Thyroid hormone modifies mitochondrial phenotype by increasing protein import without altering degradation

American Journal of Physiology - Cell Physiology

Volumn 275, Issue 6 44-6, 1998, Pages

  Craig, Elaine E ^a   Chesley, Alan ^a   Hood, David A ^a  

^a YORK UNIVERSITY   (Canada)

Author keywords

20 kDa translocase of the outer mitochondrial membrane; Cardiolipin; Mitochondrial biogenesis; Mitochondrial protein degradation; Molecular chaperones

Indexed keywords

DIHYDROFOLATE REDUCTASE; DOXORUBICIN; HEAT SHOCK PROTEIN; MALATE DEHYDROGENASE; ORNITHINE CARBAMOYLTRANSFERASE; THYROID HORMONE;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; HORMONE BINDING; MALE; MITOCHONDRIAL RESPIRATION; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN MODIFICATION; RAT;

ANIMALIA;

EID: 0032444931     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1998.275.6.c1508     Document Type: Article

References (27)

1. Bradford, M. M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 255-260, 1976.
2. Cheneval, D., M. Müller, R. Toni, S. Ruetz, and E. Carafoli. Adriamycin as a probe for the transversal distribution of cardiolipin in the inner mitochondrial membrane. J. Biol. Chem. 260: 13003-13007, 1985.
3. Connor, M. K., M. Takahashi, and D. A. Hood. Tissue-specific stability of nuclear and mitochondrially-encoded mRNAs. Arch. Biochem. Biophys. 333: 103-108, 1996.
4. Craig, E. E., and D. A. Hood. Influence of aging on protein import into cardiac mitochondria. Am. J. Physiol. 272 (Heart Circ. Physiol. 41): H2983-H2988, 1997.
5. Dekker, P. J. T., F. Martin, A. C. Maarse, U. Bomer, H. Muller, B. Guiard, M. Meijer, J. Rassow, and N. Pfanner. The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44. EMBO J. 16: 5408-5419, 1997.
6. Eilers, M., T. Endo, and G. Schatz. Adriamycin, a drug interacting with acidic phospholipids, blocks import of precursor proteins by isolated yeast mitochondria. J. Biol. Chem. 264: 2945-2950, 1989.
7. Endo, T., and G. Schatz. Latent membrane perturbation activity of a mitochondrial precursor protein is exposed by unfolding. EMBO J. 7: 1153-1158, 1988.
8. Glick, B. S. Can hsp70 proteins act as force-generating motors? Cell 80: 11-14, 1995.
9. Hajek, P., and D. M. Bedwell. Characterization of the mitochondrial binding and import properties of purified yeast F1-ATPase subunit precursor. J. Biol. Chem. 269: 7192-7200, 1994.
10. Langer, T., and T. Neupert. Regulated protein degradation in mitochondria. Experientia 52: 1069-1076, 1996.
11. Leenhouts, J. M., Z. Török, V. Mandieua, E. Goormaghtigh, and B. de Kruijff. The N-terminal half of a mitochondrial presequence peptide inserts into cardiolipin-containing membranes. FEBS Lett. 388: 34-38, 1996.
12. Mayer, A., W. Neupert, and R. Lill. Mitochondrial protein import: reversible binding of the presequence at the trans side of the outer membrane drives partial translocation and unfolding. Cell 80: 127-137, 1995.
13. McCallister, L. P., and E. Page. Effects of thyroxin on ultrastructure of rat myocardial cells: a stereological study. J. Ultrastruct. Res. 42: 136-155, 1973.
14. Mihara, K., and T. Omura. Cytosolic factors in mitochondrial protein import. Experientia 52: 1063-1068, 1996.
15. Nishiki, K., M. Erecinska, D. F. Wilson, and S. Cooper. Evaluation of oxidative phosphorylation in hearts from euthyroid, hypothyroid and hyperthyroid rats. Am. J. Physiol. 235 (Cell Physiol. 4): C212-C219, 1978.
16. Paradies, G., F. M. Ruggiero, G. Petrosillo, and E. Quagliariello. Enhanced cytochrome oxidase activity and modifications of lipids in heart mitochondria from hyperthyroid rats. Biochim. Biophys. Acta 1225: 165-170, 1994.
17. Pfanner, N. Mitochondrial import: crossing the aqueous intermembrane space. Curr. Biol. 8: R262-R265, 1998.
18. Ryan, M. T., D. J. Naylor, P. B. Høj, M. S. Clark, and N. P. Hoogenraad. The role of molecular chaperones in mitochondrial protein import and folding. Int. Rev. Cytol. 174: 127-193, 1997.
19. Schatz, G. The protein import system of mitochondria. J. Biol. Chem. 271: 31763-31766, 1996.
20. Schneider, H.-C., J. Berthold, M. F. Bauer, K. Dietmeier, B. Guiard, M. Brunner, and W. Neupert. Mitochondrial hsp70/MIM44 complex facilitates protein import. Nature 371: 768-774, 1994.
21. Soboll, S. Thyroid hormone action on mitochondrial energy transfer. Biochim. Biophys. Acta 1144: 1-16, 1993.
22. Suzuki, C. K., M. Rep, J. M. van Dijl, K. Suda, L. A. Grivell, and G. Schatz. ATP-dependent proteases that also chaperone protein biogenesis. Trends Biochem. Sci. 22: 118-123, 1997.
23. Takahashi, M., A. Chesley, D. Freyssenet, and D. A. Hood. Contractile activity-induced adaptations in the mitochondrial protein import system. Am. J. Physiol. 274 (Cell Physiol. 43): C1380-C1387, 1998.
24. Takahashi, M., and D. A. Hood. Protein import into subsarcolemmal and intermyofibrillar skeletal muscle mitochondria. J. Biol. Chem. 271: 27285-27291, 1996.
25. Terada, K., I. Ueda, K. Ohtsuka, T. Oda, A. Ishiyama, and M. Mori. The requirement of heat shock cognate 70 protein for mitochondrial import varies among precursor proteins and depends on precursor length. Mol. Cell. Biol. 16: 6103-6109, 1996.
26. Wagner, I., H. Arlt, L. van Dyck, T. Langer, and W. Neupert. Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13: 5135-5145, 1994.
27. Wang, N., S. Gottesman, M. C. Willingham, M. M. Gottesman, and M. R. Maurizi. A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. Proc. Natl. Acad. Sci. USA 90: 11247-11251, 1993.