C.E. Morris Mechanoprotection of the plasma membrane in neurons and other non-erythroid cells by the spectrin-based membrane skeleton Cell. Mol. Biol. Lett. 6 3 2001 703 720
    • (2001) Cell. Mol. Biol. Lett. , vol.6 , Issue.3 , pp. 703-720
    • Morris, C.E.1
  • 30
    • 0033808066 scopus 로고    scopus 로고
    • Still more complexity in mammalian basement membranes
    • A.C. Erickson, and J.R. Couchman Still more complexity in mammalian basement membranes J. Histochem. Cytochem. 48 10 2000 1291 1306
    • (2000) J. Histochem. Cytochem. , vol.48 , Issue.10 , pp. 1291-1306
    • Erickson, A.C.1    Couchman, J.R.2
  • 31
    • 0018392696 scopus 로고
    • Ultrastructural, functional, and biochemical criteria for estimation of reversibility of ischemic injury: A study on the effects of global ischemia on the isolated dog heart
    • J. Schaper, J. Mulch, B. Winkler, and W. Schaper Ultrastructural, functional, and biochemical criteria for estimation of reversibility of ischemic injury: a study on the effects of global ischemia on the isolated dog heart J. Mol. Cell. Cardiol. 11 6 1979 521 541
    • (1979) J. Mol. Cell. Cardiol. , vol.11 , Issue.6 , pp. 521-541
    • Schaper, J.1    Mulch, J.2    Winkler, B.3    Schaper, W.4
  • 32
    • 85047680042 scopus 로고
    • Distribution of fibrinogen and albumin in normal, ischaemic, and necrotic myocardium during the evolution of myocardial infarction: An immunohistochemical study
    • M.C. Fishbein, D. Kulber, M. Stancl, and G. Edwalds Distribution of fibrinogen and albumin in normal, ischaemic, and necrotic myocardium during the evolution of myocardial infarction: an immunohistochemical study Cardiovasc. Res. 20 1 1986 36 41
    • (1986) Cardiovasc. Res. , vol.20 , Issue.1 , pp. 36-41
    • Fishbein, M.C.1    Kulber, D.2    Stancl, M.3    Edwalds, G.4
  • 33
    • 0030783172 scopus 로고    scopus 로고
    • Animal models for muscular dystrophy show different patterns of sarcolemmal disruption
    • V. Straub, J.A. Rafael, J.S. Chamberlain, and K.P. Campbell Animal models for muscular dystrophy show different patterns of sarcolemmal disruption J. Cell Biol. 139 2 1997 375 385
    • (1997) J. Cell Biol. , vol.139 , Issue.2 , pp. 375-385
    • Straub, V.1    Rafael, J.A.2    Chamberlain, J.S.3    Campbell, K.P.4
  • 34
    • 0027056909 scopus 로고
    • Differences in snRNP localization between transformed and nontransformed cells
    • D.L. Spector, G. Lark, and S. Huang Differences in snRNP localization between transformed and nontransformed cells Mol. Biol. Cell 3 5 1992 555 569
    • (1992) Mol. Biol. Cell , vol.3 , Issue.5 , pp. 555-569
    • Spector, D.L.1    Lark, G.2    Huang, S.3
  • 35
    • 0031846441 scopus 로고    scopus 로고
    • Functional association of nuclear protein 4.1 with pre-mRNA splicing factors
    • M.J. Lallena, C. Martinez, J. Valcarcel, and I. Correas Functional association of nuclear protein 4.1 with pre-mRNA splicing factors J. Cell Sci. 111 Pt 14 1998 1963 1971
    • (1998) J. Cell Sci. , vol.111 , Issue.14 PART , pp. 1963-1971
    • Lallena, M.J.1    Martinez, C.2    Valcarcel, J.3    Correas, I.4


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