Mitochondrion and apoptosis

Acta Biochimica et Biophysica Sinica

Volumn 33, Issue 1, 2001, Pages 11-12

  Fan, Ting Jun ^a   Xia, Lan ^a   Han, Yi Ren ^b  

^a OCEAN UNIVERSITY OF CHINA   (China)

^b SHANDONG UNIVERSITY   (China)

Author keywords

Apoptosis; Mitochondrion; Mitochondrion permeability transition pore

Indexed keywords

EID: 20444426286     PISSN: 05829879     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (42)

1. Fontaine E, Ichas F, Bernardi P. A ubiquinone-binding site regulates the mitochondrial permeability transition pore. J Biol Chem, 1998, 273(40): 25734-25740
2. Skulachev V P. Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell. FEBS Lett, 1996, 397(1): 7-10
3. Lin Q S. Mitochondria and apoptosis. Acta Biochimica et Biophysica Sinica, 1999, 31(2): 116-118
4. Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem J, 1999, 341(Pt 2): 233-249
5. Brdiczka D, Beutner G, Ruck A, Dolder M, Wallimann T. The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition. Biofactors. 1998, 8(3-4): 235-242
6. 2+ from rat heart and liver mitochondria following the interaction of thyroid hormone with the adenine nucleotide translocase. Thyroid, 1996, 6(5): 513-519
7. Brenner C, Cadiou H, Vieira H L. Bcl-2 and Bax regulate the channel activity of the mitochondrial adenine nucleotide translocator. Oncogene, 2000, 19(3): 329-336
8. Bauer M K A, Schubert A, Rocks O G. Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis. J Cell Biol, 1999, 147(7): 1493-1502
9. Wallimann T, Dolder M, Schlattner U, Eder M, Homemann T, O'Gorman E, Ruck A et al. Some new aspects of creatine kinase (CK): Compartmentation, structure, function and regulation for cellular and mitochondrial bioenergetics and physiology. Biofactors, 1998, 8(3-4): 229-234
10. Wieckowski M R, Wojtczak L. Fatty acid-induced uncoupling of oxidative phosphorylation is partly due to opening of the mitochondrial permeability transition pore. FEBS Lett, 1998, 423 (3): 339-342
11. Jacotot E, Ravagnan L, Loeffler M, Ferri K F, Vieira H L, Zamzami N, Costantini P et al. The HIV-1 viral protein R induces apoptosis via a direct effect on the mitochondrial permeability transition pore. J Exp Med, 2000, 191(1): 33-46
12. Costantini P, Belzacq A S, Vieira H L, Larochette N, de Pablo M A, Zamzami N, Susin S A et al. Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis. Oncogene, 2000, 19(2): 307-314
13. Korge P, Weiss J N. Thapsigargin directly induces the mitochondrial permeability transition. Eur J Biochem, 1999, 265(1): 273-281
14. Patterson S D, Spahr C S, Daugas E. Mass spectrometric identification of proteins released from mitochondria undergoing permeability transition. Cell Death Differ, 2000, 7(2): 137-144
15. Susin S A, Lorcnzo H K, Zamzami N, Marzo I, Snow B E, Brothers G M, Mangion J et al. Molecular characterization of mitochondrialapoptosis-inducing factor. Nature, 1999, 397(4): 441-445
16. Varkey J, Chen P, Jemmerson R, Abrams J M. Altered cytochrome c display precedes apoptotic cell death in Drosophila. J Cell Biol, 1999, 144(4): 701-710
17. Jemmerson R, Liu J, Hausauer D, Lam K P, Mondino A, Nelson R D. A conformational change in cytochrome c of apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles. Biochemistry, 1999, 38(12): 3599-3609
18. Cain K, Bratton S B, Langlais C, Walker G, Brown D G, Sun X M, Cohen G M. Apaf-1 oligomerizcs into biologically active ∼700-kD and inactive ∼1.4-kDa apoptosome complexes. J Biol Chem, 2000, 275(9): 6067-6070
19. Samali A, Cai J, Zhivotovsky B, Jones D P, Orrenius S. Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells. EMBOJ, 1999, 18(8): 2040-2048
20. Marcia Barinaga. Death by dozens of cuts. Science, 1998, 280 (3): 32-34
21. Cain K, Brown D G, Langlais C, Cohen G M. Caspase activation involves the formation of the aposome, a large (approximately 700 kD) caspase-activating complex. J Biol Chem, 1999, 274(32): 22686-22692
22. Holinger E P, Chittenden T, Lutz R J. Bak BH3 peptides antagonize Bcl-xL function and induce apoptosis through cytochrome c-independent activation of caspases. J Biol Chem , 1999, 274(19): 13298-13304
23. Chen Q, Gong B, Almasan A. Distinct stages of cytochrome c release from mitochondria: Evidence for a feedback amplification loop linking caspase activation to mitochondrial dysfunction in genotoxic stress induced apoptosis. Cell Death Differ, 2000, 7(2): 227-233
24. Han Z, Li G, Bremner T A, Lange T S, Zhang G, Jemmerson R, Wyche J H, Hendrickson E A. A cytosolic factor is required for mitochondrial cytochrome c efflux during apoptosis. Cell Differ, 1998, 5(6): 469-479
25. Chien M M, Zahradka K E, Newell M K, Freed J H. Fas-induced B cell apoptosis requires an increase in free cytosolic magnesium as an early event. J Biol Chem, 1999, 274(11): 7059-7066
26. Tsujimoto Y, Shimizu S. Bcl-2 family: Life-or-death switch. FEBS Lett, 2000, 466(1): 6-10
27. Ji H B, Zhai Q W, Liu X Y, Zheng Z C. Transcription regulation of bcl-2 gene. Acta Biochimica et Biophysica Sinica, 2000, 32 (2): 95-99
28. Shi Y H, Tang X M. Transporting pathway of apoptosis and its regulation. Chin J Cell Biol, 1999, 1: 49-53
29. Bossy-Wetzel E, Green D R. Caspases induce cytochrome c release from mitochondria by activating cytosolic factors. J Biol Chem, 1999, 274(25): 17484-17490
30. Cosulich S C, Savory P J, Clarke P R. Bcl-2 regulates amplification of caspase activation by cytochrome c. Curr Biol. 1999, 9 (3): 147-150
31. Krebs J F, Armstrong R C, Srinivasan A, Aja T, Wong A M, Aboy A, Sayers R et al. Activation of membrane-associated procaspase-3 is regulated by Bcl-2. J Cell Biol, 1999, 144(5): 915-926
32. Vander Heiden M G, Chandel N S, Schumacker P T, Thompson C B. Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange. Mol Cell, 1999, 3(2): 159-167
33. Finucane D M, Waterhouse N J, Amarante-Mendes G P, Cotter T G, Green D R. Collapse of the inner mitochondrial transmembrane potential is not required for apoptosis of HL60 cells. Exp Cell Res, 1999, 251(1): 166-174
34. Wang S, Wang Z, Boise L, Dent P, Grant S. Loss of the bcl-2 phosphorylation loop domain increases resistance of human leukemia cells (U937) to paclitaxel-mediated mitochondrial dysfunction and apoptosis. Biochem Biophys Res Commun. 1999, 259(1): 67-72
35. Dimmeler S, Breitschopf K, Haendeler J, Zeiher A M. Dephosphorylation targets Bcl-2 for ubiquitin-dependent degradation: a link between the apoptosome and the proteasome pathway. J Exp Med, 1999, 189(11): 1815-1822
36. Vier J, Linsinger G, Hacker G. Cytochrome c is dispensable for fas-induced caspase activation and apoptosis. Biochem Biophys Res Commun, 1999, 261(1): 71-78
37. Montessuit S, Mazzei G, Magnenat E, Antonsson B. Expression and purification of full-length human Bax alpha. Protein Expr Purif, 1999, 15(2): 202-206
38. Desagher S, Osen-Sand A, Nichols A. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol, 1999, 144(5): 891-901
39. Pastorino J G, Tafani M, Rothman R J, Marcineviciute A, Hoek J B, Farber J L. Functional consequences of the sustained or transient activation by Bax of the mitochondrial permeability transition pore. J Biol Chem, 1999, 274(44): 31734-31739
40. 3-linked mitochondrial calcium signals. EMBO J, 1999, 18 (22): 6349-6361
41. 2-terminal kinase activity, and apoptosis. Mol Cell Biol, 1999, 19(8): 5659-5674
42. Chakraborti T, Das S, Mondai M, Roychoudhury S, Chakraborti S. Oxidant, mitochondria and calcium: an overview. Cell Signal, 1999, 11(2): 77-85