메뉴 건너뛰기




Volumn 93, Issue 3, 2015, Pages 271-278

MitoTimer: a novel protein for monitoring mitochondrial turnover in the heart

Author keywords

Fluorescence microscopy; Mitochondrial biogenesis; Mitophagy; MitoTimer

Indexed keywords

MITOCHONDRIAL PROTEIN; MITOTIMER PROTEIN; UNCLASSIFIED DRUG; BIOLOGICAL MARKER; HYBRID PROTEIN; PHOTOPROTEIN;

EID: 84925483162     PISSN: 09462716     EISSN: 14321440     Source Type: Journal    
DOI: 10.1007/s00109-014-1230-6     Document Type: Review
Times cited : (43)

References (45)
  • 1
    • 0015239454 scopus 로고
    • The turnover of mitochondria in a variety of tissues of young adult and aged rats
    • COI: 1:CAS:528:DyaE3MXhtlOksro%3D, PID: 5553400
    • Menzies RA, Gold PH (1971) The turnover of mitochondria in a variety of tissues of young adult and aged rats. J Biol Chem 246(8):2425–2429
    • (1971) J Biol Chem , vol.246 , Issue.8 , pp. 2425-2429
    • Menzies, R.A.1    Gold, P.H.2
  • 2
    • 56849084137 scopus 로고    scopus 로고
    • Mitochondrial turnover in liver is fast in vivo and is accelerated by dietary restriction: application of a simple dynamic model
    • COI: 1:CAS:528:DC%2BD1cXhsFemt77E, PID: 18691181
    • Miwa S, Lawless C, Von Zglinicki T (2008) Mitochondrial turnover in liver is fast in vivo and is accelerated by dietary restriction: application of a simple dynamic model. Aging Cell 7(6):920–923
    • (2008) Aging Cell , vol.7 , Issue.6 , pp. 920-923
    • Miwa, S.1    Lawless, C.2    Von Zglinicki, T.3
  • 3
    • 84870713042 scopus 로고    scopus 로고
    • Metabolic labeling reveals proteome dynamics of mouse mitochondria
    • PID: 22915825
    • Kim TY et al (2012) Metabolic labeling reveals proteome dynamics of mouse mitochondria. Mol Cell Proteomics 11(12):1586–94
    • (2012) Mol Cell Proteomics , vol.11 , Issue.12 , pp. 1586-1594
    • Kim, T.Y.1
  • 4
    • 79954622220 scopus 로고    scopus 로고
    • Mitophagy selectively degrades individual damaged mitochondria after photoirradiation
    • Kim I, Lemasters JJ (2010) Mitophagy selectively degrades individual damaged mitochondria after photoirradiation. Antioxid Redox Signal 14(10):1919–1928
    • (2010) Antioxid Redox Signal , vol.14 , Issue.10 , pp. 1919-1928
    • Kim, I.1    Lemasters, J.J.2
  • 5
    • 0015090563 scopus 로고
    • Sterological measurements of cardiac ultrastructures implicated in excitation-contraction coupling
    • COI: 1:STN:280:DyaE3M3lsFyjug%3D%3D, PID: 5283936
    • Page E, McCallister LP, Power B (1971) Sterological measurements of cardiac ultrastructures implicated in excitation-contraction coupling. Proc Natl Acad Sci U S A 68(7):1465–1466
    • (1971) Proc Natl Acad Sci U S A , vol.68 , Issue.7 , pp. 1465-1466
    • Page, E.1    McCallister, L.P.2    Power, B.3
  • 6
    • 0031456762 scopus 로고    scopus 로고
    • The effect of delayed reperfusion following infarction in the rat on structural changes in viable myocardium
    • COI: 1:STN:280:DyaK1c7ps1emtg%3D%3D, PID: 9534855
    • McDonald K et al (1997) The effect of delayed reperfusion following infarction in the rat on structural changes in viable myocardium. Cardiovasc Res 36(3):347–353
    • (1997) Cardiovasc Res , vol.36 , Issue.3 , pp. 347-353
    • McDonald, K.1
  • 7
    • 0015090563 scopus 로고
    • Stereological measurements of cardiac ultrastructures implicated in excitation-contraction coupling
    • COI: 1:STN:280:DyaE3M3lsFyjug%3D%3D, PID: 5283936
    • Page E, McCallister LP, Power B (1971) Stereological measurements of cardiac ultrastructures implicated in excitation-contraction coupling. Proc Natl Acad Sci 68(7):1465–1466
    • (1971) Proc Natl Acad Sci , vol.68 , Issue.7 , pp. 1465-1466
    • Page, E.1    McCallister, L.P.2    Power, B.3
  • 8
    • 0014544519 scopus 로고
    • The ultrastructure of the cat myocardium. I. Ventricular papillary muscle
    • COI: 1:STN:280:DyaF1M3htVyqtg%3D%3D, PID: 4891913
    • Fawcett DW, McNutt NS (1969) The ultrastructure of the cat myocardium. I. Ventricular papillary muscle. J Cell Biol 42(1):1–45
    • (1969) J Cell Biol , vol.42 , Issue.1 , pp. 1-45
    • Fawcett, D.W.1    McNutt, N.S.2
  • 10
    • 0011017415 scopus 로고    scopus 로고
    • Kluwer Academic Publishers, Norwell:
    • Ingwall JS (2002) ATP and the heart. Kluwer Academic Publishers, Norwell
    • (2002) ATP and the heart
    • Ingwall, J.S.1
  • 11
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • COI: 1:CAS:528:DC%2BD1cXhtVKkurs%3D, PID: 18200046
    • Twig G et al (2008) Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J 27(2):433–446
    • (2008) EMBO J , vol.27 , Issue.2 , pp. 433-446
    • Twig, G.1
  • 12
    • 79952328398 scopus 로고    scopus 로고
    • Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease
    • COI: 1:CAS:528:DC%2BC3MXjs1Gks7g%3D, PID: 21209324
    • Bender T, Lewrenz I, Franken S, Baitzel C, Voos W (2011) Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease. Mol Biol Cell 22(5):541–554
    • (2011) Mol Biol Cell , vol.22 , Issue.5 , pp. 541-554
    • Bender, T.1    Lewrenz, I.2    Franken, S.3    Baitzel, C.4    Voos, W.5
  • 13
    • 84905694155 scopus 로고    scopus 로고
    • Circadian regulation of metabolism
    • COI: 1:CAS:528:DC%2BC2cXhsVChtrjI, PID: 24928941
    • Bailey SM, Udoh US, Young ME (2014) Circadian regulation of metabolism. J Endocrinol 222(2):R75–96
    • (2014) J Endocrinol , vol.222 , Issue.2 , pp. 75-96
    • Bailey, S.M.1    Udoh, U.S.2    Young, M.E.3
  • 14
    • 77953704724 scopus 로고    scopus 로고
    • Cyclophilin D is required for mitochondrial removal by autophagy in cardiac cells
    • COI: 1:CAS:528:DC%2BC3cXpvFWit7c%3D, PID: 20364102
    • Carreira RS, Lee Y, Ghochani M, Gustafsson AB, Gottlieb RA (2010) Cyclophilin D is required for mitochondrial removal by autophagy in cardiac cells. Autophagy 6(4):462–72
    • (2010) Autophagy , vol.6 , Issue.4 , pp. 462-472
    • Carreira, R.S.1    Lee, Y.2    Ghochani, M.3    Gustafsson, A.B.4    Gottlieb, R.A.5
  • 15
    • 79958172986 scopus 로고    scopus 로고
    • Preconditioning involves selective mitophagy mediated by Parkin and p62/SQSTM1
    • COI: 1:CAS:528:DC%2BC3MXns1yju7c%3D, PID: 21687634
    • Huang C et al (2011) Preconditioning involves selective mitophagy mediated by Parkin and p62/SQSTM1. PLoS One 6(6):e20975
    • (2011) PLoS One , vol.6 , Issue.6 , pp. 20975
    • Huang, C.1
  • 16
    • 79954622220 scopus 로고    scopus 로고
    • Mitophagy selectively degrades individual damaged mitochondria after photoirradiation
    • COI: 1:CAS:528:DC%2BC3MXkvVSqs70%3D, PID: 21126216
    • Kim I, Lemasters JJ (2011) Mitophagy selectively degrades individual damaged mitochondria after photoirradiation. Antioxid Redox Signal 14(10):1919–1928
    • (2011) Antioxid Redox Signal , vol.14 , Issue.10 , pp. 1919-1928
    • Kim, I.1    Lemasters, J.J.2
  • 17
    • 33749334061 scopus 로고    scopus 로고
    • Altered skeletal muscle subsarcolemmal mitochondrial compartment during catch-up fat after caloric restriction
    • COI: 1:CAS:528:DC%2BD28Xot1Oguro%3D, PID: 16873692
    • Crescenzo R et al (2006) Altered skeletal muscle subsarcolemmal mitochondrial compartment during catch-up fat after caloric restriction. Diabetes 55(8):2286–2293
    • (2006) Diabetes , vol.55 , Issue.8 , pp. 2286-2293
    • Crescenzo, R.1
  • 18
    • 68949150785 scopus 로고    scopus 로고
    • What can mitochondrial heterogeneity tell us about mitochondrial dynamics and autophagy?
    • COI: 1:CAS:528:DC%2BD1MXhtVentbjP, PID: 19549572
    • Wikstrom JD, Twig G, Shirihai OS (2009) What can mitochondrial heterogeneity tell us about mitochondrial dynamics and autophagy? Int J Biochem Cell Biol 41(10):1914–1927
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.10 , pp. 1914-1927
    • Wikstrom, J.D.1    Twig, G.2    Shirihai, O.S.3
  • 19
    • 27544510276 scopus 로고    scopus 로고
    • Inhibition of mitochondrial aldehyde dehydrogenase by nitric oxide-mediated S-nitrosylation
    • COI: 1:CAS:528:DC%2BD2MXhtFyktr3P, PID: 16242127
    • Moon K-H, Kim B-J, Song BJ (2005) Inhibition of mitochondrial aldehyde dehydrogenase by nitric oxide-mediated S-nitrosylation. FEBS Lett 579(27):6115–6120
    • (2005) FEBS Lett , vol.579 , Issue.27 , pp. 6115-6120
    • Moon, K.-H.1    Kim, B.-J.2    Song, B.J.3
  • 20
    • 0037029129 scopus 로고    scopus 로고
    • Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage
    • COI: 1:CAS:528:DC%2BD38XisFyru7c%3D, PID: 11943469
    • Paradies G, Petrosillo G, Pistolese M, Ruggiero FM (2002) Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage. Gene 286(1):135–141
    • (2002) Gene , vol.286 , Issue.1 , pp. 135-141
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 21
    • 0033803048 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma coactivator-1 promotes cardiac mitochondrial biogenesis
    • 7802877
    • Lehman JJ et al (2000) Peroxisome proliferator-activated receptor gamma coactivator-1 promotes cardiac mitochondrial biogenesis. J Clin Invest JID 7802877 106(7):847–856
    • (2000) J Clin Invest JID , vol.106 , Issue.7 , pp. 847-856
    • Lehman, J.J.1
  • 22
    • 42049114034 scopus 로고    scopus 로고
    • Transcriptional paradigms in mammalian mitochondrial biogenesis and function
    • COI: 1:CAS:528:DC%2BD1cXls1KhsLw%3D, PID: 18391175
    • Scarpulla RC (2008) Transcriptional paradigms in mammalian mitochondrial biogenesis and function. Physiol Rev 88(2):611–638
    • (2008) Physiol Rev , vol.88 , Issue.2 , pp. 611-638
    • Scarpulla, R.C.1
  • 23
    • 37549025047 scopus 로고    scopus 로고
    • A role for the transcriptional coactivator PGC-1α in muscle refueling
    • COI: 1:CAS:528:DC%2BD2sXhsVSgtrfN, PID: 17932032
    • Wende AR et al (2007) A role for the transcriptional coactivator PGC-1α in muscle refueling. J Biol Chem 282(50):36642–36651
    • (2007) J Biol Chem , vol.282 , Issue.50 , pp. 36642-36651
    • Wende, A.R.1
  • 24
    • 77951872309 scopus 로고    scopus 로고
    • Adiponectin and AdipoR1 regulate PGC-1alpha and mitochondria by Ca (2+) and AMPK/SIRT1
    • COI: 1:CAS:528:DC%2BC3cXktVGjt7Y%3D, PID: 20357764
    • Iwabu M et al (2010) Adiponectin and AdipoR1 regulate PGC-1alpha and mitochondria by Ca (2+) and AMPK/SIRT1. Nature 464(7293):1313–1319
    • (2010) Nature , vol.464 , Issue.7293 , pp. 1313-1319
    • Iwabu, M.1
  • 25
    • 70350500068 scopus 로고    scopus 로고
    • FoxO transcription factors promote autophagy in cardiomyocytes
    • COI: 1:CAS:528:DC%2BD1MXht1SqsbvP, PID: 19696026
    • Sengupta A, Molkentin JD, Yutzey KE (2009) FoxO transcription factors promote autophagy in cardiomyocytes. J Biol Chem 284(41):28319–28331
    • (2009) J Biol Chem , vol.284 , Issue.41 , pp. 28319-28331
    • Sengupta, A.1    Molkentin, J.D.2    Yutzey, K.E.3
  • 26
    • 79952303794 scopus 로고    scopus 로고
    • PARIS (ZNF746) repression of PGC-1alpha contributes to neurodegeneration in Parkinson’s disease
    • COI: 1:CAS:528:DC%2BC3MXjsFeqtrc%3D, PID: 21376232
    • Shin JH et al (2011) PARIS (ZNF746) repression of PGC-1alpha contributes to neurodegeneration in Parkinson’s disease. Cell 144(5):689–702
    • (2011) Cell , vol.144 , Issue.5 , pp. 689-702
    • Shin, J.H.1
  • 27
    • 76849100919 scopus 로고    scopus 로고
    • The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans
    • COI: 1:CAS:528:DC%2BC3cXlt1Kku7o%3D, PID: 20188671
    • Haynes CM, Yang Y, Blais SP, Neubert TA, Ron D (2010) The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. elegans. Mol Cell 37(4):529–540
    • (2010) Mol Cell , vol.37 , Issue.4 , pp. 529-540
    • Haynes, C.M.1    Yang, Y.2    Blais, S.P.3    Neubert, T.A.4    Ron, D.5
  • 28
    • 37849048003 scopus 로고    scopus 로고
    • Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements
    • PID: 17849004
    • Aldridge JE, Horibe T, Hoogenraad NJ (2007) Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements. PLoS One 2(9):e874
    • (2007) PLoS One , vol.2 , Issue.9 , pp. 874
    • Aldridge, J.E.1    Horibe, T.2    Hoogenraad, N.J.3
  • 29
    • 78649728763 scopus 로고    scopus 로고
    • The mitochondrial UPR—protecting organelle protein homeostasis
    • COI: 1:CAS:528:DC%2BC3cXhsF2jsL%2FP, PID: 21048161
    • Haynes CM, Ron D (2010) The mitochondrial UPR—protecting organelle protein homeostasis. J Cell Sci 123(Pt 22):3849–3855
    • (2010) J Cell Sci , vol.123 , pp. 3849-3855
    • Haynes, C.M.1    Ron, D.2
  • 31
    • 80052145606 scopus 로고    scopus 로고
    • A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery
    • COI: 1:CAS:528:DC%2BC3MXhtV2itLfP, PID: 21867919
    • Katayama H, Kogure T, Mizushima N, Yoshimori T, Miyawaki A (2011) A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery. Chem Biol 18(8):1042–1052
    • (2011) Chem Biol , vol.18 , Issue.8 , pp. 1042-1052
    • Katayama, H.1    Kogure, T.2    Mizushima, N.3    Yoshimori, T.4    Miyawaki, A.5
  • 32
    • 84899450022 scopus 로고    scopus 로고
    • A novel MitoTimer reporter gene for mitochondrial content, structure, stress, and damage in vivo
    • COI: 1:CAS:528:DC%2BC2cXmvVSgtrk%3D, PID: 24644293
    • Laker RC et al (2014) A novel MitoTimer reporter gene for mitochondrial content, structure, stress, and damage in vivo. J Biol Chem 289(17):12005–12015
    • (2014) J Biol Chem , vol.289 , Issue.17 , pp. 12005-12015
    • Laker, R.C.1
  • 33
    • 84887464529 scopus 로고    scopus 로고
    • MitoTimer: a novel tool for monitoring mitochondrial turnover
    • COI: 1:CAS:528:DC%2BC2cXhtVyiur3L, PID: 24128932
    • Hernandez G et al (2013) MitoTimer: a novel tool for monitoring mitochondrial turnover. Autophagy 9(11):1852–1861
    • (2013) Autophagy , vol.9 , Issue.11 , pp. 1852-1861
    • Hernandez, G.1
  • 34
    • 84887499718 scopus 로고    scopus 로고
    • MitoTimer probe reveals the impact of autophagy, fusion, and motility on subcellular distribution of young and old mitochondrial protein and on relative mitochondrial protein age
    • COI: 1:CAS:528:DC%2BC2cXhtVyiurrM, PID: 24149000
    • Ferree AW et al (2013) MitoTimer probe reveals the impact of autophagy, fusion, and motility on subcellular distribution of young and old mitochondrial protein and on relative mitochondrial protein age. Autophagy 9(11):1887–1896
    • (2013) Autophagy , vol.9 , Issue.11 , pp. 1887-1896
    • Ferree, A.W.1
  • 35
    • 0034711442 scopus 로고    scopus 로고
    • Fluorescent timer”: protein that changes color with time
    • COI: 1:CAS:528:DC%2BD3cXotl2kt70%3D, PID: 11090358
    • Terskikh A et al (2000) “Fluorescent timer”: protein that changes color with time. Science 290(5496):1585–1588
    • (2000) Science , vol.290 , Issue.5496 , pp. 1585-1588
    • Terskikh, A.1
  • 36
    • 79851486626 scopus 로고    scopus 로고
    • Age-dependent spatial segregation of synaptobrevin 2-containing vesicles in astrocytes
    • COI: 1:CAS:528:DC%2BC3MXjt1amtb0%3D, PID: 21214554
    • Loson OC, Ha CM, Parpura V (2011) Age-dependent spatial segregation of synaptobrevin 2-containing vesicles in astrocytes. J Neurochem 116(5):909–15
    • (2011) J Neurochem , vol.116 , Issue.5 , pp. 909-915
    • Loson, O.C.1    Ha, C.M.2    Parpura, V.3
  • 37
    • 33644893402 scopus 로고    scopus 로고
    • Elastic fiber formation: a dynamic view of extracellular matrix assembly using timer reporters
    • COI: 1:CAS:528:DC%2BD28XisFOjsrY%3D, PID: 16261592
    • Kozel BA et al (2006) Elastic fiber formation: a dynamic view of extracellular matrix assembly using timer reporters. J Cell Physiol 207(1):87–96
    • (2006) J Cell Physiol , vol.207 , Issue.1 , pp. 87-96
    • Kozel, B.A.1
  • 38
    • 0035839465 scopus 로고    scopus 로고
    • An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation
    • COI: 1:CAS:528:DC%2BD3MXmtFeitb4%3D, PID: 11408473
    • Verkhusha VV et al (2001) An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation. J Biol Chem 276(32):29621–29624
    • (2001) J Biol Chem , vol.276 , Issue.32 , pp. 29621-29624
    • Verkhusha, V.V.1
  • 39
    • 84901370753 scopus 로고    scopus 로고
    • Coxsackie virus B exits the host cell in shed microvesicles displaying autophagosomal markers
    • PID: 24722773
    • Robinson SM et al (2014) Coxsackie virus B exits the host cell in shed microvesicles displaying autophagosomal markers. PLoS Pathog 10(4):e1004045
    • (2014) PLoS Pathog , vol.10 , Issue.4 , pp. 1004045
    • Robinson, S.M.1
  • 40
    • 84871764874 scopus 로고    scopus 로고
    • Protein targeting to subcellular organelles via mRNA localization
    • COI: 1:CAS:528:DC%2BC38XmvFeqt7Y%3D, PID: 23457718
    • Weis BL, Schleiff E, Zerges W (2013) Protein targeting to subcellular organelles via mRNA localization. Biochim Biophys Acta 1833(2):260–273
    • (2013) Biochim Biophys Acta , vol.1833 , Issue.2 , pp. 260-273
    • Weis, B.L.1    Schleiff, E.2    Zerges, W.3
  • 41
    • 84857858536 scopus 로고    scopus 로고
    • Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons
    • COI: 1:CAS:528:DC%2BC38XjtV2hsLY%3D, PID: 22331844
    • Maday S, Wallace KE, Holzbaur EL (2012) Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons. J Cell Biol 196(4):407–417
    • (2012) J Cell Biol , vol.196 , Issue.4 , pp. 407-417
    • Maday, S.1    Wallace, K.E.2    Holzbaur, E.L.3
  • 42
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • COI: 1:CAS:528:DC%2BD2sXhtVehtbzE, PID: 17263664
    • Neupert W, Herrmann JM (2007) Translocation of proteins into mitochondria. Annu Rev Biochem 76(1):723–749
    • (2007) Annu Rev Biochem , vol.76 , Issue.1 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 43
    • 84899769902 scopus 로고    scopus 로고
    • Potential role of oxidative protein modification in energy metabolism in exercise
    • PID: 24374928
    • Aoi W, Naito Y, Yoshikawa T (2014) Potential role of oxidative protein modification in energy metabolism in exercise. Subcell Biochem 77:175–187
    • (2014) Subcell Biochem , vol.77 , pp. 175-187
    • Aoi, W.1    Naito, Y.2    Yoshikawa, T.3
  • 44
    • 34948890528 scopus 로고    scopus 로고
    • {Beta}-Cell mitochondria exhibit membrane potential heterogeneity that Can Be altered by stimulatory or toxic fuel levels
    • COI: 1:CAS:528:DC%2BD2sXhtFygt73N, PID: 17686943
    • Wikstrom JD et al (2007) {Beta}-Cell mitochondria exhibit membrane potential heterogeneity that Can Be altered by stimulatory or toxic fuel levels. Diabetes 56(10):2569–2578
    • (2007) Diabetes , vol.56 , Issue.10 , pp. 2569-2578
    • Wikstrom, J.D.1
  • 45
    • 84860705893 scopus 로고    scopus 로고
    • Mitochondrial DNA that escapes from autophagy causes inflammation and heart failure
    • COI: 1:CAS:528:DC%2BC38XmvVeqtbk%3D, PID: 22535248
    • Oka T et al (2012) Mitochondrial DNA that escapes from autophagy causes inflammation and heart failure. Nature 485(7397):251–255
    • (2012) Nature , vol.485 , Issue.7397 , pp. 251-255
    • Oka, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.