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Volumn 41, Issue 3, 2006, Pages 406-409

TOM20 and the Heartbreakers: Evidence for the role of mitochondrial transport proteins in cardioprotection

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE SENSITIVE POTASSIUM CHANNEL; CALCIUM ION; CARRIER PROTEIN; HEAT SHOCK PROTEIN 70; MITOCHONDRIAL PROTEIN; NITRIC OXIDE; PROSTAGLANDIN SYNTHASE; PROTEIN KINASE; REACTIVE OXYGEN METABOLITE; TRANSLOCASE OF OUTER MITOCHONDRIAL MEMBRANE 20;

EID: 33748425875     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2006.06.073     Document Type: Editorial
Times cited : (6)

References (30)
  • 1
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium
    • Murry C.E., Jennings R.B., and Reimer K.A. Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium. Circulation 74 (1986) 1124-1136
    • (1986) Circulation , vol.74 , pp. 1124-1136
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 2
    • 20644434910 scopus 로고    scopus 로고
    • Mitochondrial K(ATP) channels in cell survival and death
    • Ardehali H., and O'Rourke B. Mitochondrial K(ATP) channels in cell survival and death. J. Mol. Cell Cardiol. 39 (2005) 7-16
    • (2005) J. Mol. Cell Cardiol. , vol.39 , pp. 7-16
    • Ardehali, H.1    O'Rourke, B.2
  • 3
    • 0034634284 scopus 로고    scopus 로고
    • Myocardial K(ATP) channels in preconditioning
    • O'Rourke B. Myocardial K(ATP) channels in preconditioning. Circ. Res. 87 (2000) 845-855
    • (2000) Circ. Res. , vol.87 , pp. 845-855
    • O'Rourke, B.1
  • 4
    • 0042859821 scopus 로고    scopus 로고
    • Role of the mitochondrial permeability transition in myocardial disease
    • Weiss J.N., Korge P., Honda H.M., and Ping P. Role of the mitochondrial permeability transition in myocardial disease. Circ. Res. 93 (2003) 292-301
    • (2003) Circ. Res. , vol.93 , pp. 292-301
    • Weiss, J.N.1    Korge, P.2    Honda, H.M.3    Ping, P.4
  • 5
    • 1542343927 scopus 로고    scopus 로고
    • Evidence for mitochondrial K+ channels and their role in cardioprotection
    • O'Rourke B. Evidence for mitochondrial K+ channels and their role in cardioprotection. Circ. Res. 94 (2004) 420-432
    • (2004) Circ. Res. , vol.94 , pp. 420-432
    • O'Rourke, B.1
  • 6
    • 4143097031 scopus 로고    scopus 로고
    • Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity
    • Ardehali H., Chen Z., Ko Y., Mejia-Alvarez R., and Marban E. Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 11880-11885
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11880-11885
    • Ardehali, H.1    Chen, Z.2    Ko, Y.3    Mejia-Alvarez, R.4    Marban, E.5
  • 7
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W. Protein import into mitochondria. Annu. Rev. Biochem. 66 (1997) 863-917
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 8
    • 0001777212 scopus 로고    scopus 로고
    • Protein translocation into mitochondria: the role of TIM complexes
    • Bauer M.F., Hofmann S., Neupert W., and Brunner M. Protein translocation into mitochondria: the role of TIM complexes. Trends Cell Biol. 10 (2000) 25-31
    • (2000) Trends Cell Biol. , vol.10 , pp. 25-31
    • Bauer, M.F.1    Hofmann, S.2    Neupert, W.3    Brunner, M.4
  • 9
    • 0036499987 scopus 로고    scopus 로고
    • The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier
    • Curran S.P., Leuenberger D., Oppliger W., and Koehler C.M. The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier. Embo. J. 21 (2002) 942-953
    • (2002) Embo. J. , vol.21 , pp. 942-953
    • Curran, S.P.1    Leuenberger, D.2    Oppliger, W.3    Koehler, C.M.4
  • 11
    • 0034209222 scopus 로고    scopus 로고
    • The protein import machinery of the mitochondrial membranes
    • Rassow J., and Pfanner N. The protein import machinery of the mitochondrial membranes. Traffic 1 (2000) 457-464
    • (2000) Traffic , vol.1 , pp. 457-464
    • Rassow, J.1    Pfanner, N.2
  • 12
    • 0037009132 scopus 로고    scopus 로고
    • Insertion of proteins into the inner membrane of mitochondria: the role of the oxa1 complex
    • Stuart R. Insertion of proteins into the inner membrane of mitochondria: the role of the oxa1 complex. Biochim. Biophys. Acta 1592 (2002) 79-87
    • (2002) Biochim. Biophys. Acta , vol.1592 , pp. 79-87
    • Stuart, R.1
  • 13
    • 0022065342 scopus 로고
    • A leader peptide is sufficient to direct mitochondrial import of a chimeric protein
    • Horwich A.L., Kalousek F., Mellman I., and Rosenberg L.E. A leader peptide is sufficient to direct mitochondrial import of a chimeric protein. Embo. J. 4 (1985) 1129-1135
    • (1985) Embo. J. , vol.4 , pp. 1129-1135
    • Horwich, A.L.1    Kalousek, F.2    Mellman, I.3    Rosenberg, L.E.4
  • 14
    • 0021676056 scopus 로고
    • The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix
    • Hurt E.C., Pesold-Hurt B., and Schatz G. The cleavable prepiece of an imported mitochondrial protein is sufficient to direct cytosolic dihydrofolate reductase into the mitochondrial matrix. FEBS Lett. 178 (1984) 306-310
    • (1984) FEBS Lett. , vol.178 , pp. 306-310
    • Hurt, E.C.1    Pesold-Hurt, B.2    Schatz, G.3
  • 15
    • 0022108729 scopus 로고
    • The first twelve amino acids (less than half of the pre-sequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix
    • Hurt E.C., Pesold-Hurt B., Suda K., Oppliger W., and Schatz G. The first twelve amino acids (less than half of the pre-sequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix. Embo. J. 4 (1985) 2061-2068
    • (1985) Embo. J. , vol.4 , pp. 2061-2068
    • Hurt, E.C.1    Pesold-Hurt, B.2    Suda, K.3    Oppliger, W.4    Schatz, G.5
  • 17
    • 0036138945 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Paschen S.A., and Neupert W. Protein import into mitochondria. IUBMB Life 52 (2001) 101-112
    • (2001) IUBMB Life , vol.52 , pp. 101-112
    • Paschen, S.A.1    Neupert, W.2
  • 18
    • 0142059893 scopus 로고    scopus 로고
    • Mitochondria use different mechanisms for transport of multispanning membrane proteins through the intermembrane space
    • Frazier A.E., Chacinska A., Truscott K.N., Guiard B., Pfanner N., and Rehling P. Mitochondria use different mechanisms for transport of multispanning membrane proteins through the intermembrane space. Mol. Cell Biol. 23 (2003) 7818-7828
    • (2003) Mol. Cell Biol. , vol.23 , pp. 7818-7828
    • Frazier, A.E.1    Chacinska, A.2    Truscott, K.N.3    Guiard, B.4    Pfanner, N.5    Rehling, P.6
  • 19
    • 0025953614 scopus 로고
    • Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences
    • Martin J., Mahlke K., and Pfanner N. Role of an energized inner membrane in mitochondrial protein import. Delta psi drives the movement of presequences. J. Biol. Chem. 266 (1991) 18051-18057
    • (1991) J. Biol. Chem. , vol.266 , pp. 18051-18057
    • Martin, J.1    Mahlke, K.2    Pfanner, N.3
  • 20
    • 0036343904 scopus 로고    scopus 로고
    • The protein import motor of mitochondria
    • Neupert W., and Brunner M. The protein import motor of mitochondria. Nat. Rev. Mol. Cell Biol. 3 (2002) 555-565
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 555-565
    • Neupert, W.1    Brunner, M.2
  • 21
    • 0042386354 scopus 로고    scopus 로고
    • Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles
    • Endo T., Yamamoto H., and Esaki M. Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles. J. Cell Sci. 116 (2003) 3259-3267
    • (2003) J. Cell Sci. , vol.116 , pp. 3259-3267
    • Endo, T.1    Yamamoto, H.2    Esaki, M.3
  • 22
    • 0034940401 scopus 로고    scopus 로고
    • Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences
    • Taylor A.B., Smith B.S., Kitada S., Kojima K., Miyaura H., Otwinowski Z., et al. Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. Structure 9 (2001) 615-625
    • (2001) Structure , vol.9 , pp. 615-625
    • Taylor, A.B.1    Smith, B.S.2    Kitada, S.3    Kojima, K.4    Miyaura, H.5    Otwinowski, Z.6
  • 23
    • 32444451348 scopus 로고    scopus 로고
    • A novel mutation in the gene encoding TIMM8a, a component of the mitochondrial protein translocase complexes, in a Spanish familial case of deafness-dystonia (Mohr-Tranebjaerg) syndrome
    • Aguirre L.A., del Castillo I., Macaya A., Meda C., Villamar M., Moreno-Pelayo M.A., et al. A novel mutation in the gene encoding TIMM8a, a component of the mitochondrial protein translocase complexes, in a Spanish familial case of deafness-dystonia (Mohr-Tranebjaerg) syndrome. Am. J. Med. Genet. A. 140 (2006) 392-397
    • (2006) Am. J. Med. Genet. A. , vol.140 , pp. 392-397
    • Aguirre, L.A.1    del Castillo, I.2    Macaya, A.3    Meda, C.4    Villamar, M.5    Moreno-Pelayo, M.A.6
  • 24
    • 0027246118 scopus 로고
    • A fatal, systemic mitochondrial disease with decreased mitochondrial enzyme activities, abnormal ultrastructure of the mitochondria and deficiency of heat shock protein 60
    • Agsteribbe E., Huckriede A., Veenhuis M., Ruiters M.H., Niezen-Koning K.E., Skjeldal O.H., et al. A fatal, systemic mitochondrial disease with decreased mitochondrial enzyme activities, abnormal ultrastructure of the mitochondria and deficiency of heat shock protein 60. Biochem. Biophys. Res. Commun. 193 (1993) 146-154
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 146-154
    • Agsteribbe, E.1    Huckriede, A.2    Veenhuis, M.3    Ruiters, M.H.4    Niezen-Koning, K.E.5    Skjeldal, O.H.6
  • 25
    • 0028131509 scopus 로고
    • Decreased synthesis and inefficient mitochondrial import of hsp60 in a patient with a mitochondrial encephalomyopathy
    • Huckriede A., and Agsteribbe E. Decreased synthesis and inefficient mitochondrial import of hsp60 in a patient with a mitochondrial encephalomyopathy. Biochim. Biophys. Acta 1227 (1994) 200-206
    • (1994) Biochim. Biophys. Acta , vol.1227 , pp. 200-206
    • Huckriede, A.1    Agsteribbe, E.2
  • 27
    • 0031831491 scopus 로고    scopus 로고
    • Contractile activity-induced adaptations in the mitochondrial protein import system
    • Takahashi M., Chesley A., Freyssenet D., and Hood D.A. Contractile activity-induced adaptations in the mitochondrial protein import system. Am. J. Physiol. 274 (1998) C1380-C1387
    • (1998) Am. J. Physiol. , vol.274
    • Takahashi, M.1    Chesley, A.2    Freyssenet, D.3    Hood, D.A.4
  • 29
    • 0032444931 scopus 로고    scopus 로고
    • Thyroid hormone modifies mitochondrial phenotype by increasing protein import without altering degradation
    • Craig E.E., Chesley A., and Hood D.A. Thyroid hormone modifies mitochondrial phenotype by increasing protein import without altering degradation. Am. J. Physiol. 275 (1998) C1508-C1515
    • (1998) Am. J. Physiol. , vol.275
    • Craig, E.E.1    Chesley, A.2    Hood, D.A.3
  • 30
    • 22544431970 scopus 로고    scopus 로고
    • The mitochondrial biogenesis regulatory program in cardiac adaptation to ischemia-a putative target for therapeutic intervention
    • McLeod C.J., Pagel I., and Sack M.N. The mitochondrial biogenesis regulatory program in cardiac adaptation to ischemia-a putative target for therapeutic intervention. Trends Cardiovasc. Med. 15 (2005) 118-123
    • (2005) Trends Cardiovasc. Med. , vol.15 , pp. 118-123
    • McLeod, C.J.1    Pagel, I.2    Sack, M.N.3


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