CoChat
Sign Up
Cited by 610Mitochondrial Function and PathologyCell death mechanisms and regulationAutophagy in Disease and Therapy

Contributions of mitochondria to animal physiology: from homeostatic sensor to calcium signalling and cell death

Open access
Duchen, Michael R.·1999·The Journal of Physiology
DOI 10.1111/j.1469-7793.1999.001aa.xPMC PMC2269224
Open this paper in CoChat — free account

Abstract

Over recent years, it has become clear that mitochondria play a central role in many key aspects of animal physiology and pathophysiology. Their central and ubiquitous task is clearly the production of ATP. Nevertheless, they also play subtle roles in glucose homeostasis, acting as the sensor for substrate supply in the transduction pathway that promotes insulin secretion by the pancreatic β‐cell and that modulates the excitability of the hypothalamic glucose‐sensitive neurons involved in appetite control. Mitochondria may also act as sensors of availability of oxygen, the other major mitochondrial substrate, in the regulation of respiration. Mitochondria take up calcium, and the high capacity mitochondrial calcium uptake pathway provides a mechanism that couples energy demand to increased ATP production through the calcium‐dependent upregulation of mitochondrial enzyme activity. Mitochondrial calcium accumulation may also have a substantial impact on the spatiotemporal dynamics of cellular calcium signals, with subtle differences of detail in different cell types. Recent work has also revealed the centrality of mitochondrial dysfunction as an irreversible step in the pathway to both necrotic and apoptotic cell death. This review looks at recent developments in these rapidly evolving areas of cell physiology in an attempt to draw together disparate areas of research into a common theme.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1111/j.1469-7793.1999.001aa.x

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • The reactive species detected by CM-H2DCFDA in Aβ(22-35)-treated cortical neurons were primarily of mitochondrial origin.

    “Consistent with the findings of others (Saraiva et al., 2010), brief incubation with FCCP caused the loss of most CM-H2DCFDA fluorescence in Aβ(22–35)-treated cortical neurons (Fig. 2 B), suggesting that the RS detected by this dye was primarily of mitochondrial origin (Duchen, 1999).”

    From The mitochondria-targeted antioxidant MitoQ prevents loss of spatial memory retention and early neuropathology in a transgenic mouse model of Alzheimer’s disease (2011) · cites this paper as Duchen, 1999

    The paper’s discussion of FCCP (indexed as Abstract; page unavailable) supports the mechanistic premise that FCCP disrupts mitochondrial membrane potential. It does not report CM-H2DCFDA fluorescence or establish that the reactive species detected in Aβ(22–35)-treated cortical neurons were primarily mitochondrial. (LLM, conf=0.82)

    Experimental — accuracy not yet measured

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 110

  1. Acker H. Oxygen sensing in the carotid body: ideas and models. Advances in Experimental Medicine and Biology. 1994;360:21–27. doi: 10.1007/978-1-4615-2572-1_3. [DOI] [PubMed] [Google Scholar] · DOI
  2. Anichkov SV, Belen'kii ML. Pharmacology of the Carotid Body Chemo-receptors. New York: MacMillan; 1963. [Google Scholar]
  3. Ashcroft FM, Gribble FM. Correlating structure and function in ATP-sensitive K+ channels. Trends in Neurosciences. 1998;21:288–294. doi: 10.1016/s0166-2236(98)01225-9. [DOI] [PubMed] [Google Scholar] · DOI
  4. Ashford ML, Boden PR, Treherne JM. Glucose-induced excitation of hypothalamic neurones is mediated by ATP-sensitive K+ channels. Pflügers Archiv. 1990;415:479–483. doi: 10.1007/BF00373626. [DOI] [PubMed] [Google Scholar] · DOI
  5. Babcock DF, Herrington J, Goodwin PC, Park YB, Hille B. Mitochondrial participation in the intracellular Ca2+ network. Journal of Cell Biology. 1997;136:833–844. doi: 10.1083/jcb.136.4.833. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  6. Babcock DF, Hille B. Mitochondrial oversight of cellular Ca2+ signaling. Current Opinion in Neurobiology. 1998;8:398–404. doi: 10.1016/s0959-4388(98)80067-6. [DOI] [PubMed] [Google Scholar] · DOI
  7. Bezprozvanny I, Watras J, Ehrlich BE. Bell-shaped calcium-response curves of Ins(1,4,5)P3- and calcium-gated channels from endoplasmic reticulum of cerebellum. Nature. 1991;351:751–754. doi: 10.1038/351751a0. [DOI] [PubMed] [Google Scholar] · DOI
  8. Bindokas VP, Chong C, Lee CC, Colmers WF, Miller RJ. Changes in mitochondrial function resulting from synaptic activity in the rat hippocampal slice. Journal of Neuroscience. 1998;18:4570–4587. doi: 10.1523/JNEUROSCI.18-12-04570.1998. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  9. Biscoe TJ, Duchen MR. Responses of type I cells dissociated from the rabbit carotid body to hypoxia. The Journal of Physiology. 1990;428:39–59. doi: 10.1113/jphysiol.1990.sp018199. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  10. Boitier E, Rea R, Duchen MR. Modulation of the propagation of intracellular calcium waves by mitochondria in rat cortical astrocytes. Biophysical Journal. 1999;76:A223. doi: 10.1083/jcb.145.4.795. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  11. Boss O, Muzzin P, Giacobino JP. The uncoupling proteins, a review. European Journal of Endocrinology. 1998;139:1–9. doi: 10.1530/eje.0.1390001. [DOI] [PubMed] [Google Scholar] · DOI
  12. Brini M, Marsault R, Bastianutto C, Alvarez J, Pozzan T, Rizzuto R. Transfected aequorin in the measurement of cytosolic Ca2+ concentration ([Ca2+]c). A critical evaluation. Journal of Biological Chemistry. 1995;270:9896–9903. doi: 10.1074/jbc.270.17.9896. [DOI] [PubMed] [Google Scholar] · DOI
  13. Brustovetsky N, Klingenberg M. Mitochondrial ADP/ATP carrier can be reversibly converted into a large channel by Ca2+ Biochemistry. 1996;35:8483–8488. doi: 10.1021/bi960833v. [DOI] [PubMed] [Google Scholar] · DOI
  14. Buckler KJ. A novel oxygen-sensitive potassium current in rat carotid body type I cells. The Journal of Physiology. 1997;498:649–662. doi: 10.1113/jphysiol.1997.sp021890. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  15. Buckler KJ, Vaughan-Jones R. Effects of mitochondrial uncouplers on intracellular calcium, pH and membrane potential in rat carotid body type I cells. The Journal of Physiology. 1998;513:819–833. doi: 10.1111/j.1469-7793.1998.819ba.x. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  16. Castilho RF, Hansson O, Ward MW, Budd SL, Nicholls DG. Mitochondrial control of acute glutamate excitotoxicity in cultured cerebellar granule cells. Journal of Neuroscience. 1998;18:10277–10288. doi: 10.1523/JNEUROSCI.18-24-10277.1998. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI · Paper page
  17. Choi DW. Calcium and excitotoxic neuronal injury. Annals of the New York Academy of Sciences. 1994;747:162–171. doi: 10.1111/j.1749-6632.1994.tb44407.x. [DOI] [PubMed] [Google Scholar] · DOI
  18. Crompton M, Andreeva L. On the interactions of Ca2+ and cyclosporin A with a mitochondrial inner membrane pore: a study using cobaltammine complex inhibitors of the Ca2+ uniporter. Biochemical Journal. 1994;302:181–185. doi: 10.1042/bj3020181. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  19. Crompton M, Costi A. A heart mitochondrial pore with possible relevance to reperfusion injury. Biochemical Journal. 1990;266:33–39. doi: 10.1042/bj2660033. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  20. Crompton M, Ellinger H, Costi A. Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochemical Journal. 1988;255:357–360. [PMC free article] [PubMed] [Google Scholar]
  21. Crompton M, Virji S, Ward JM. Cyclophilin D binds strongly to complexes of the voltage dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore. European Journal of Biochemistry. 1998;258:729–735. doi: 10.1046/j.1432-1327.1998.2580729.x. [DOI] [PubMed] [Google Scholar] · DOI
  22. David G, Barrett DG, Barrett EF. Evidence that mitochondria bufffer physiological Ca2+ loads in lizard motor nerve terminals. The Journal of Physiology. 1998;509:59–97. doi: 10.1111/j.1469-7793.1998.059bo.x. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  23. Di Lisa F, Fan CZ, Gambassi G, Hogue BA, Kudryashova I, Hansford RG. Altered pyruvate dehydrogenase control and mitochondrial free Ca2+ in hearts of cardiomyopathic hamsters. American Journal of Physiology. 1993;264:H2188–2197. doi: 10.1152/ajpheart.1993.264.6.H2188. [DOI] [PubMed] [Google Scholar] · DOI
  24. Donnelly DF. Are oxygen dependent K+ channels essential for carotid body chemo-transduction? Respiratory Physiology. 1997;110:211–218. doi: 10.1016/s0034-5687(97)00085-6. [DOI] [PubMed] [Google Scholar] · DOI
  25. Duchen MR. Ca2+-dependent changes in the mitochondrial energetics of single mouse sensory neurones. Biochemical Journal. 1992;283:41–50. doi: 10.1042/bj2830041. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  26. Duchen MR, Biscoe TJ. Mitochondrial function in type I cells isolated from the rabbit carotid body. The Journal of Physiology. 1992a;450:13–31. doi: 10.1113/jphysiol.1992.sp019114. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  27. Duchen MR, Biscoe TJ. Relative mitochondrial membrane potential and [Ca2+]i in type I cells isolated from the rabbit carotid body. The Journal of Physiology. 1992b;450:31–61. doi: 10.1113/jphysiol.1992.sp019115. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  28. Duchen MR, Leyssens A, Crompton M. Transient mitochondrial depolarisations in response to focal SR calcium release in single rat cardiomyocytes. Journal of Cell Biology. 1998;142:975–988. doi: 10.1083/jcb.142.4.975. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  29. Duchen MR, McGuinness O, Brown L, Crompton M. The role of the cyclosporin-A sensitive mitochondrial pore in myocardial reperfusion injury. Cardiovascular Research. 1993a;27:1790–1794. doi: 10.1093/cvr/27.10.1790. [DOI] [PubMed] [Google Scholar] · DOI
  30. Duchen MR, Smith PA, Ashcroft FM. Substrate-dependent changes in mitochondrial function, [Ca2+]i and membrane channels in pancreatic beta cells in culture. Biochemical Journal. 1993b;294:35–42. doi: 10.1042/bj2940035. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  31. Fein A, Tsacopoulos M. Activation of mitochondrial oxidative metabolism by calcium ions in Limulus ventral photoreceptor. Nature. 1988;331:437–440. doi: 10.1038/331437a0. [DOI] [PubMed] [Google Scholar] · DOI
  32. Friedman JM, Halaas JL. Leptin and the regulation of body weight in mammals. Nature. 1998;395:763–770. doi: 10.1038/27376. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  33. Friel DD, Tsien RW. An FCCP-sensitive Ca2+ store in bullfrog sympathetic neurons and its participation in stimulus-evoked changes in [Ca2+]i. Journal of Neuroscience. 1994;14:4007–4024. doi: 10.1523/JNEUROSCI.14-07-04007.1994. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  34. Graeber MB, Muller U. Recent developments in the molecular genetics of mitochondrial disorders. Journal of the Neurological Sciences. 1998;153:251–263. doi: 10.1016/s0022-510x(97)00295-5. [DOI] [PubMed] [Google Scholar] · DOI
  35. Gray MW. Rickettsia, typhus and the mitochondrial connection. Nature. 1998;396:109–110. doi: 10.1038/24030. [DOI] [PubMed] [Google Scholar] · DOI
  36. Green DR, Reed JC. Mitochondria and apoptosis. Science. 1998;281:1309–1312. doi: 10.1126/science.281.5381.1309. [DOI] [PubMed] [Google Scholar] · DOI
  37. Griffiths EJ, Halestrap AP. Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion. Biochemical Journal. 1995;307:93–98. doi: 10.1042/bj3070093. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  38. Gunter TE, Buntinas L, Sparagna GC, Gunter KK. The Ca2+ transport mechanisms of mitochondria and Ca2+ uptake from physiological-type Ca2+ transients. Biochimica et Biophysica Acta. 1998;1366:5–15. doi: 10.1016/s0005-2728(98)00117-0. [DOI] [PubMed] [Google Scholar] · DOI
  39. Hagar RE, Burgstahler AD, Nathanson MH, Ehrlich BE. Type III InsP3 receptor channel stays open in the presence of increased calcium. Nature. 1998;396:81–84. doi: 10.1038/23954. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  40. Hajnoczky G, Robb-Gaspers LD, Seitz MB, Thomas AP. Decoding of cytosolic calcium oscillations in the mitochondria. Cell. 1995;82:415–424. doi: 10.1016/0092-8674(95)90430-1. [DOI] [PubMed] [Google Scholar] · DOI
  41. Harvey J, McKenna F, Herson PS, Spanswick D, Ashford ML. Leptin activates ATP-sensitive potassium channels in the rat insulin-secreting cell line, CRI-G1. The Journal of Physiology. 1997;504:527–535. doi: 10.1111/j.1469-7793.1997.527bd.x. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  42. Haworth RA, Hunter DR. The Ca2+-induced membrane transition in mitochondria. I. The protective mechanisms. Archives of Biochemistry and Biophysics. 1979a;195:453–459. doi: 10.1016/0003-9861(79)90371-0. [DOI] [PubMed] [Google Scholar] · DOI
  43. Haworth RA, Hunter DR. The Ca2+-induced membrane transition in mitochondria. II. Nature of the Ca2+ trigger site. Archives of Biochemistry and Biophysics. 1979b;195:460–467. doi: 10.1016/0003-9861(79)90372-2. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  44. Haworth RA, Hunter DR. The Ca2+-induced membrane transition in mitochondria. III. Transitional Ca2+ release. Archives of Biochemistry and Biophysics. 1979c;195:468–477. doi: 10.1016/0003-9861(79)90373-4. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  45. Herrington J, Park YB, Babcock D, Hille B. Dominant role of mitochondria in clearance of large Ca2+ loads from rat adrenal chromaffin cells. Neuron. 1996;16:219–228. doi: 10.1016/s0896-6273(00)80038-0. [DOI] [PubMed] [Google Scholar] · DOI
  46. Hoth M, Fanger CM, Lewis RS. Mitochondrial regulation of store-operated calcium signaling in T lymphocytes. Journal of Cell Biology. 1997;137:633–648. doi: 10.1083/jcb.137.3.633. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  47. Ichas F, Jouaville LS, Mazat JP. Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals. Cell. 1997;89:1145–1153. doi: 10.1016/s0092-8674(00)80301-3. [DOI] [PubMed] [Google Scholar] · DOI
  48. Ichas F, Mazat JP. From calcium signaling to cell death: two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state. Biochimica et Biophysica Acta. 1998;1366:33–50. doi: 10.1016/s0005-2728(98)00119-4. [DOI] [PubMed] [Google Scholar] · DOI
  49. Iino M. Biphasic Ca2+ dependence of inositol 1,4,5-trisphosphate-induced Ca2+ release in smooth muscle cells of the guinea pig taenia caeci. Journal of General Physiology. 1990;95:1103–1122. doi: 10.1085/jgp.95.6.1103. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  50. Jacobson D, Duchen MR. Fluorescence imaging of the mitochondrial permeability transition in rat cortical astrocytes in culture. The Journal of Physiology. 1998;506.P:75P. [Google Scholar]
  51. Jou MJ, Peng TI, Sheu SS. Histamine induces oscillations of mitochondrial free Ca2+ concentration in single cultured rat brain astrocytes. The Journal of Physiology. 1996;497:299–308. doi: 10.1113/jphysiol.1996.sp021769. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  52. Jouaville LS, Ichas F, Holmuhamedov EL, Camacho P, Lechleiter JD. Synchronization of calcium waves by mitochondrial substrates in Xenopus laevis oocytes. Nature. 1995;377:438–441. doi: 10.1038/377438a0. [DOI] [PubMed] [Google Scholar] · DOI
  53. Keelan J, Vergun O, Khodorov B, Duchen MR. Calcium-dependent mitochondrial depolarization specific to toxic glutamate stimulation in cultured rat hippocampal neurones. The Journal of Physiology. 1998;506.P:75P. doi: 10.1111/j.1469-7793.1999.0451m.x. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  54. Kennedy ED, Wollheim CB. Role of mitochondrial calcium in metabolism-secretion coupling in nutrient-stimulated insulin release. Diabetes and Metabolism. 1998;24:15–24. [PubMed] [Google Scholar]
  55. Kerr JFR, Wyllie AM, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. British Journal of Cancer. 1972;26:239–257. doi: 10.1038/bjc.1972.33. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  56. Khodorov B, Pinelis V, Storozhevykh T, Vergun O, Vinskaya N. Dominant role of mitochondria in protection against a delayed neuronal Ca2+ overload induced by endogenous excitatory amino acids following a glutamate pulse. FEBS Letters. 1996;393:135–138. doi: 10.1016/0014-5793(96)00873-3. [DOI] [PubMed] [Google Scholar] · DOI
  57. Khodorov B, Pinelis V, Vergun O, Storozhevykh T, Vinskaya N. Mitochondrial deenergization underlies neuronal calcium overload following a prolonged glutamate challenge. FEBS Letters. 1996;397:230–234. doi: 10.1016/s0014-5793(96)01139-8. [DOI] [PubMed] [Google Scholar] · DOI
  58. Kong J, Xu Z. Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1. Journal of Neuroscience. 1998;18:3241–3250. doi: 10.1523/JNEUROSCI.18-09-03241.1998. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  59. Kroemer G, Dallaporta B, Resche-Rigon M. The mitochondrial death/life regulator in apoptosis and necrosis. Annual Review of Physiology. 1998;60:619–642. doi: 10.1146/annurev.physiol.60.1.619. [DOI] [PubMed] [Google Scholar] · DOI
  60. Lahiri S, Chugh DK, Mokashi A, Vinogradov S, Osanai S, Wilson DF. Cytochrome oxidase is the primary oxygen sensor in the cat carotid body. Advances in Experimental Medicine and Biology. 1996;388:213–217. doi: 10.1007/978-1-4613-0333-6_26. [DOI] [PubMed] [Google Scholar] · DOI
  61. Lahiri S, Roy A, Rozanov C, Mokashi A. K+-current modulated by PO2 in type I cells in rat carotid body is not a chemosensor. Brain Research. 1998;794:162–165. doi: 10.1016/s0006-8993(98)00276-5. [DOI] [PubMed] [Google Scholar] · DOI
  62. Landolfi B, Curci S, Debellis L, Pozzan T, Hofer AM. Ca2+ homeostasis in the agonist-sensitive internal store: functional interactions between mitochondria and the ER measured in situ in intact cells. Journal of Cell Biology. 1998;142:1235–1243. doi: 10.1083/jcb.142.5.1235. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  63. Lawrie AM, Rizzuto R, Pozzan T, Simpson AW. A role for calcium influx in the regulation of mitochondrial calcium in endothelial cells. Journal of Biological Chemistry. 1996;271:10753–10759. doi: 10.1074/jbc.271.18.10753. [DOI] [PubMed] [Google Scholar] · DOI
  64. Lemasters JJ, Nieminen AL, Qian T, Trost LC, Elmore SP, Nishimura Y, Crowe RA, Cascio WE, Bradham CA, Brenner DA, Herman B. The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy. Biochimica et Biophysica Acta. 1998;1366:177–196. doi: 10.1016/s0005-2728(98)00112-1. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  65. Leyssens A, Nowicky AV, Patterson DL, Crompton M, Duchen MR. The relationship between mitochondrial state, ATP hydrolysis, [Mg2+]i and [Ca2+]i studied in isolated rat cardiomyocytes. The Journal of Physiology. 1996;496:111–128. doi: 10.1113/jphysiol.1996.sp021669. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  66. Lin J H-C, Weigel H, Cotrina ML, Liu S, Bueno E, Hansen AJ, Hansen TW, Goldman S, Nedergaard M. Gap-junction mediated propagation and amplification of cell injury. Nature Neuroscience. 1998;1:494–500. doi: 10.1038/2210. [DOI] [PubMed] [Google Scholar] · DOI
  67. Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell. 1996;86:147–157. doi: 10.1016/s0092-8674(00)80085-9. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  68. Lopez-Barneo J. Oxygen-sensing by ion channels and the regulation of cellular functions. Trends in Neurosciences. 1996;19:435–440. doi: 10.1016/0166-2236(96)10050-3. [DOI] [PubMed] [Google Scholar] · DOI
  69. Maechler P, Kennedy ED, Pozzan T, Wollheim CB. Mitochondrial activation directly triggers the exocytosis of insulin in permeabilized pancreatic beta-cells. EMBO Journal. 1997;16:3833–3841. doi: 10.1093/emboj/16.13.3833. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  70. Maechler P, Kennedy ED, Wang H, Wollheim CB. Desensitization of mitochondrial Ca2+ and insulin secretion responses in the beta cell. Journal of Biological Chemistry. 1998;273:20770–20778. doi: 10.1074/jbc.273.33.20770. [DOI] [PubMed] [Google Scholar] · DOI
  71. Margulis L. Archaeal-eubacterial mergers in the origin of Eukarya: phylogenetic classification of life. Proceedings of the National Academy of Sciences of the USA. 1996;93:1071–1076. doi: 10.1073/pnas.93.3.1071. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  72. Marzo I, Brenner C, Zamzami N, Jurgensmeier JM, Susin SA, Vieira HL, Prevost MC, Xie Z, Matsuyama S, Reed JC, Kroemer G. Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis. Science. 1998;281:2027–203. doi: 10.1126/science.281.5385.2027. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  73. Matlib MA, Zhou Z, Knight S, Ahmed S, Choi KM, Krause-Bauer J, Phillips R, Altschuld R, Katsube Y, Sperelakis N, Bers DM. Oxygen-bridged dinuclear ruthenium amine complex specifically inhibits Ca2+ uptake into mitochondria in vitro and in situ in single cardiac myocytes. Journal of Biological Chemistry. 1998;273:10223–10231. doi: 10.1074/jbc.273.17.10223. [DOI] [PubMed] [Google Scholar] · DOI
  74. Melamed-Book N, Rahamimoff R. The revival of the role of the mitochondrion in regulation of transmitter release. The Journal of Physiology. 1998;509:2. doi: 10.1111/j.1469-7793.1998.002bo.x. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  75. Miller RJ. Mitochondria - the Kraken wakes. Trends in Neurosciences. 1998;21:95–97. doi: 10.1016/s0166-2236(97)01206-x. [DOI] [PubMed] [Google Scholar] · DOI
  76. Mills E, Jöbsis FF. Simultaneous measurement of cytochrome a3 reduction and chemoreceptor afferent activity in the carotid body. Nature. 1970;225:1147–1149. doi: 10.1038/2251147a0. [DOI] [PubMed] [Google Scholar] · DOI
  77. Mills E, Jöbsis FF. Mitochondrial respiratory chain of carotid body and chemoreceptor response to changes in oxygen tension. Journal of Neurophysiology. 1972;35:405–428. doi: 10.1152/jn.1972.35.4.405. [DOI] [PubMed] [Google Scholar] · DOI
  78. Mitchell P, Moyle J. Chemiosmotic hypothesis of oxidative phosphorylation. Nature. 1967;213:137–139. doi: 10.1038/213137a0. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  79. Mogami H, Nakano K, Tepikin AV, Petersen OH. Ca2+ flow via tunnels in polarized cells: recharging of apical Ca2+ stores by focal Ca2+ entry through basal membrane patch. Cell. 1997;88:49–55. doi: 10.1016/s0092-8674(00)81857-7. [DOI] [PubMed] [Google Scholar] · DOI
  80. Morgan-Hughes JA, Schapira AH, Cooper JM, Holt IJ, Harding AE, Clark JB. The molecular pathology of respiratory-chain dysfunction in human mitochondrial myopathies. Biochimica et Biophysica Acta. 1990;1018:217–222. doi: 10.1016/0005-2728(90)90252-y. [DOI] [PubMed] [Google Scholar] · DOI
  81. Nicholls DG, Ferguson SJ. Bioenergetics 2. Academic Press; 1992. [Google Scholar]
  82. Nieminen AL, Petrie TG, Lemasters JJ, Selman WR. Cyclosporin A delays mitochondrial depolarization induced by N-methyl-D-aspartate in cortical neurons: evidence of the mitochondrial permeability transition. Neuroscience. 1996;75:993–997. doi: 10.1016/0306-4522(96)00378-8. [DOI] [PubMed] [Google Scholar] · DOI
  83. Noji H, Yasuda R, Yoshida M, Kinoshita K., Jr Direct observation of the rotation of F1-ATPase. Nature. 1997;386:299–302. doi: 10.1038/386299a0. [DOI] [PubMed] [Google Scholar] · DOI
  84. Palou A, Pico C, Bonet ML, Oliver P. The uncoupling protein, thermogenin. International Journal of Biochemistry and Cell Biology. 1998;30:7–11. doi: 10.1016/s1357-2725(97)00065-4. [DOI] [PubMed] [Google Scholar] · DOI
  85. Peers C. Oxygen-sensitive ion channels. Trends in Pharmacological Sciences. 1997;18:405–408. doi: 10.1016/s0165-6147(97)01120-6. [DOI] [PubMed] [Google Scholar] · DOI
  86. Petronilli V, Costantini P, Scorrano L, Colonna R, Passamonti S, Bernardi P. The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents. Journal of Biological Chemistry. 1994;269:16638–16642. [PubMed] [Google Scholar]
  87. Peuchen S, Duchen MR, Clark JB. Energy metabolism of adult astrocytes in vitro. Neuroscience. 1996;71:855–870. doi: 10.1016/0306-4522(95)00480-7. [DOI] [PubMed] [Google Scholar] · DOI
  88. Pralong WF, Spat A, Wollheim CB. Dynamic pacing of cell metabolism by intracellular Ca2+ transients. Journal of Biological Chemistry. 1994;269:27310–27314. [PubMed] [Google Scholar]
  89. Quayle JM, Nelson MT, Standen NB. ATP-sensitive and inwardly rectifying potassium channels in smooth muscle. Physiological Reviews. 1997;77:1165–1232. doi: 10.1152/physrev.1997.77.4.1165. [DOI] [PubMed] [Google Scholar] · DOI
  90. Ramos-Franco J, Fill M, Mignery GA. Isoform-specific function of single inositol 1,4,5-trisphosphate receptor channels. Biophysical Journal. 1998;75:834–839. doi: 10.1016/S0006-3495(98)77572-1. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  91. Rizzuto R, Bastianutto C, Brini M, Murgia M, Pozzan T. Mitochondrial Ca2+ homeostasis in intact cells. Journal of Cell Biology. 1994;126:1183–1194. doi: 10.1083/jcb.126.5.1183. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  92. Rizzuto R, Pinton P, Carrington W, Fay FS, Fogarty KE, Lifshitz LM, Tuft RA, Pozzan T. Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses. Science. 1998;280:1763–1766. doi: 10.1126/science.280.5370.1763. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  93. Rizzuto R, Simpson AW, Brini M, Pozzan T. Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin. Nature. 1992;358:325–327. doi: 10.1038/358325a0. [DOI] [PubMed] [Google Scholar] · DOI
  94. Robb-Gaspers LD, Burnett P, Rutter GA, Denton RM, Rizzuto R, Thomas AP. Integrating cytosolic calcium signals into mitochondrial metabolic responses. EMBO Journal. 1998;17:4987–5000. doi: 10.1093/emboj/17.17.4987. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  95. Rowe IC, Treherne JM, Ashford ML. Activation by intracellular ATP of a potassium channel in neurones from rat basomedial hypothalamus. The Journal of Physiology. 1996;490:97–113. doi: 10.1113/jphysiol.1996.sp021129. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  96. Schapira AH, Gu M, Taanman JW, Tabrizi SJ, Seaton T, Cleeter M, Cooper JM. Mitochondria in the etiology and pathogenesis of Parkinson's disease. Annals of Neurology. 1998;44(suppl. 1):S89–98. doi: 10.1002/ana.410440714. [DOI] [PubMed] [Google Scholar] · DOI
  97. Schinder AF, Olson EC, Spitzer NC, Montal M. Mitochondrial dysfunction is a primary event in glutamate neurotoxicity. Journal of Neuroscience. 1996;16:6125–6133. doi: 10.1523/JNEUROSCI.16-19-06125.1996. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  98. Shepherd CA, Simpson PB, Sharp AH, Nucifora FC, Ross CA, Lange GD, Russell JT. Comparison of Type 2 inositol 1,4,5,-trisphosphate receptor distribution and subcellular Ca2+ release sites that support Ca2+ waves in cultured astrocytes. Journal of Neurochemistry. 1997;68:2317–2327. doi: 10.1046/j.1471-4159.1997.68062317.x. [DOI] [PubMed] [Google Scholar] · DOI
  99. Simpson PB, Russell JT. Role of mitochondrial Ca2+ regulation in neuronal and glial cell signalling. Brain Research Reviews. 1998;26:72–81. doi: 10.1016/s0165-0173(97)00056-8. [DOI] [PubMed] [Google Scholar] · DOI
  100. Skulachev VP. Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell. FEBS Letters. 1996;397:7–10. doi: 10.1016/0014-5793(96)00989-1. [DOI] [PubMed] [Google Scholar] · DOI
  101. Spanswick D, Smith MA, Groppi VE, Logan SD, Ashford ML. Leptin inhibits hypothalamic neurons by activation of ATP-sensitive potassium channels. Nature. 1997;390:521–525. doi: 10.1038/37379. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  102. Stout AK, Raphael HM, Kanterewicz BI, Klann E, Reynolds IJ. Glutamate-induced neuron death requires mitochondrial calcium uptake. Nature Neuroscience. 1998;1:366–373. doi: 10.1038/1577. [DOI] [PubMed] [Google Scholar] · DOI
  103. Tang YG, Zucker RS. Mitochondrial involvement in post-tetanic potentiation of synaptic transmission. Neuron. 1997;18:483–491. doi: 10.1016/s0896-6273(00)81248-9. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  104. Thayer SA, Miller RJ. Regulation of the intracellular free calcium concentration in single rat dorsal root ganglion neurones in vitro. The Journal of Physiology. 1990;425:85–115. doi: 10.1113/jphysiol.1990.sp018094. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  105. Vander Heiden MG, Chandel NS, Williamson EK, Schumacker PT, Thompson CB. Bcl-xL regulates the membrane potential and volume homeostasis of mitochondria. Cell. 1997;91:627–637. doi: 10.1016/s0092-8674(00)80450-x. [DOI] [PubMed] [Google Scholar] · DOI
  106. Walker JE. The regulation of catalysis in ATP synthase. Current Opinion in Structural Biology. 1994;4:912–918. doi: 10.1016/0959-440x(94)90274-7. [DOI] [PubMed] [Google Scholar] · DOI
  107. Werth JL, Thayer SA. Mitochondria buffer physiological calcium loads in cultured rat dorsal root ganglion neurons. Journal of Neuroscience. 1994;14:348–356. doi: 10.1523/JNEUROSCI.14-01-00348.1994. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  108. White RJ, Reynolds IJ. Mitochondria and Na+/Ca2+ exchange buffer glutamate-induced calcium loads in cultured cortical neurons. Journal of Neuroscience. 1995;15:1318–1328. doi: 10.1523/JNEUROSCI.15-02-01318.1995. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  109. White RJ, Reynolds IJ. Mitochondria accumulate Ca2+ following intense glutamate stimulation of cultured rat forebrain neurones. The Journal of Physiology. 1997;498:31–47. doi: 10.1113/jphysiol.1997.sp021839. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  110. Zoratti M, Szabo I. The mitochondrial permeability transition. Biochimica et Biophysica Acta. 1995;1241:139–176. doi: 10.1016/0304-4157(95)00003-a. [DOI] [PubMed] [Google Scholar] · DOI

Cited by

Sorted by citations

Authors
Duchen, M. R.
Affiliations
University College London (GB)
Corresponding author
Duchen, Michael R.
ORCID
Duchen, Michael R.
Venue
The Journal of Physiology
Publisher
Wiley
Published
1999-04
Volume
516
Issue
1
Pages
1-17
ISSN
  • 0022-3751 (ISSN-L)
  • 1469-7793
DOI
10.1111/j.1469-7793.1999.001aa.x
PMC
PMC2269224
OpenAlex
W2080312195
Cited by
610
References
2
Citations by year
2026: 4 · 2025: 8 · 2024: 5 · 2023: 9 · 2022: 8 · 2021: 11 · 2020: 16 · 2019: 8 · 2018: 12 · 2017: 10 · 2016: 10 · 2015: 10 · 2014: 21 · 2013: 20 · 2012: 26
FWCI
4.07
Type
journal article
Language
en
Open access
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 1987 d)
Locations
  • The Journal of Physiology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Wellcome Trust
  • British Heart Foundation
  • Biotechnology and Biological Sciences Research Council
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords
mitochondria, animal physiology, glucose homeostasis, insulin secretion, pancreatic beta cells, appetite regulation, oxygen sensing, respiratory control, mitochondrial calcium uptake, calcium signaling, mitochondrial dysfunction, necrosis, apoptosis, ATP production
MeSH terms
Animals, Homeostasis, Humans, Mitochondria, Cell Death, Calcium Signaling

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review