메뉴 건너뛰기




Volumn 584, Issue 10, 2010, Pages 1942-1947

Mitochondrial Ca2+ channels: Great unknowns with important functions

Author keywords

Calcium signaling; ER Ca2+ release; Grp75; IP3 receptor; Letm1; MCa1; MCa2; MCU; MiCa; Mitochondrial Ca2+ uniporter; Mitofusin; P38MAPK; UCP2 3; Uncoupling protein

Indexed keywords

ANTIPORTER; CALCIUM CHANNEL; CALCIUM ION; CALCIUM PROTON EXCHANGE PROTEIN; GLYCOPROTEIN; MITOCHONDRIAL CALCIUM CHANNEL; UNCLASSIFIED DRUG; UNCOUPLING PROTEIN 2; UNCOUPLING PROTEIN 3; CALCIUM;

EID: 77952723041     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.01.010     Document Type: Review
Times cited : (32)

References (99)
  • 1
    • 4043086952 scopus 로고    scopus 로고
    • Mitochondria in health and disease: perspectives on a new mitochondrial biology
    • Duchen M.R. Mitochondria in health and disease: perspectives on a new mitochondrial biology. Mol. Aspects Med. 2004, 25:365-451.
    • (2004) Mol. Aspects Med. , vol.25 , pp. 365-451
    • Duchen, M.R.1
  • 2
    • 35448983147 scopus 로고    scopus 로고
    • Mitochondria and Ca2+ signaling: old guests, new functions
    • Graier W.F., Frieden M., Malli R. Mitochondria and Ca2+ signaling: old guests, new functions. Pflugers Arch. 2007, 455:375-396.
    • (2007) Pflugers Arch. , vol.455 , pp. 375-396
    • Graier, W.F.1    Frieden, M.2    Malli, R.3
  • 4
    • 56349133547 scopus 로고    scopus 로고
    • Positioning mitochondrial plasticity within cellular signaling cascades
    • Soubannier V., McBride H. Positioning mitochondrial plasticity within cellular signaling cascades. Biochim. Biophys. Acta 2008, 1793:154-170.
    • (2008) Biochim. Biophys. Acta , vol.1793 , pp. 154-170
    • Soubannier, V.1    McBride, H.2
  • 5
    • 0035853040 scopus 로고    scopus 로고
    • Circularly permuted green fluorescent proteins engineered to sense Ca2+
    • Nagai T., Sawano A., Park E.S., Miyawaki A. Circularly permuted green fluorescent proteins engineered to sense Ca2+. Proc. Natl. Acad. Sci. USA 2001, 98:3197-3202.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3197-3202
    • Nagai, T.1    Sawano, A.2    Park, E.S.3    Miyawaki, A.4
  • 6
    • 0026659512 scopus 로고
    • Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin
    • Rizzuto R., Simpson A.W., Brini M., Pozzan T. Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin. Nature 1992, 358:325-327.
    • (1992) Nature , vol.358 , pp. 325-327
    • Rizzuto, R.1    Simpson, A.W.2    Brini, M.3    Pozzan, T.4
  • 7
    • 0041534404 scopus 로고    scopus 로고
    • Ca2+ signalling in mitochondria: mechanism and role in physiology and pathology
    • Brini M. Ca2+ signalling in mitochondria: mechanism and role in physiology and pathology. Cell Calcium 2003, 34:399-405.
    • (2003) Cell Calcium , vol.34 , pp. 399-405
    • Brini, M.1
  • 8
    • 23744440457 scopus 로고    scopus 로고
    • Mitochondrial Ca2+ homeostasis in health and disease
    • Campanella M., Pinton P., Rizzuto R. Mitochondrial Ca2+ homeostasis in health and disease. Biol. Res. 2004, 37:653-660.
    • (2004) Biol. Res. , vol.37 , pp. 653-660
    • Campanella, M.1    Pinton, P.2    Rizzuto, R.3
  • 9
    • 42049090126 scopus 로고    scopus 로고
    • Mitochondria: the hub of cellular Ca2+ signaling
    • Szabadkai G., Duchen M.R. Mitochondria: the hub of cellular Ca2+ signaling. Physiology 2008, 23:84-94.
    • (2008) Physiology , vol.23 , pp. 84-94
    • Szabadkai, G.1    Duchen, M.R.2
  • 10
    • 0034668833 scopus 로고    scopus 로고
    • Mitochondria and calcium: from cell signalling to cell death
    • Duchen M.R. Mitochondria and calcium: from cell signalling to cell death. J. Physiol. 2000, 529:57-68.
    • (2000) J. Physiol. , vol.529 , pp. 57-68
    • Duchen, M.R.1
  • 11
    • 0016294206 scopus 로고
    • The influence of respiration and ATP hydrolysis on the proton-electrochemical gradient across the inner membrane of rat-liver mitochondria as determined by ion distribution
    • Nicholls D.G. The influence of respiration and ATP hydrolysis on the proton-electrochemical gradient across the inner membrane of rat-liver mitochondria as determined by ion distribution. Eur. J. Biochem. 1974, 50:305-315.
    • (1974) Eur. J. Biochem. , vol.50 , pp. 305-315
    • Nicholls, D.G.1
  • 12
    • 0037395951 scopus 로고    scopus 로고
    • Historical review: mitochondria and calcium: ups and downs of an unusual relationship
    • Carafoli E. Historical review: mitochondria and calcium: ups and downs of an unusual relationship. Trends Biochem. Sci. 2003, 28:175-181.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 175-181
    • Carafoli, E.1
  • 13
    • 0018363365 scopus 로고
    • The effects of calcium ions and adenine nucleotides on the activity of pig heart 2-oxoglutarate dehydrogenase complex
    • McCormack J.G., Denton R.M. The effects of calcium ions and adenine nucleotides on the activity of pig heart 2-oxoglutarate dehydrogenase complex. Biochem. J. 1979, 180:533-544.
    • (1979) Biochem. J. , vol.180 , pp. 533-544
    • McCormack, J.G.1    Denton, R.M.2
  • 14
    • 0021289002 scopus 로고
    • Role of Ca2+ ions in the regulation of intramitochondrial metabolism in rat heart. Evidence from studies with isolated mitochondria that adrenaline activates the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes by increasing the intramitochondrial concentration of Ca2+
    • McCormack J.G., Denton R.M. Role of Ca2+ ions in the regulation of intramitochondrial metabolism in rat heart. Evidence from studies with isolated mitochondria that adrenaline activates the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes by increasing the intramitochondrial concentration of Ca2+. Biochem. J. 1984, 218:235-247.
    • (1984) Biochem. J. , vol.218 , pp. 235-247
    • McCormack, J.G.1    Denton, R.M.2
  • 15
    • 0025319665 scopus 로고
    • Role of calcium ions in regulation of mammalian intramitochondrial metabolism
    • McCormack J.G., Halestrap A.P., Denton R.M. Role of calcium ions in regulation of mammalian intramitochondrial metabolism. Physiol. Rev. 1990, 70:391-425.
    • (1990) Physiol. Rev. , vol.70 , pp. 391-425
    • McCormack, J.G.1    Halestrap, A.P.2    Denton, R.M.3
  • 17
    • 0033598828 scopus 로고    scopus 로고
    • Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming
    • Jouaville L.S., Pinton P., Bastianutto C., Rutter G.A., Rizzuto R. Regulation of mitochondrial ATP synthesis by calcium: evidence for a long-term metabolic priming. Proc. Natl. Acad. Sci. USA 1999, 96:13807-13812.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13807-13812
    • Jouaville, L.S.1    Pinton, P.2    Bastianutto, C.3    Rutter, G.A.4    Rizzuto, R.5
  • 18
    • 0037518121 scopus 로고    scopus 로고
    • Mitochondria efficiently buffer subplasmalemmal Ca2+ elevation during agonist stimulation
    • Malli R., Frieden M., Osibow K., Graier W.F. Mitochondria efficiently buffer subplasmalemmal Ca2+ elevation during agonist stimulation. J. Biol. Chem. 2003, 278:10807-10815.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10807-10815
    • Malli, R.1    Frieden, M.2    Osibow, K.3    Graier, W.F.4
  • 19
    • 13444282233 scopus 로고    scopus 로고
    • The spatial pattern of atrial cardiomyocyte calcium signalling modulates contraction
    • Mackenzie L., Roderick H.L., Berridge M.J., Conway S.J., Bootman M.D. The spatial pattern of atrial cardiomyocyte calcium signalling modulates contraction. J. Cell Sci. 2004, 117:6327-6337.
    • (2004) J. Cell Sci. , vol.117 , pp. 6327-6337
    • Mackenzie, L.1    Roderick, H.L.2    Berridge, M.J.3    Conway, S.J.4    Bootman, M.D.5
  • 20
    • 39549112572 scopus 로고    scopus 로고
    • Polarized calcium signaling in exocrine gland cells
    • Petersen O.H., Tepikin A.V. Polarized calcium signaling in exocrine gland cells. Annu. Rev. Physiol. 2008, 70:273-299.
    • (2008) Annu. Rev. Physiol. , vol.70 , pp. 273-299
    • Petersen, O.H.1    Tepikin, A.V.2
  • 21
    • 0035800813 scopus 로고    scopus 로고
    • Mitochondria recycle Ca2+ to the endoplasmic reticulum and prevent the depletion of neighboring endoplasmic reticulum regions
    • Arnaudeau S., Kelley W.L., Walsh J.V., Demaurex N. Mitochondria recycle Ca2+ to the endoplasmic reticulum and prevent the depletion of neighboring endoplasmic reticulum regions. J. Biol. Chem. 2001, 276:29430-29439.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29430-29439
    • Arnaudeau, S.1    Kelley, W.L.2    Walsh, J.V.3    Demaurex, N.4
  • 22
    • 16844385280 scopus 로고    scopus 로고
    • The role of mitochondria for Ca2+ refilling of the ER
    • Malli R., Frieden M., Trenker M., Graier W.F. The role of mitochondria for Ca2+ refilling of the ER. J. Biol. Chem. 2005, 280:12114-12122.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12114-12122
    • Malli, R.1    Frieden, M.2    Trenker, M.3    Graier, W.F.4
  • 23
    • 59849120392 scopus 로고    scopus 로고
    • Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
    • Michalak M., Groenendyk J., Szabo E., Gold L.I., Opas M. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem. J. 2009, 417:651-666.
    • (2009) Biochem. J. , vol.417 , pp. 651-666
    • Michalak, M.1    Groenendyk, J.2    Szabo, E.3    Gold, L.I.4    Opas, M.5
  • 24
    • 0032216661 scopus 로고    scopus 로고
    • Calreticulin, a multifunctional Ca2+ binding chaperone of the endoplasmic reticulum
    • Michalak M., Mariani P., Opas M. Calreticulin, a multifunctional Ca2+ binding chaperone of the endoplasmic reticulum. Biochem. Cell Biol. 1998, 76:779-785.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 779-785
    • Michalak, M.1    Mariani, P.2    Opas, M.3
  • 25
    • 0036877146 scopus 로고    scopus 로고
    • Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • Michalak M., Robert Parker J.M., Opas M. Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 2002, 32:269-278.
    • (2002) Cell Calcium , vol.32 , pp. 269-278
    • Michalak, M.1    Robert Parker, J.M.2    Opas, M.3
  • 26
    • 33646806797 scopus 로고    scopus 로고
    • Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum
    • Osibow K., Frank S., Malli R., Zechner R., Graier W.F. Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum. Biochem. J. 2006, 396:173-182.
    • (2006) Biochem. J. , vol.396 , pp. 173-182
    • Osibow, K.1    Frank, S.2    Malli, R.3    Zechner, R.4    Graier, W.F.5
  • 27
    • 54949110895 scopus 로고    scopus 로고
    • Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis
    • Pinton P., Giorgi C., Siviero R., Zecchini E., Rizzuto R. Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis. Oncogene 2008, 27:6407-6418.
    • (2008) Oncogene , vol.27 , pp. 6407-6418
    • Pinton, P.1    Giorgi, C.2    Siviero, R.3    Zecchini, E.4    Rizzuto, R.5
  • 28
    • 56249094217 scopus 로고    scopus 로고
    • Calcium, mitochondria and apoptosis studied by fluorescence measurements
    • Roy S.S., Hajnóczky G. Calcium, mitochondria and apoptosis studied by fluorescence measurements. Methods 2008, 46:213-223.
    • (2008) Methods , vol.46 , pp. 213-223
    • Roy, S.S.1    Hajnóczky, G.2
  • 30
    • 0018269944 scopus 로고
    • The regulation of extramitochondrial free calcium ion concentration by rat liver mitochondria
    • Nicholls D.G. The regulation of extramitochondrial free calcium ion concentration by rat liver mitochondria. Biochem. J. 1978, 176:463-474.
    • (1978) Biochem. J. , vol.176 , pp. 463-474
    • Nicholls, D.G.1
  • 31
    • 24644462789 scopus 로고    scopus 로고
    • Mitochondria and calcium signaling
    • Nicholls D.G. Mitochondria and calcium signaling. Cell Calcium 2005, 38:311-317.
    • (2005) Cell Calcium , vol.38 , pp. 311-317
    • Nicholls, D.G.1
  • 32
    • 0024804336 scopus 로고
    • Calcium ion transport in mitochondria
    • Saris N.E., Allshire A. Calcium ion transport in mitochondria. Methods Enzymol. 1989, 174:68-85.
    • (1989) Methods Enzymol. , vol.174 , pp. 68-85
    • Saris, N.E.1    Allshire, A.2
  • 33
    • 17144417734 scopus 로고    scopus 로고
    • A historical review of cellular calcium handling, with emphasis on mitochondria
    • Saris N.E., Carafoli E. A historical review of cellular calcium handling, with emphasis on mitochondria. Biochemistry (Mosc) 2005, 70:187-194.
    • (2005) Biochemistry (Mosc) , vol.70 , pp. 187-194
    • Saris, N.E.1    Carafoli, E.2
  • 34
    • 33745186921 scopus 로고    scopus 로고
    • Ca2+-dependent control of the permeability properties of the mitochondrial outer membrane and voltage-dependent anion-selective channel (VDAC)
    • Bathori G., Csordas G., Garcia-Perez C., Davies E., Hajnoczky G. Ca2+-dependent control of the permeability properties of the mitochondrial outer membrane and voltage-dependent anion-selective channel (VDAC). J. Biol. Chem. 2006, 281:17347-17358.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17347-17358
    • Bathori, G.1    Csordas, G.2    Garcia-Perez, C.3    Davies, E.4    Hajnoczky, G.5
  • 35
    • 0035881510 scopus 로고    scopus 로고
    • Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function
    • Gincel D., Zaid H., Shoshan-Barmatz V. Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function. Biochem. J. 2001, 358:147-155.
    • (2001) Biochem. J. , vol.358 , pp. 147-155
    • Gincel, D.1    Zaid, H.2    Shoshan-Barmatz, V.3
  • 36
    • 0036877961 scopus 로고    scopus 로고
    • Old players in a new role: mitochondria-associated membranes, VDAC, and ryanodine receptors as contributors to calcium signal propagation from endoplasmic reticulum to the mitochondria
    • Hajnoczky G., Csordas G., Yi M. Old players in a new role: mitochondria-associated membranes, VDAC, and ryanodine receptors as contributors to calcium signal propagation from endoplasmic reticulum to the mitochondria. Cell Calcium 2002, 32:363-377.
    • (2002) Cell Calcium , vol.32 , pp. 363-377
    • Hajnoczky, G.1    Csordas, G.2    Yi, M.3
  • 38
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 1999, 341:233-249.
    • (1999) Biochem. J. , vol.341 , pp. 233-249
    • Crompton, M.1
  • 40
    • 0034525413 scopus 로고    scopus 로고
    • VDAC regulation by the Bcl-2 family of proteins
    • Tsujimoto Y., Shimizu S. VDAC regulation by the Bcl-2 family of proteins. Cell Death Differ. 2000, 7:1174-1181.
    • (2000) Cell Death Differ. , vol.7 , pp. 1174-1181
    • Tsujimoto, Y.1    Shimizu, S.2
  • 41
    • 0036479011 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: an essential player in apoptosis
    • Tsujimoto Y., Shimizu S. The voltage-dependent anion channel: an essential player in apoptosis. Biochimie 2002, 84:187-193.
    • (2002) Biochimie , vol.84 , pp. 187-193
    • Tsujimoto, Y.1    Shimizu, S.2
  • 42
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: channels, exchangers, and permeability transition
    • Bernardi P. Mitochondrial transport of cations: channels, exchangers, and permeability transition. Physiol. Rev. 1999, 79:1127-1155.
    • (1999) Physiol. Rev. , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 43
    • 55549085893 scopus 로고    scopus 로고
    • UCP2/3 - likely to be fundamental for mitochondrial Ca2+ uniport
    • Trenker M., Fertschai I., Malli R., Graier W.F. UCP2/3 - likely to be fundamental for mitochondrial Ca2+ uniport. Nat. Cell Biol. 2008, 10:1237-1240.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1237-1240
    • Trenker, M.1    Fertschai, I.2    Malli, R.3    Graier, W.F.4
  • 45
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y., Krapivinsky G., Clapham D.E. The mitochondrial calcium uniporter is a highly selective ion channel. Nature 2004, 427:360-364.
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 46
    • 0021759404 scopus 로고
    • Pathway for uncoupler-induced calcium efflux in rat liver mitochondria: inhibition by ruthenium red
    • Bernardi P., Paradisi V., Pozzan T., Azzone G.F. Pathway for uncoupler-induced calcium efflux in rat liver mitochondria: inhibition by ruthenium red. Biochemistry 1984, 23:1645-1651.
    • (1984) Biochemistry , vol.23 , pp. 1645-1651
    • Bernardi, P.1    Paradisi, V.2    Pozzan, T.3    Azzone, G.F.4
  • 47
    • 0016246085 scopus 로고
    • The inhibition of mitochondrial calcium transport by lanthanides and ruthenium red
    • Reed K.C., Bygrave F.L. The inhibition of mitochondrial calcium transport by lanthanides and ruthenium red. Biochem. J. 1974, 140:143-155.
    • (1974) Biochem. J. , vol.140 , pp. 143-155
    • Reed, K.C.1    Bygrave, F.L.2
  • 48
    • 22144479425 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial calcium uniporter by the oxo-bridged dinuclear ruthenium amine complex (Ru360) prevents from irreversible injury in postischemic rat heart
    • de Jesús García-Rivas G., Guerrero-Hernández A., Guerrero-Serna G., Rodríguez-Zavala J.S., Zazueta C. Inhibition of the mitochondrial calcium uniporter by the oxo-bridged dinuclear ruthenium amine complex (Ru360) prevents from irreversible injury in postischemic rat heart. FEBS J. 2005, 272:3477-3488.
    • (2005) FEBS J. , vol.272 , pp. 3477-3488
    • de Jesús García-Rivas, G.1    Guerrero-Hernández, A.2    Guerrero-Serna, G.3    Rodríguez-Zavala, J.S.4    Zazueta, C.5
  • 50
    • 68649096360 scopus 로고    scopus 로고
    • Regulation of plasma membrane calcium fluxes by mitochondria
    • Demaurex N., Poburko D., Frieden M. Regulation of plasma membrane calcium fluxes by mitochondria. Biochim. Biophys. Acta 2009, 1787:1383-1394.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1383-1394
    • Demaurex, N.1    Poburko, D.2    Frieden, M.3
  • 53
    • 0017119234 scopus 로고
    • Specific inhibition of mitochondrial Ca2+ transport by antibodies directed to the Ca2+-binding glycoprotein
    • Panfili E., Sandri G., Sottocasa G.L., Lunazzi G., Liut G., Graziosi G. Specific inhibition of mitochondrial Ca2+ transport by antibodies directed to the Ca2+-binding glycoprotein. Nature 1976, 264:185-186.
    • (1976) Nature , vol.264 , pp. 185-186
    • Panfili, E.1    Sandri, G.2    Sottocasa, G.L.3    Lunazzi, G.4    Liut, G.5    Graziosi, G.6
  • 54
    • 0034518449 scopus 로고    scopus 로고
    • Mitochondria and Ca2+ in cell physiology and pathophysiology
    • Duchen M.R. Mitochondria and Ca2+ in cell physiology and pathophysiology. Cell Calcium 2000, 28:339-348.
    • (2000) Cell Calcium , vol.28 , pp. 339-348
    • Duchen, M.R.1
  • 55
  • 56
    • 34249092704 scopus 로고    scopus 로고
    • Calcium and neurodegeneration
    • Mattson M.P. Calcium and neurodegeneration. Aging Cell 2007, 6:337-350.
    • (2007) Aging Cell , vol.6 , pp. 337-350
    • Mattson, M.P.1
  • 57
    • 33744492597 scopus 로고    scopus 로고
    • Mitochondrial Ca2+ transport, permeability transition and oxidative stress in cell death: implications in cardiotoxicity, neurodegeneration and dyslipidemias
    • Vercesi A.E., Kowaltowski A.J., Oliveira H.C.F., Castilho R.F. Mitochondrial Ca2+ transport, permeability transition and oxidative stress in cell death: implications in cardiotoxicity, neurodegeneration and dyslipidemias. Front. Biosci. 2006, 11:2554-2564.
    • (2006) Front. Biosci. , vol.11 , pp. 2554-2564
    • Vercesi, A.E.1    Kowaltowski, A.J.2    Oliveira, H.C.F.3    Castilho, R.F.4
  • 58
    • 34247598856 scopus 로고    scopus 로고
    • Endothelial mitochondria: contributing to vascular function and disease
    • Davidson S.M., Duchen M.R. Endothelial mitochondria: contributing to vascular function and disease. Circ. Res. 2007, 100:1128-1141.
    • (2007) Circ. Res. , vol.100 , pp. 1128-1141
    • Davidson, S.M.1    Duchen, M.R.2
  • 59
    • 67650688732 scopus 로고    scopus 로고
    • Regulation of mitochondrial Ca2+ and its effects on energetics and redox balance in normal and failing heart
    • Liu T., O'Rourke B. Regulation of mitochondrial Ca2+ and its effects on energetics and redox balance in normal and failing heart. J. Bioenerg. Biomembr. 2009, 41:127-132.
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 127-132
    • Liu, T.1    O'Rourke, B.2
  • 60
    • 39049106146 scopus 로고    scopus 로고
    • Mitocans: mitochondrial targeted anti-cancer drugs as improved therapies and related patent documents
    • Ralph S.J., Low P., Dong L., Lawen A., Neuzil J. Mitocans: mitochondrial targeted anti-cancer drugs as improved therapies and related patent documents. Recent Pat. Anti-cancer Drug Discov. 2006, 1:327-346.
    • (2006) Recent Pat. Anti-cancer Drug Discov. , vol.1 , pp. 327-346
    • Ralph, S.J.1    Low, P.2    Dong, L.3    Lawen, A.4    Neuzil, J.5
  • 62
    • 0032466538 scopus 로고    scopus 로고
    • Advances in the purification of the mitochondrial Ca2+ uniporter using the labeled inhibitor 103Ru360
    • Zazueta C., Zafra G., Vera G., Sanchez C., Chavez E. Advances in the purification of the mitochondrial Ca2+ uniporter using the labeled inhibitor 103Ru360. J. Bioenerg. Biomembr. 1998, 30:489-498.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 489-498
    • Zazueta, C.1    Zafra, G.2    Vera, G.3    Sanchez, C.4    Chavez, E.5
  • 63
    • 0036584365 scopus 로고    scopus 로고
    • Uncoupling proteins and thermoregulation
    • Argyropoulos G., Harper M.-E. Uncoupling proteins and thermoregulation. J. Appl. Physiol. 2002, 92:2187-2198.
    • (2002) J. Appl. Physiol. , vol.92 , pp. 2187-2198
    • Argyropoulos, G.1    Harper, M.-E.2
  • 64
    • 33745615380 scopus 로고    scopus 로고
    • The physiological regulation of uncoupling proteins
    • Nicholls D.G. The physiological regulation of uncoupling proteins. Biochim. Biophys. Acta 2006, 1757:459-466.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 459-466
    • Nicholls, D.G.1
  • 65
    • 38449115596 scopus 로고    scopus 로고
    • Novel uncoupling proteins. Novartis Found Symp. 287, discussion 80-91.
    • Affourtit, C., Crichton, P.G., Parker, N. and Brand, M.D. (2007). Novel uncoupling proteins. Novartis Found Symp. 287, 70-80; discussion 80-91.
    • (2007) , pp. 70-80
    • Affourtit, C.1    Crichton, P.G.2    Parker, N.3    Brand, M.D.4
  • 67
    • 0033379826 scopus 로고    scopus 로고
    • UCP1: the original uncoupling protein-and perhaps the only one? New perspectives on UCP1, UCP2, and UCP3 in the light of the bioenergetics of the UCP1-ablated mice
    • Nedergaard J., Matthias A., Golozoubova V., Jacobsson A., Cannon B. UCP1: the original uncoupling protein-and perhaps the only one? New perspectives on UCP1, UCP2, and UCP3 in the light of the bioenergetics of the UCP1-ablated mice. J. Bioenerg. Biomembr. 1999, 31:475-491.
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 475-491
    • Nedergaard, J.1    Matthias, A.2    Golozoubova, V.3    Jacobsson, A.4    Cannon, B.5
  • 68
    • 0037253404 scopus 로고    scopus 로고
    • The " novel" uncoupling proteins UCP2 and UCP3: what do they really do? Pros and cons for suggested functions
    • Nedergaard J., Cannon B. The " novel" uncoupling proteins UCP2 and UCP3: what do they really do? Pros and cons for suggested functions. Exp. Physiol. 2003, 88:65-84.
    • (2003) Exp. Physiol. , vol.88 , pp. 65-84
    • Nedergaard, J.1    Cannon, B.2
  • 70
    • 70349669093 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter
    • Jiang D., Zhao L., Clapham D.E. Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter. Science 2009, 326:144-147.
    • (2009) Science , vol.326 , pp. 144-147
    • Jiang, D.1    Zhao, L.2    Clapham, D.E.3
  • 72
    • 19444366152 scopus 로고    scopus 로고
    • Electroneutral K+/H+ exchange in mitochondrial membrane vesicles involves Yol027/Letm1 proteins
    • Froschauer E., Nowikovsky K., Schweyen R.J. Electroneutral K+/H+ exchange in mitochondrial membrane vesicles involves Yol027/Letm1 proteins. Biochim. Biophys. Acta 2005, 1711:41-48.
    • (2005) Biochim. Biophys. Acta , vol.1711 , pp. 41-48
    • Froschauer, E.1    Nowikovsky, K.2    Schweyen, R.J.3
  • 73
    • 44749086938 scopus 로고    scopus 로고
    • Mitochondrial Ca2+, the secret behind the function of uncoupling proteins 2 and 3?
    • Graier W.F., Trenker M., Malli R. Mitochondrial Ca2+, the secret behind the function of uncoupling proteins 2 and 3?. Cell Calcium 2008, 44:36-50.
    • (2008) Cell Calcium , vol.44 , pp. 36-50
    • Graier, W.F.1    Trenker, M.2    Malli, R.3
  • 74
    • 44749086506 scopus 로고    scopus 로고
    • Mitochondrial regulation of store-operated CRAC channels
    • Parekh A.B. Mitochondrial regulation of store-operated CRAC channels. Cell Calcium 2008, 44:6-13.
    • (2008) Cell Calcium , vol.44 , pp. 6-13
    • Parekh, A.B.1
  • 75
    • 0033429387 scopus 로고    scopus 로고
    • The mitochondrial permeability transition and the calcium, oxygen and pH paradoxes: one paradox after another
    • Lemasters J.J. The mitochondrial permeability transition and the calcium, oxygen and pH paradoxes: one paradox after another. Cardiovasc. Res. 1999, 44:470-473.
    • (1999) Cardiovasc. Res. , vol.44 , pp. 470-473
    • Lemasters, J.J.1
  • 77
    • 67349285823 scopus 로고    scopus 로고
    • The molecular composition of the mitochondrial permeability transition pore
    • Baines C.P. The molecular composition of the mitochondrial permeability transition pore. J. Mol. Cell Cardiol. 2009, 46:850-857.
    • (2009) J. Mol. Cell Cardiol. , vol.46 , pp. 850-857
    • Baines, C.P.1
  • 80
    • 0037175393 scopus 로고    scopus 로고
    • Recombinant expression of the voltage-dependent anion channel enhances the transfer of Ca2+ microdomains to mitochondria
    • Rapizzi E., et al. Recombinant expression of the voltage-dependent anion channel enhances the transfer of Ca2+ microdomains to mitochondria. J. Cell Biol. 2002, 159:613-624.
    • (2002) J. Cell Biol. , vol.159 , pp. 613-624
    • Rapizzi, E.1
  • 81
    • 33845692166 scopus 로고    scopus 로고
    • Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
    • Szabadkai G., et al. Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels. J. Cell Biol. 2006, 175:901-911.
    • (2006) J. Cell Biol. , vol.175 , pp. 901-911
    • Szabadkai, G.1
  • 82
    • 68649115556 scopus 로고    scopus 로고
    • Ca2+ transfer from the ER to mitochondria: when, how and why
    • Rizzuto R., et al. Ca2+ transfer from the ER to mitochondria: when, how and why. Biochim. Biophys. Acta 2009, 1787:1342-1351.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1342-1351
    • Rizzuto, R.1
  • 84
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • de Brito O.M., Scorrano L. Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 2008, 456:605-610.
    • (2008) Nature , vol.456 , pp. 605-610
    • de Brito, O.M.1    Scorrano, L.2
  • 85
    • 33749022800 scopus 로고    scopus 로고
    • Structural and functional features and significance of the physical linkage between ER and mitochondria
    • Csordas G., et al. Structural and functional features and significance of the physical linkage between ER and mitochondria. J. Cell Biol. 2006, 174:915-921.
    • (2006) J. Cell Biol. , vol.174 , pp. 915-921
    • Csordas, G.1
  • 86
    • 0036884142 scopus 로고    scopus 로고
    • A novel regulatory mechanism of the mitochondrial Ca2+ uniporter revealed by the p38 mitogen-activated protein kinase inhibitor SB202190
    • Montero M., Lobaton C.D., Moreno A., Alvarez J. A novel regulatory mechanism of the mitochondrial Ca2+ uniporter revealed by the p38 mitogen-activated protein kinase inhibitor SB202190. FASEB J. 2002, 16:1955-1957.
    • (2002) FASEB J. , vol.16 , pp. 1955-1957
    • Montero, M.1    Lobaton, C.D.2    Moreno, A.3    Alvarez, J.4
  • 87
    • 0346749523 scopus 로고    scopus 로고
    • Modulation of histamine-induced Ca2+ release by protein kinase C: effects on cytosolic and mitochondrial [Ca2+] peaks
    • Montero M., Lobaton C.D., Gutierrez-Fernandez S., Moreno A., Alvarez J. Modulation of histamine-induced Ca2+ release by protein kinase C: effects on cytosolic and mitochondrial [Ca2+] peaks. J. Biol. Chem. 2003, 278:49972-49979.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49972-49979
    • Montero, M.1    Lobaton, C.D.2    Gutierrez-Fernandez, S.3    Moreno, A.4    Alvarez, J.5
  • 89
    • 39149139316 scopus 로고    scopus 로고
    • Participation of p38 MAPK and a novel-type protein kinase C in the control of mitochondrial Ca2+ uptake
    • Szanda G., Koncz P., Rajki A., Spät A. Participation of p38 MAPK and a novel-type protein kinase C in the control of mitochondrial Ca2+ uptake. Cell Calcium 2008, 43:250-259.
    • (2008) Cell Calcium , vol.43 , pp. 250-259
    • Szanda, G.1    Koncz, P.2    Rajki, A.3    Spät, A.4
  • 90
    • 68249162449 scopus 로고    scopus 로고
    • Mitochondrial Ca2+ uptake is inhibited by a concerted action of p38 MAPK and protein kinase D
    • Koncz P., Szanda G., Fülöp L., Rajki A., Spät A. Mitochondrial Ca2+ uptake is inhibited by a concerted action of p38 MAPK and protein kinase D. Cell Calcium 2009, 46:122-129.
    • (2009) Cell Calcium , vol.46 , pp. 122-129
    • Koncz, P.1    Szanda, G.2    Fülöp, L.3    Rajki, A.4    Spät, A.5
  • 91
    • 57449087643 scopus 로고    scopus 로고
    • When is high-Ca2+ microdomain required for mitochondrial Ca+ uptake?
    • Spät A., Fülöp L., Koncz P., Szanda G. When is high-Ca2+ microdomain required for mitochondrial Ca+ uptake?. Acta Physiol. (Oxf) 2009, 195:139-147.
    • (2009) Acta Physiol. (Oxf) , vol.195 , pp. 139-147
    • Spät, A.1    Fülöp, L.2    Koncz, P.3    Szanda, G.4
  • 92
    • 2142707179 scopus 로고    scopus 로고
    • Long-term modulation of mitochondrial Ca2+ signals by protein kinase C isozymes
    • Pinton P., Leo S., Wieckowski M.R., Di Benedetto G., Rizzuto R. Long-term modulation of mitochondrial Ca2+ signals by protein kinase C isozymes. J. Cell Biol. 2004, 165:223-232.
    • (2004) J. Cell Biol. , vol.165 , pp. 223-232
    • Pinton, P.1    Leo, S.2    Wieckowski, M.R.3    Di Benedetto, G.4    Rizzuto, R.5
  • 93
    • 0022928283 scopus 로고
    • Ca2+ ions, an allosteric activator of calcium uptake in rat liver mitochondria
    • Kröner H. Ca2+ ions, an allosteric activator of calcium uptake in rat liver mitochondria. Arch. Biochem. Biophys. 1986, 251:525-535.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 525-535
    • Kröner, H.1
  • 94
    • 55549110813 scopus 로고    scopus 로고
    • UCPs - unlikely calcium porters
    • Brookes P.S., et al. UCPs - unlikely calcium porters. Nat. Cell Biol. 2008, 10:1235-1237.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1235-1237
    • Brookes, P.S.1
  • 95
    • 33747176845 scopus 로고    scopus 로고
    • Biphasic regulation of mitochondrial Ca2+ uptake by cytosolic Ca2+ concentration
    • Moreau B., Nelson C., Parekh A.B. Biphasic regulation of mitochondrial Ca2+ uptake by cytosolic Ca2+ concentration. Curr. Biol. 2006, 16:1672-1677.
    • (2006) Curr. Biol. , vol.16 , pp. 1672-1677
    • Moreau, B.1    Nelson, C.2    Parekh, A.B.3
  • 96
    • 0142149115 scopus 로고    scopus 로고
    • Plasticity of mitochondrial calcium signaling
    • Csordas G., Hajnoczky G. Plasticity of mitochondrial calcium signaling. J. Biol. Chem. 2003, 278:42273-42282.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42273-42282
    • Csordas, G.1    Hajnoczky, G.2
  • 97
    • 44349138089 scopus 로고    scopus 로고
    • Ca2+-dependent inactivation of the mitochondrial Ca2+ uniporter involves proton flux through the ATP synthase
    • Moreau B., Parekh A.B. Ca2+-dependent inactivation of the mitochondrial Ca2+ uniporter involves proton flux through the ATP synthase. Curr. Biol. 2008, 18:855-859.
    • (2008) Curr. Biol. , vol.18 , pp. 855-859
    • Moreau, B.1    Parekh, A.B.2
  • 98
    • 0035795178 scopus 로고    scopus 로고
    • The rapid mode of calcium uptake into heart mitochondria (RaM): comparison to RaM in liver mitochondria
    • Buntinas L., Gunter K.K., Sparagna G.C., Gunter T.E. The rapid mode of calcium uptake into heart mitochondria (RaM): comparison to RaM in liver mitochondria. Biochim. Biophys. Acta 2001, 1504:248-261.
    • (2001) Biochim. Biophys. Acta , vol.1504 , pp. 248-261
    • Buntinas, L.1    Gunter, K.K.2    Sparagna, G.C.3    Gunter, T.E.4
  • 99
    • 0028865759 scopus 로고
    • Mitochondrial calcium uptake from physiological-type pulses of calcium. A description of the rapid uptake mode
    • Sparagna G.C., Gunter K.K., Sheu S.S., Gunter T.E. Mitochondrial calcium uptake from physiological-type pulses of calcium. A description of the rapid uptake mode. J. Biol. Chem. 1995, 270:27510-27515.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27510-27515
    • Sparagna, G.C.1    Gunter, K.K.2    Sheu, S.S.3    Gunter, T.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.