메뉴 건너뛰기




Volumn 263, Issue 2, 1999, Pages 353-359

Import and processing of heart mitochondrial cyclophilin D

Author keywords

Cyclophilins; Import; Mitochondria; Polymerase chain reaction

Indexed keywords

CYCLOPHILIN; CYCLOPHILIN D; CYCLOSPORIN A; DIGITONIN; UNCLASSIFIED DRUG;

EID: 0033565965     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00490.x     Document Type: Article
Times cited : (52)

References (43)
  • 1
    • 0027049848 scopus 로고
    • Structural and evolutionary relationships among the immunophilins: Two ubiquitous families of peptidyl-prolyl cis-trans isomerases
    • 1. Trandinh, C.C., Pao, G.M. & Saier, M.H. Jr (1992) Structural and evolutionary relationships among the immunophilins: two ubiquitous families of peptidyl-prolyl cis-trans isomerases. FASEB J. 6, 3410-3420.
    • (1992) Faseb J. , vol.6 , pp. 3410-3420
    • Trandinh, C.C.1    Pao, G.M.2    Saier M.H., Jr.3
  • 2
    • 0027363385 scopus 로고
    • Peptidyl cis-trans-isomerases: Immunophilins
    • 2. Galat, A. (1993) Peptidyl cis-trans-isomerases: immunophilins. Eur. J. Biochem. 216, 689-707.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 689-707
    • Galat, A.1
  • 7
    • 0026696585 scopus 로고
    • Purification and n-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin
    • 7. Connern, C.P. & Halestrap, A.P. (1992) Purification and N-terminal sequencing of peptidyl-prolyl cis-trans-isomerase from rat liver mitochondrial matrix reveals the existence of a distinct mitochondrial cyclophilin. Biochem. J. 284, 381-385.
    • (1992) Biochem. J. , vol.284 , pp. 381-385
    • Connern, C.P.1    Halestrap, A.P.2
  • 9
    • 0025916166 scopus 로고
    • Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum
    • 9. Lodish, H.F. & Kong, N. (1991) Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum. J. Biol. Chem. 266, 14835-14838.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14835-14838
    • Lodish, H.F.1    Kong, N.2
  • 11
    • 0028948314 scopus 로고
    • Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60
    • 11. Rassow, J., Mohrs, K., Koidl, S., Barthelmess, I.B., Pfanner, N. & Tropschug, M. (1995) Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60. Mol. Cell. Biol. 15, 2654-2662.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2654-2662
    • Rassow, J.1    Mohrs, K.2    Koidl, S.3    Barthelmess, I.B.4    Pfanner, N.5    Tropschug, M.6
  • 12
    • 0023821864 scopus 로고
    • 2+ dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • 2+ dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem. J. 25, 357-360.
    • (1988) Biochem. J. , vol.25 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 13
    • 0017089948 scopus 로고
    • Relationship between configuration, function and permeability in calcium-treated mitochondria
    • 13. Hunter, D.R., Haworth, R.A. & Southard, J.H. (1976) Relationship between configuration, function and permeability in calcium-treated mitochondria. J. Biol. Chem. 251, 5069-5077.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5069-5077
    • Hunter, D.R.1    Haworth, R.A.2    Southard, J.H.3
  • 14
    • 0018332596 scopus 로고
    • 2+-induced membrane transition in mitochondria
    • 2+-induced membrane transition in mitochondria. Arch. Biochem. 195, 453-459.
    • (1979) Arch. Biochem. , vol.195 , pp. 453-459
    • Hunter, D.R.1    Howarth, R.A.2
  • 15
    • 0026336737 scopus 로고
    • Inhibition of anoxia-induced injury in heart myocytes by cyclosporin A
    • 15. Nazareth, W., Yafei, N. & Crompton, M. (1991) Inhibition of anoxia-induced injury in heart myocytes by cyclosporin A. J. Mol. Cell. Cardiol. 23, 1351-1354.
    • (1991) J. Mol. Cell. Cardiol. , vol.23 , pp. 1351-1354
    • Nazareth, W.1    Yafei, N.2    Crompton, M.3
  • 17
    • 0028968606 scopus 로고
    • Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion
    • 17. Griffiths, E.J. & Halestrap, A.P. (1995) Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion. Biochem. J. 307, 93-98.
    • (1995) Biochem. J. , vol.307 , pp. 93-98
    • Griffiths, E.J.1    Halestrap, A.P.2
  • 18
    • 0028923778 scopus 로고
    • Contribution of the mitochondrial permeability transition to lethal injury after exposure of hepatocytes to t-butylhydroperoxide
    • 18. Nieminen, A.-L., Saylor, A.K., Tesfai, S.A., Herman, B. & LeMasters, J.J. (1995) Contribution of the mitochondrial permeability transition to lethal injury after exposure of hepatocytes to t-butylhydroperoxide. Biochem. J. 307, 99-106.
    • (1995) Biochem. J. , vol.307 , pp. 99-106
    • Nieminen, A.-L.1    Saylor, A.K.2    Tesfai, S.A.3    Herman, B.4    Lemasters, J.J.5
  • 20
    • 0023759935 scopus 로고
    • Involvement of the ADP/ATP carrier in calcium-induced perturbations of the mitochondrial inner membrane permeability: Importance of the orientation of the nucleotide binding site
    • 20. Le Quoc, K. & Le Quoc, D. (1988) Involvement of the ADP/ATP carrier in calcium-induced perturbations of the mitochondrial inner membrane permeability: importance of the orientation of the nucleotide binding site. Arch. Biochem. Biophys. 265, 249-257.
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 249-257
    • Le Quoc, K.1    Le Quoc, D.2
  • 21
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • 21. Zoratti, M. & Szabo, I. (1995) The mitochondrial permeability transition. Biochim. Biophys. Acta 1241, 139-176.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 22
    • 0030569305 scopus 로고    scopus 로고
    • Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore
    • 22. Beutner, G., Ruck, A., Riede, B., Welte, W. & Brdiczka, D. (1996) Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. FEBS Lett. 396, 189-195.
    • (1996) Febs Lett. , vol.396 , pp. 189-195
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Welte, W.4    Brdiczka, D.5
  • 23
    • 0344653616 scopus 로고    scopus 로고
    • Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases
    • 23. Beutner, G., Ruck, A., Riede, B. & Brdiczka, D. (1998) Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases. Biochim. Biophys. Acta 1368, 7-18.
    • (1998) Biochim. Biophys. Acta , vol.1368 , pp. 7-18
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Brdiczka, D.4
  • 24
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-d binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • 24. Crompton, M., Virji, S. & Ward, J.M. (1998) Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore. Eur. J. Biochem. 258, 729-735.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 25
    • 0032387842 scopus 로고    scopus 로고
    • Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition
    • 25. Woodfield, K., Ruck, A., Brdiczka, D. & Halestrap, A.P. (1998) Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition. Biochem. J. 336, 287-290.
    • (1998) Biochem. J. , vol.336 , pp. 287-290
    • Woodfield, K.1    Ruck, A.2    Brdiczka, D.3    Halestrap, A.P.4
  • 27
    • 0025821619 scopus 로고
    • Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide
    • 27. Isaya, G., Kalousek, F., Fenton, W.A. & Rosenberg, L.E. (1991) Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide. J. Cell. Biol. 113, 65-76.
    • (1991) J. Cell. Biol. , vol.113 , pp. 65-76
    • Isaya, G.1    Kalousek, F.2    Fenton, W.A.3    Rosenberg, L.E.4
  • 29
    • 0024688488 scopus 로고
    • Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: Leader peptides cleaved by two matrix proteases share a three-amino acid motif
    • 29. Hendrick, J.P., Hodges, P.E. & Rosenberg, L.E. (1989) Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif. Proc. Natl Acad. Sci. USA 86, 4056-4060.
    • (1989) Proc. Natl Acad. Sci. Usa , vol.86 , pp. 4056-4060
    • Hendrick, J.P.1    Hodges, P.E.2    Rosenberg, L.E.3
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 31. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0023993152 scopus 로고
    • Latent membrane perturbation activity of a mitochondrial precursor is exposed by unfolding
    • 32. Endo, T. & Schatz, G. (1988) Latent membrane perturbation activity of a mitochondrial precursor is exposed by unfolding. EMBO J. 7, 1153-1158.
    • (1988) Embo J. , vol.7 , pp. 1153-1158
    • Endo, T.1    Schatz, G.2
  • 33
    • 0031559892 scopus 로고    scopus 로고
    • Direct expression of PCR products in a cell-free transcription/translation system: Synthesis of antibacterial peptide cecropin
    • 33. Martemyanov, K.A., Spirin, A.S. & Gudkov, A.T. (1997) Direct expression of PCR products in a cell-free transcription/translation system: synthesis of antibacterial peptide cecropin. FEBS Lett. 414, 268-270.
    • (1997) Febs Lett. , vol.414 , pp. 268-270
    • Martemyanov, K.A.1    Spirin, A.S.2    Gudkov, A.T.3
  • 34
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • 34. Kozak, M. (1986) Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44, 283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 35
    • 0026715079 scopus 로고
    • Plasmid cDNA-directed protein synthesis in a coupled eukaryotic in vitro transcription-translation system
    • 35. Craig, D., Howell, M.T., Gibbs, C.L., Hunt, T. & Jackson, R.J. (1992) Plasmid cDNA-directed protein synthesis in a coupled eukaryotic in vitro transcription-translation system. Nucleic Acids Res. 20, 4987-4995.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4987-4995
    • Craig, D.1    Howell, M.T.2    Gibbs, C.L.3    Hunt, T.4    Jackson, R.J.5
  • 36
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • 36. Neupert, W. (1997) Protein import into mitochondria. Annu. Rev. Biochem. 66, 863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 37
    • 0030051609 scopus 로고    scopus 로고
    • Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, a cyclosporin a-sensitive channel
    • 37. Nicolli, A., Basso, E., Petronilli, V., Wenger, R.M. & Bernardi, P. (1996) Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, a cyclosporin A-sensitive channel. J. Biol. Chem. 271, 2185-2192.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2185-2192
    • Nicolli, A.1    Basso, E.2    Petronilli, V.3    Wenger, R.M.4    Bernardi, P.5
  • 38
    • 0018400880 scopus 로고
    • Rapid separation of particulate and soluble fractions from isolated cell preparations (digitonin and cell cavitation procedures)
    • 38. Zuurendonk, P.F., Tischler, M.E., Akerboom, T.P.M., Van Der Meer, R., Williamson, J.R. & Tager, J.M. (1979) Rapid separation of particulate and soluble fractions from isolated cell preparations (digitonin and cell cavitation procedures). Methods Enzymol. 56, 207-223.
    • (1979) Methods Enzymol. , vol.56 , pp. 207-223
    • Zuurendonk, P.F.1    Tischler, M.E.2    Akerboom, T.P.M.3    Van Der Meer, R.4    Williamson, J.R.5    Tager, J.M.6
  • 39
    • 0027217548 scopus 로고
    • Cyclophilin 40 a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterisation
    • 39. Kieffer, L.J., Seng, T.W., Li, W., Osterman, D.G., Handschummacher, R.E. & Bayney, R.M. (1993) Cyclophilin 40 a protein with homology to the P59 component of the steroid receptor complex. Cloning of the cDNA and further characterisation. J. Biol. Chem. 268, 12303-12310.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12303-12310
    • Kieffer, L.J.1    Seng, T.W.2    Li, W.3    Osterman, D.G.4    Handschummacher, R.E.5    Bayney, R.M.6
  • 40
    • 0026013566 scopus 로고
    • Human cyclophilin B: A second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence
    • 40. Price, E.R., Zydowsky, L.D., Jin, M.J., Baker, C.H., McKeon, F.D. & Walsh, C.T. (1991) Human cyclophilin B: a second cyclophilin gene encodes a peptidyl-prolyl isomerase with a signal sequence. Proc. Natl Acad. Sci. USA 88, 1903-1907.
    • (1991) Proc. Natl Acad. Sci. Usa , vol.88 , pp. 1903-1907
    • Price, E.R.1    Zydowsky, L.D.2    Jin, M.J.3    Baker, C.H.4    McKeon, F.D.5    Walsh, C.T.6
  • 41
    • 0027964239 scopus 로고
    • Human cyclophilin C: Primary structure, tissue distribution and determination of binding specificity for cyclosporins
    • 41. Schneider, H., Chora, N., Schmitz, R., Wehrli, S., Mikol, V., Zurinin, M.G.N., Quesniaux, V.F.J. & Movva, N.R. (1994) Human cyclophilin C: primary structure, tissue distribution and determination of binding specificity for cyclosporins. Biochemistry 33, 8218-8224.
    • (1994) Biochemistry , vol.33 , pp. 8218-8224
    • Schneider, H.1    Chora, N.2    Schmitz, R.3    Wehrli, S.4    Mikol, V.5    Zurinin, M.G.N.6    Quesniaux, V.F.J.7    Movva, N.R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.