WordNet

make or undergo a transition (from one state or system to another); "The airline transitioned to more fuel-efficient jets"; "The adagio transitioned into an allegro"
a musical passage moving from one key to another (同)modulation
a change from one place or state or subject or stage to another
a passage that connects a topic to one that follows
cause to convert or undergo a transition; "the company had to transition the old practices to modern technology"
any tiny hole admitting passage of a liquid (fluid or gas)
any small opening in the skin or outer surface of an animal
the property of something that can be pervaded by a liquid (as by osmosis or diffusion) (同)permeableness

PrepTutorEJDIC

(…から…へ)移り変わること,変遷;(…から…への)過渡期《+from+名+to+名》
《pore over+名》(…を)熟読する,注意深く考える・没頭する, 熟考［熟視，熟読］する
気孔,毛穴
浸透性

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/02/15 14:03:58」(JST)

wiki en

Mitochondrial permeability transition pore is a protein that is formed in the inner membrane of the mitochondria under certain pathological conditions such as traumatic brain injury and stroke. Opening allows increase in the permeability of the mitochondrial membranes to molecules of less than 1500 Daltons in molecular weight. Induction of the permeability transition pore can lead to mitochondrial swelling and cell death through apoptosis or necrosis depending on the particular biological setting.^[1]

Roles in pathology

The MPTP was originally discovered by Haworth and Hunter^[2] in 1979 and has been found to be involved in neurodegeneration, hepatotoxicity from Reye-related agents, cardiac necrosis and nervous and muscular dystrophies among other deleterious events inducing cell damage and death.^[1]^[3]^[4]^[5]

MPT is one of the major causes of cell death in a variety of conditions. For example, it is key in neuronal cell death in excitotoxicity, in which overactivation of glutamate receptors causes excessive calcium entry into the cell.^[6]^[7]^[8] MPT also appears to play a key role in damage caused by ischemia, as occurs in a heart attack and stroke.^[9] However, research has shown that the MPT pore remains closed during ischemia, but opens once the tissues are reperfused with blood after the ischemic period,^[10] playing a role in reperfusion injury.

MPT is also thought to underlie the cell death induced by Reye's syndrome, since chemicals that can cause the syndrome, like salicylate and valproate, cause MPT.^[11] MPT may also play a role in mitochondrial autophagy.^[11] Cells exposed to toxic amounts of Ca²⁺ ionophores also undergo MPT and death by necrosis.^[11]

MPTP Structure

While the MPT modulation has been widely studied, little is known about its structure^[12] . Initial experiments by Szabó and Zoratti proposed the MPT may comprise Voltage Dependent Anion Channel (VDAC) molecules. Nevertheless, this hypothesis was shown to be incorrect as VDAC^−/− mitochondria were still capable to undergo MPT.^[13]^[14] Further hypothesis by Halestrap´s group convincingly suggested the MPT was formed by the inner membrane Adenine Nucleotide Translocase (ANT), but genetic ablation of such protein still led to MPT onset.^[15]^[16] Thus, the only MPTP components identified so far are the TSPO (previously known as the peripheral benzodiazepine receptor) located in the mitochondrial outer membrane and cyclophilin-D in the mitochondrial matrix.^[17]^[18] Mice lacking the gene for cyclophilin-D develop normally, but their cells do not undergo Cyclosporin A-sensitive MPT, and they are resistant to necrotic death from ischemia or overload of Ca²⁺ or free radicals.^[19] However, these cells do die in response to stimuli that kill cells through apoptosis, suggesting that MPT does not control cell death by apoptosis.^[19]

MPTP blockers

Agents that transiently block MPT include the immune suppressant cyclosporin A (CsA); N-methyl-Val-4-cyclosporin A (MeValCsA), a non-immunosuppressant derivative of CsA; another non-immunosuppressive agent, NIM811, 2-aminoethoxydiphenyl borate (2-APB),^[20] bongkrekic acid and alisporivir (also known as Debio-025). TRO40303 is a newly synthetitised MPT blocker developed by Trophos company and currently is in Phase I clinical trial.^[21] MPTP as target in cardioprotection. ^[22]

Factors in MPT induction

Various factors enhance the likelihood of MPTP opening. In some mitochondria, such as those in the central nervous system, high levels of Ca²⁺ within mitochondria can cause the MPT pore to open.^[23]^[24] This is possibly because Ca²⁺ binds to and activates Ca²⁺ binding sites on the matrix side of the MPTP.^[6] MPT induction is also due to the dissipation of the difference in voltage across the inner mitochondrial membrane (known as transmembrane potential, or Δψ). In neurons and astrocytes, the contribution of membrane potential to MPT induction is complex, see.^[25] The presence of free radicals, another result of excessive intracellular calcium concentrations, can also cause the MPT pore to open.^[26]

Other factors that increase the likelihood that the MPTP will be induced include the presence of certain fatty acids,^[27] and inorganic phosphate.^[28] However, these factors cannot open the pore without Ca²⁺, though at high enough concentrations, Ca²⁺ alone can induce MPT.^[29]

Stress in the endoplasmic reticulum can be a factor in triggering MPT.^[30]

Conditions that cause the pore to close or remain closed include acidic conditions,^[31] high concentrations of ADP,^[26]^[32] high concentrations of ATP,^[33] and high concentrations of NADH. Divalent cations like Mg²⁺ also inhibit MPT, because they can compete with Ca²⁺ for the Ca²⁺ binding sites on the matrix and/or cytoplasmic side of the MPTP.^[25]

Effects of MPT

Multiple studies have found the MPT to be a key factor in the damage to neurons caused by excitotoxicity.^[6]^[7]^[8]

The induction of MPT, which increases mitochondrial membrane permeability, causes mitochondria to become further depolarized, meaning that Δψ is abolished. When Δψ is lost, protons and some molecules are able to flow across the outer mitochondrial membrane uninhibited.^[7]^[8] Loss of Δψ interferes with the production of adenosine triphosphate (ATP), the cell's main source of energy, because mitochondria must have an electrochemical gradient to provide the driving force for ATP production.

In cell damage resulting from conditions such as neurodegenerative diseases and head injury, opening of the mitochondrial permeability transition pore can greatly reduce ATP production, and can cause ATP synthase to begin hydrolysing, rather than producing, ATP.^[34] This produces an energy deficit in the cell, just when it most needs ATP to fuel activity of ion pumps such as the Na⁺/Ca²⁺ exchanger, which must be activated more than under normal conditions in order to rid the cell of excess calcium.

MPT also allows Ca²⁺ to leave the mitochondrion, which can place further stress on nearby mitochondria, and which can activate harmful calcium-dependent proteases such as calpain.

Reactive oxygen species (ROS) are also produced as a result of opening the MPT pore. MPT can allow antioxidant molecules such as glutathione to exit mitochondria, reducing the organelles' ability to neutralize ROS. In addition, the electron transport chain (ETC) may produce more free radicals due to loss of components of the ETC, such as cytochrome c, through the MPTP.^[35] Loss of ETC components can lead to escape of electrons from the chain, which can then reduce molecules and form free radicals.

MPT causes mitochondria to become permeable to molecules smaller than 1.5 kDa, which, once inside, draw water in by increasing the organelle's osmolar load.^[36] This event may lead mitochondria to swell and may cause the outer membrane to rupture, releasing cytochrome c.^[36] Cytochrome c can in turn cause the cell to go through apoptosis ("commit suicide") by activating pro-apoptotic factors. Other researchers contend that it is not mitochondrial membrane rupture that leads to cytochrome c release, but rather another mechanism, such as translocation of the molecule through channels in the outer membrane, which does not involve the MPTP.^[37]

Much research has found that the fate of the cell after an insult depends on the extent of MPT. If MPT occurs to only a slight extent, the cell may recover, whereas if it occurs more it may undergo apoptosis. If it occurs to an even larger degree the cell is likely to undergo necrotic cell death.^[9]

Possible evolutionary purpose of the MPTP

Despite the MPTP has been studied mainly in mitochondria from mammalian sources, mitochondria from diverse species also undergo a similar transition.^[38] While its occurrence can be easily detected, its purpose still remains elusive. Some have speculated that the regulated opening of the MPT pore may minimize cell injury by causing ROS-producing mitochondria to undergo selective lysosome-dependent mitophagy during nutrient starvation conditions.^[39] Under severe stress/pathologic conditions, MPTP opening would trigger injured cell death mainly through necrosis.^[40]

There is controversy about the question of whether the MPTP is able to exist in a harmless, "low-conductance" state. This low-conductance state would not induce MPT^[6] and would allow certain molecules and ions to cross the mitochondrial membranes. The low-conductance state may allow small ions like Ca²⁺ to leave mitochondria quickly, in order to aid in the cycling of Ca²⁺ in healthy cells.^[32]^[41] If this is the case, MPT may be a harmful side effect of abnormal activity of a usually beneficial MPTP.

MPTP has been detected in mitochondria from plants,^[42] yeasts, such as Saccharomyces cerevisiae,^[43] birds, such as guinea fowl ^[44] and primitive vertebrates such as the Baltic lamprey.^[45] While the permeability transition is evident in mitochondria from these sources, its sensitivity to its classic modulators may differ when compared with mammalian mitochondria. Nevertheless, CsA-insensitive MPTP can be triggered in mammalian mitochondria given appropriate experimental conditions^[46] strongly suggesting this event may be a conserved characteristic throughout the eukaryotic domain.^[47]

References

^ ^a ^b Lemasters, J. J.; Theruvath, T. P.; Zhong, Z.; Nieminen, A. L. (2009). "Mitochondrial calcium and the permeability transition in cell death". Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1787 (11): 1395–1401. doi:10.1016/j.bbabio.2009.06.009. PMC 2730424. PMID 19576166.
^ Haworth, R. A.; Hunter, D. R. (1979). "The Ca2+-induced membrane transition in mitochondria. II. Nature of the Ca2+ trigger site". Archives of Biochemistry and Biophysics. 195 (2): 460–467. doi:10.1016/0003-9861(79)90372-2. PMID 38751.
^ Fiskum, G. (2000). "Mitochondrial participation in ischemic and traumatic neural cell death". Journal of Neurotrauma. 17 (10): 843–855. doi:10.1089/neu.2000.17.843. PMID 11063052.
^ Bernardi, P.; Bonaldo, P. (2008). "Dysfunction of Mitochondria and Sarcoplasmic Reticulum in the Pathogenesis of Collagen VI Muscular Dystrophies". Annals of the New York Academy of Sciences. 1147: 303–311. doi:10.1196/annals.1427.009. PMID 19076452.
^ Baines, C. P. (2010). "The Cardiac Mitochondrion: Nexus of Stress". Annual Review of Physiology. 72: 61–80. doi:10.1146/annurev-physiol-021909-135929. PMID 20148667.
^ ^a ^b ^c ^d Ichas, F.; Mazat, J. P. (1998). "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. 1366 (1–2): 33–50. doi:10.1016/S0005-2728(98)00119-4. PMID 9714722.
^ ^a ^b ^c Schinder, A. F.; Olson, E. C.; Spitzer, N. C.; Montal, M. (1996). "Mitochondrial dysfunction is a primary event in glutamate neurotoxicity". The Journal of Neuroscience. 16 (19): 6125–6133. PMID 8815895.
^ ^a ^b ^c White, R. J.; Reynolds, I. J. (1996). "Mitochondrial depolarization in glutamate-stimulated neurons: An early signal specific to excitotoxin exposure". The Journal of Neuroscience. 16 (18): 5688–5697. PMID 8795624.
^ ^a ^b Honda, H. M.; Ping, P. (2006). "Mitochondrial Permeability Transition in Cardiac Cell Injury and Death". Cardiovascular Drugs and Therapy. 20 (6): 425–432. doi:10.1007/s10557-006-0642-0. PMID 17171295.
^ Bopassa, J. C.; Michel, P.; Gateau-Roesch, O.; Ovize, M.; Ferrera, R. (2005). "Low-pressure reperfusion alters mitochondrial permeability transition". AJP: Heart and Circulatory Physiology. 288 (6): H2750–H2755. doi:10.1152/ajpheart.01081.2004. PMID 15653760.
^ ^a ^b ^c Lemasters, J. J.; Nieminen, A. L.; Qian, T.; Trost, L. C.; Elmore, S. P.; Nishimura, Y.; Crowe, R. A.; Cascio, W. E.; Bradham, C. A.; Brenner, D. A.; Herman, B. (1998). "The mitochondrial permeability transition in cell death: A common mechanism in necrosis, apoptosis and autophagy". Biochimica et Biophysica Acta. 1366 (1–2): 177–196. doi:10.1016/S0005-2728(98)00112-1. PMID 9714796.
^ Srinivasan, B. (2012). "Mitochondrial permeability transition pore: an enigmatic gatekeeper". New Horizons in Science & Technology (NHS&T). 1 (3): 47–51. ISSN 1929-2015.
^ Szabó, I.; Zoratti, M. (1993). "The mitochondrial permeability transition pore may comprise VDAC molecules. I. Binary structure and voltage dependence of the pore". FEBS Letters. 330 (2): 201–205. doi:10.1016/0014-5793(93)80273-w. PMID 7689983.
^ Baines, C. P.; Kaiser, R. A.; Sheiko, T.; Craigen, W. J.; Molkentin, J. D. (2007). "Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death". Nature Cell Biology. 9 (5): 550–555. doi:10.1038/ncb1575. PMC 2680246. PMID 17417626.
^ Kokoszka, J. E.; Waymire, K. G.; Levy, S. E.; Sligh, J. E.; Cai, J.; Jones, D. P.; MacGregor, G. R.; Wallace, D. C. (2004). "The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore". Nature. 427 (6973): 461–465. doi:10.1038/nature02229. PMC 3049806. PMID 14749836.
^ Varanyuwatana, P.; Halestrap, A. P. (2012). "The roles of phosphate and the phosphate carrier in the mitochondrial permeability transition pore". Mitochondrion. 12 (1): 120–125. doi:10.1016/j.mito.2011.04.006. PMC 3281194. PMID 21586347.
^ Sileikyte, J.; Petronilli, V.; Zulian, A.; Dabbeni-Sala, F.; Tognon, G.; Nikolov, P.; Bernardi, P.; Ricchelli, F. (2010). "Regulation of the Inner Membrane Mitochondrial Permeability Transition by the Outer Membrane Translocator Protein (Peripheral Benzodiazepine Receptor)". Journal of Biological Chemistry. 286 (2): 1046–1053. doi:10.1074/jbc.M110.172486. PMC 3020711. PMID 21062740.
^ Baines, C. P.; Kaiser, R. A.; Purcell, N. H.; Blair, N. S.; Osinska, H.; Hambleton, M. A.; Brunskill, E. W.; Sayen, M. R.; Gottlieb, R. A.; Dorn, G. W.; Robbins, J.; Molkentin, J. D. (2005). "Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death". Nature. 434 (7033): 658–662. doi:10.1038/nature03434. PMID 15800627.
^ ^a ^b Nakagawa, T.; Shimizu, S.; Watanabe, T.; Yamaguchi, O.; Otsu, K.; Yamagata, H.; Inohara, H.; Kubo, T.; Tsujimoto, Y. (2005). "Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death". Nature. 434 (7033): 652–658. doi:10.1038/nature03317. PMID 15800626.
^ Chinopoulos, C.; Starkov, A. A.; Fiskum, G. (2003). "Cyclosporin A-insensitive Permeability Transition in Brain Mitochondria: INHIBITION BY 2-AMINOETHOXYDIPHENYL BORATE". Journal of Biological Chemistry. 278 (30): 27382–27389. doi:10.1074/jbc.M303808200. PMID 12750371.
^ Le Lamer S (Feb 2014). "Translation of TRO40303 from myocardial infarction models to demonstration of safety and tolerance in a randomized Phase I trial.". J Transl Med. 12: 38. doi:10.1186/1479-5876-12-38. PMC 3923730. PMID 24507657.
^ Bernardi, J Mol Cell Cardiol 78:100 2015 http://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25268651/
^ Brustovetsky, N.; Brustovetsky, T.; Jemmerson, R.; Dubinsky, J. M. (2002). "Calcium-induced cytochrome c release from CNS mitochondria is associated with the permeability transition and rupture of the outer membrane". Journal of Neurochemistry. 80 (2): 207–218. doi:10.1046/j.0022-3042.2001.00671.x. PMID 11902111.
^ Hunter, D. R.; Haworth, R. A. (1979). "The Ca2+-induced membrane transition in mitochondria. I. The protective mechanisms". Archives of Biochemistry and Biophysics. 195 (2): 453–459. doi:10.1016/0003-9861(79)90371-0. PMID 383019.
^ ^a ^b Doczi, J.; Turiák, L.; Vajda, S.; Mándi, M.; Töröcsik, B.; Gerencser, A. A.; Kiss, G.; Konràd, C.; Adam-Vizi, V.; Chinopoulos, C. (2010). "Complex Contribution of Cyclophilin D to Ca2+-induced Permeability Transition in Brain Mitochondria, with Relation to the Bioenergetic State". Journal of Biological Chemistry. 286 (8): 6345–6353. doi:10.1074/jbc.M110.196600. PMC 3057831. PMID 21173147.
^ ^a ^b Brustovetsky, N.; Brustovetsky, T.; Purl, K. J.; Capano, M.; Crompton, M.; Dubinsky, J. M. (2003). "Increased susceptibility of striatal mitochondria to calcium-induced permeability transition". The Journal of Neuroscience. 23 (12): 4858–4867. PMID 12832508.
^ García-Ruiz, C.; Colell, A.; París, R.; Fernández-Checa, J. C. (2000). "Direct interaction of GD3 ganglioside with mitochondria generates reactive oxygen species followed by mitochondrial permeability transition, cytochrome c release, and caspase activation". FASEB Journal. 14 (7): 847–858. PMID 10783138.
^ Nicholls, D. G.; Brand, M. D. (1980). "The nature of the calcium ion efflux induced in rat liver mitochondria by the oxidation of endogenous nicotinamide nucleotides". The Biochemical Journal. 188 (1): 113–118. doi:10.1042/bj1880113. PMC 1162544. PMID 7406874.
^ Gunter, T. E.; Gunter, K. K.; Sheu, S. S.; Gavin, C. E. (1994). "Mitochondrial calcium transport: Physiological and pathological relevance". The American journal of physiology. 267 (2 Pt 1): C313–C339. PMID 8074170.
^ Deniaud, A.; Sharaf El Dein, O.; Maillier, E.; Poncet, D.; Kroemer, G.; Lemaire, C.; Brenner, C. (2007). "Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis". Oncogene. 27 (3): 285–299. doi:10.1038/sj.onc.1210638. PMID 17700538.
^ Friberg, H.; Wieloch, T. (2002). "Mitochondrial permeability transition in acute neurodegeneration". Biochimie. 84 (2–3): 241–250. doi:10.1016/s0300-9084(02)01381-0. PMID 12022955.
^ ^a ^b Hunter, D. R.; Haworth, R. A. (1979). "The Ca2+-induced membrane transition in mitochondria. III. Transitional Ca2+ release". Archives of Biochemistry and Biophysics. 195 (2): 468–477. doi:10.1016/0003-9861(79)90373-4. PMID 112926.
^ Beutner, G.; Rück, 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". Biochimica et Biophysica Acta. 1368 (1): 7–18. doi:10.1016/s0005-2736(97)00175-2. PMID 9459579.
^ Stavrovskaya, I. G.; Kristal, B. S. (2005). "The powerhouse takes control of the cell: Is the mitochondrial permeability transition a viable therapeutic target against neuronal dysfunction and death?". Free Radical Biology and Medicine. 38 (6): 687–697. doi:10.1016/j.freeradbiomed.2004.11.032. PMID 15721979.
^ Luetjens, C. M.; Bui, N. T.; Sengpiel, B.; Münstermann, G.; Poppe, M.; Krohn, A. J.; Bauerbach, E.; Krieglstein, J.; Prehn, J. H. (2000). "Delayed mitochondrial dysfunction in excitotoxic neuron death: Cytochrome c release and a secondary increase in superoxide production". The Journal of Neuroscience. 20 (15): 5715–5723. PMID 10908611.
^ ^a ^b Büki, A.; Okonkwo, D. O.; Wang, K. K.; Povlishock, J. T. (2000). "Cytochrome c release and caspase activation in traumatic axonal injury". The Journal of Neuroscience. 20 (8): 2825–2834. PMID 10751434.
^ Priault, M.; Chaudhuri, B.; Clow, A.; Camougrand, N.; Manon, S. (1999). "Investigation of bax-induced release of cytochrome c from yeast mitochondria permeability of mitochondrial membranes, role of VDAC and ATP requirement". European Journal of Biochemistry / FEBS. 260 (3): 684–691. doi:10.1046/j.1432-1327.1999.00198.x. PMID 10102996.
^ Azzolin, L.; Von Stockum, S.; Basso, E.; Petronilli, V.; Forte, M. A.; Bernardi, P. (2010). "The mitochondrial permeability transition from yeast to mammals". FEBS Letters. 584 (12): 2504–2509. doi:10.1016/j.febslet.2010.04.023. PMC 2878904. PMID 20398660.
^ Kim, I.; Rodriguez-Enriquez, S.; Lemasters, J. J. (2007). "Selective degradation of mitochondria by mitophagy". Archives of Biochemistry and Biophysics. 462 (2): 245–253. doi:10.1016/j.abb.2007.03.034. PMC 2756107. PMID 17475204.
^ Haworth RA and Hunter DR. 2001. Ca²⁺-induced transition in mitochondria: A cellular catastrophe? Chapter 6 In Mitochondria in pathogenesis. Lemasters JJ and Nieminen AL, eds. Kluwer Academic/Plenum Publishers. New York. Pages 115 - 124.
^ Altschuld, R. A.; Hohl, C. M.; Castillo, L. C.; Garleb, A. A.; Starling, R. C.; Brierley, G. P. (1992). "Cyclosporin inhibits mitochondrial calcium efflux in isolated adult rat ventricular cardiomyocytes". The American journal of physiology. 262 (6 Pt 2): H1699–H1704. PMID 1377876.
^ Curtis, M. J.; Wolpert, T. J. (2002). "The oat mitochondrial permeability transition and its implication in victorin binding and induced cell death". The Plant Journal. 29 (3): 295–312. doi:10.1046/j.0960-7412.2001.01213.x. PMID 11844107.
^ Jung, D. W.; Bradshaw, P. C.; Pfeiffer, D. R. (1997). "Properties of a Cyclosporin-insensitive Permeability Transition Pore in Yeast Mitochondria". Journal of Biological Chemistry. 272 (34): 21104–21112. doi:10.1074/jbc.272.34.21104. PMID 9261114.
^ Vedernikov, A. A.; Dubinin, M. V.; Zabiakin, V. A.; Samartsev, V. N. (2015). "Ca²⁺-dependent nonspecific permeability of the inner membrane of liver mitochondria in the guinea fowl (Numida meleagris)". Journal of Bioenergetics and Biomembranes. 47 (3): 235–242. doi:10.1007/s10863-015-9606-z. PMID 25690874.
^ Savina, M. V.; Emelyanova, L. V.; Belyaeva, E. A. (2006). "Bioenergetic parameters of lamprey and frog liver mitochondria during metabolic depression and activity". Comparative Biochemistry and Physiology B. 145 (3–4): 296–305. doi:10.1016/j.cbpb.2006.07.011. PMID 17070716.
^ García, N.; Martínez-Abundis, E.; Pavón, N.; Chávez, E. (2007). "On the Opening of an Insensitive Cyclosporin a Non-specific Pore by Phenylarsine Plus Mersalyl". Cell Biochemistry and Biophysics. 49 (2): 84–90. doi:10.1007/s12013-007-0047-0. PMID 17906363.
^ Uribe-Carvajal, S.; Luévano-Martínez, L. S. A.; Guerrero-Castillo, S.; Cabrera-Orefice, A.; Corona-De-La-Peña, N. A.; Gutiérrez-Aguilar, M. (2011). "Mitochondrial Unselective Channels throughout the eukaryotic domain". Mitochondrion. 11 (3): 382–390. doi:10.1016/j.mito.2011.02.004. PMID 21385626.

External links

Mitochondrial permeability transition pore: an enigmatic gatekeeper (2012) NHS&T, Vol 1(3):47-51
Mitochondrial Permeability Transition (PT) from Celldeath.de. Accessed January 1, 2007.
mitochondrial permeability transition pore at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 虚血プレコンディショニングの定義および病因 definition and pathogenesis of ischemic preconditioning
2. 心臓の虚血性再潅流障害 ischemic reperfusion injury of the heart
3. パーキンソン病の病因および発症機序 etiology and pathogenesis of parkinson disease
4. 外科手術で使用される再建材料：分類および宿主応答 reconstructive materials used in surgery classification and host response
5. 肝性脳症：病因 hepatic encephalopathy pathogenesis

English Journal

Mitochondrial Ca(2+) influx and efflux rates in guinea pig cardiac mitochondria:Low and high affinity effects of cyclosporine A.

Wei AC, Liu T, Cortassa S, Winslow RL, O'Rourke B.SourceDepartment of Biomedical Engineering, Institute of Computational Medicine, The Johns Hopkins University, Baltimore MD 21205-2195, USA.
Biochimica et biophysica acta.Biochim Biophys Acta.2011 Jul;1813(7):1373-81. Epub 2011 Feb 26.
Ca(2+) plays a central role in energy supply and demand matching in cardiomyocytes by transmitting changes in excitation-contraction coupling to mitochondrial oxidative phosphorylation. Matrix Ca(2+) is controlled primarily by the mitochondrial Ca(2+) uniporter and the mitochondrial Na(+)/Ca(2+) exc
PMID 21362444