메뉴 건너뛰기




Volumn 287, Issue 53, 2012, Pages 44109-44120

Rescue of PINK1 protein null-specific mitochondrial complex IV deficits by ginsenoside Re activation of nitric oxide signaling

Author keywords

[No Author keywords available]

Indexed keywords

ALLYLAMINO; CO-EXPRESSION; DRUG SCREENING; GELDANAMYCIN; GINSENOSIDE RE; METHYL ESTERS; MITOCHONDRIAL COMPLEX; MITOCHONDRIAL DYSFUNCTION; MITOCHONDRIAL FUNCTION; NEURONAL CELL; NITRIC OXIDE SIGNALING; OVER-EXPRESSION; PARKINSON'S DISEASE; PHARMACOLOGICAL EFFECTS;

EID: 84871748170     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.408146     Document Type: Article
Times cited : (36)

References (48)
  • 1
    • 84857969901 scopus 로고    scopus 로고
    • Targeting mitochondria for neuroprotection in Parkinson's disease
    • Schapira, A. H. (2012) Targeting mitochondria for neuroprotection in Parkinson's disease. Antioxid. Redox Signal. 16, 965-973
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 965-973
    • Schapira, A.H.1
  • 3
    • 33750220194 scopus 로고    scopus 로고
    • C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1
    • Sim, C. H., Lio, D. S., Mok, S. S., Masters, C. L., Hill, A. F., Culvenor, J. G., and Cheng, H. C. (2006) C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1. Hum. Mol. Genet. 15, 3251-3262
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 3251-3262
    • Sim, C.H.1    Lio, D.S.2    Mok, S.S.3    Masters, C.L.4    Hill, A.F.5    Culvenor, J.G.6    Cheng, H.C.7
  • 4
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D., Tanaka, A., Suen, D. F., and Youle, R. J. (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 183, 795-803
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 5
    • 44349195101 scopus 로고    scopus 로고
    • Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery
    • Yang, Y., Ouyang, Y., Yang, L., Beal, M. F., McQuibban, A., Vogel, H., and Lu, B. (2008) Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery. Proc. Natl. Acad. Sci. U.S.A. 105, 7070-7075
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7070-7075
    • Yang, Y.1    Ouyang, Y.2    Yang, L.3    Beal, M.F.4    McQuibban, A.5    Vogel, H.6    Lu, B.7
  • 6
    • 79961207215 scopus 로고    scopus 로고
    • The antioxidant Trolox helps recovery from the familial Parkinson's disease-specific mitochondrial deficits caused by PINK1- and DJ-1-deficiency in dopaminergic neuronal cells
    • Shim, J. H., Yoon, S. H., Kim, K. H., Han, J. Y., Ha, J. Y., Hyun, D. H., Paek, S. H., Kang, U. J., Zhuang, X., and Son, J. H. (2011) The antioxidant Trolox helps recovery from the familial Parkinson's disease-specific mitochondrial deficits caused by PINK1- and DJ-1-deficiency in dopaminergic neuronal cells. Mitochondrion 11, 707-715
    • (2011) Mitochondrion , vol.11 , pp. 707-715
    • Shim, J.H.1    Yoon, S.H.2    Kim, K.H.3    Han, J.Y.4    Ha, J.Y.5    Hyun, D.H.6    Paek, S.H.7    Kang, U.J.8    Zhuang, X.9    Son, J.H.10
  • 7
    • 62749113469 scopus 로고    scopus 로고
    • Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells
    • Gegg, M. E., Cooper, J. M., Schapira, A. H., and Taanman, J. W. (2009) Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells. PloS ONE 4, e4756
    • (2009) PloS ONE , vol.4
    • Gegg, M.E.1    Cooper, J.M.2    Schapira, A.H.3    Taanman, J.W.4
  • 9
    • 56349099660 scopus 로고    scopus 로고
    • Suppression mechanisms of COX assembly defects in yeast and human. Insights into the COX assembly process
    • Barrientos, A., Gouget, K., Horn, D., Soto, I. C., and Fontanesi, F. (2009) Suppression mechanisms of COX assembly defects in yeast and human. Insights into the COX assembly process. Biochim. Biophys. Acta 1793, 97-107
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 97-107
    • Barrientos, A.1    Gouget, K.2    Horn, D.3    Soto, I.C.4    Fontanesi, F.5
  • 10
    • 71849115876 scopus 로고    scopus 로고
    • Cytochrome c oxidase deficiency. Patients and animal models
    • Diaz, F. (2010) Cytochrome c oxidase deficiency. Patients and animal models. Biochim. Biophys. Acta 1802, 100-110
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 100-110
    • Diaz, F.1
  • 11
    • 77953871095 scopus 로고    scopus 로고
    • Assembly factors and ATP-dependent proteases in cytochrome c oxidase biogenesis
    • Stiburek, L., and Zeman, J. (2010) Assembly factors and ATP-dependent proteases in cytochrome c oxidase biogenesis. Biochim. Biophys. Acta 1797, 1149-1158
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1149-1158
    • Stiburek, L.1    Zeman, J.2
  • 18
    • 77956012154 scopus 로고    scopus 로고
    • Nitric oxide and neuronal death
    • Brown, G. C. (2010) Nitric oxide and neuronal death. Nitric Oxide 23, 153-165
    • (2010) Nitric Oxide , vol.23 , pp. 153-165
    • Brown, G.C.1
  • 19
    • 68149169007 scopus 로고    scopus 로고
    • What is the real physiological NO concentration in vivo?
    • Hall, C. N., and Garthwaite, J. (2009) What is the real physiological NO concentration in vivo? Nitric Oxide 21, 92-103
    • (2009) Nitric Oxide , vol.21 , pp. 92-103
    • Hall, C.N.1    Garthwaite, J.2
  • 21
    • 0023940538 scopus 로고
    • Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor cells results in L-arginine-dependent inhibition of mitochondrial iron-sulfur enzymes in the macrophage effector cells
    • Drapier, J. C., and Hibbs, J. B., Jr. (1988) Differentiation of murine macrophages to express nonspecific cytotoxicity for tumor cells results in L-arginine-dependent inhibition of mitochondrial iron-sulfur enzymes in the macrophage effector cells. J. Immunol. 140, 2829-2838
    • (1988) J. Immunol. , vol.140 , pp. 2829-2838
    • Drapier, J.C.1    Hibbs Jr., J.B.2
  • 22
    • 24144494527 scopus 로고    scopus 로고
    • The physiology and pathophysiology of nitric oxide in the brain
    • Guix, F. X., Uribesalgo, I., Coma, M., and Muñoz, F. J. (2005) The physiology and pathophysiology of nitric oxide in the brain. Prog. Neurobiol. 76, 126-152
    • (2005) Prog. Neurobiol. , vol.76 , pp. 126-152
    • Guix, F.X.1    Uribesalgo, I.2    Coma, M.3    Muñoz, F.J.4
  • 23
    • 0025117611 scopus 로고
    • EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages
    • Lancaster, J. R., Jr., and Hibbs, J. B., Jr. (1990) EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages. Proc. Natl. Acad. Sci. U.S.A. 87, 1223-1227
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 1223-1227
    • Lancaster Jr., J.R.1    Hibbs Jr., J.B.2
  • 24
    • 0029033427 scopus 로고
    • Nitric oxide produced by activated astrocytes rapidly and reversibly inhibits cellular respiration
    • Brown, G. C., Bolaños, J. P., Heales, S. J., and Clark, J. B. (1995) Nitric oxide produced by activated astrocytes rapidly and reversibly inhibits cellular respiration. Neurosci. Lett. 193, 201-204
    • (1995) Neurosci. Lett. , vol.193 , pp. 201-204
    • Brown, G.C.1    Bolaños, J.P.2    Heales, S.J.3    Clark, J.B.4
  • 25
    • 0028865420 scopus 로고
    • Nitric oxide. An important signaling mechanism between vascular endothelium and parenchymal cells in the regulation of oxygen consumption
    • Shen, W., Hintze, T. H., and Wolin, M. S. (1995) Nitric oxide. An important signaling mechanism between vascular endothelium and parenchymal cells in the regulation of oxygen consumption. Circulation 92, 3505-3512
    • (1995) Circulation , vol.92 , pp. 3505-3512
    • Shen, W.1    Hintze, T.H.2    Wolin, M.S.3
  • 29
    • 33846890205 scopus 로고    scopus 로고
    • Neuroprotective effects of ginsenoside-Rg1 in primary nigral neurons against rotenone toxicity
    • Leung, K. W., Yung, K. K., Mak, N. K., Chan, Y. S., Fan, T. P., and Wong, R. N. (2007) Neuroprotective effects of ginsenoside-Rg1 in primary nigral neurons against rotenone toxicity. Neuropharmacology 52, 827-835
    • (2007) Neuropharmacology , vol.52 , pp. 827-835
    • Leung, K.W.1    Yung, K.K.2    Mak, N.K.3    Chan, Y.S.4    Fan, T.P.5    Wong, R.N.6
  • 30
    • 36849043044 scopus 로고    scopus 로고
    • Ginsenosides. Are any of them candidates for drugs acting on the central nervous system?
    • Nah, S. Y., Kim, D. H., and Rhim, H. (2007) Ginsenosides. Are any of them candidates for drugs acting on the central nervous system? CNS Drug Rev. 13, 381-404
    • (2007) CNS Drug Rev. , vol.13 , pp. 381-404
    • Nah, S.Y.1    Kim, D.H.2    Rhim, H.3
  • 31
    • 64549087639 scopus 로고    scopus 로고
    • 20(S)-ginsenoside Rg3, a neuroprotective agent, inhibits mitochondrial permeability transition pores in rat brain
    • Tian, J., Zhang, S., Li, G., Liu, Z., and Xu, B. (2009) 20(S)-ginsenoside Rg3, a neuroprotective agent, inhibits mitochondrial permeability transition pores in rat brain. Phytother. Res. 23, 486-491
    • (2009) Phytother. Res. , vol.23 , pp. 486-491
    • Tian, J.1    Zhang, S.2    Li, G.3    Liu, Z.4    Xu, B.5
  • 32
    • 79952005057 scopus 로고    scopus 로고
    • Ginsenoside Rd attenuates mitochondrial dysfunction and sequential apoptosis after transient focal ischemia
    • Ye, R., Zhang, X., Kong, X., Han, J., Yang, Q., Zhang, Y., Chen, Y., Li, P., Liu, J., Shi, M., Xiong, L., and Zhao, G. (2011) Ginsenoside Rd attenuates mitochondrial dysfunction and sequential apoptosis after transient focal ischemia. Neuroscience 178, 169-180
    • (2011) Neuroscience , vol.178 , pp. 169-180
    • Ye, R.1    Zhang, X.2    Kong, X.3    Han, J.4    Yang, Q.5    Zhang, Y.6    Chen, Y.7    Li, P.8    Liu, J.9    Shi, M.10    Xiong, L.11    Zhao, G.12
  • 33
    • 0032937111 scopus 로고    scopus 로고
    • Neuroprotection and neuronal differentiation studies using substantia nigra dopaminergic cells derived from transgenic mouse embryos
    • Son, J. H., Chun, H. S., Joh, T. H., Cho, S., Conti, B., and Lee, J. W. (1999) Neuroprotection and neuronal differentiation studies using substantia nigra dopaminergic cells derived from transgenic mouse embryos. J. Neurosci. 19, 10-20
    • (1999) J. Neurosci. , vol.19 , pp. 10-20
    • Son, J.H.1    Chun, H.S.2    Joh, T.H.3    Cho, S.4    Conti, B.5    Lee, J.W.6
  • 34
    • 79955688677 scopus 로고    scopus 로고
    • Development of a rapid and convenient method to separate eight ginsenosides from Panax ginseng by high-speed counter-current chromatography coupled with evaporative light scattering detection
    • Shehzad, O., Ha, I. J., Park, Y., Ha, Y. W., and Kim, Y. S. (2011) Development of a rapid and convenient method to separate eight ginsenosides from Panax ginseng by high-speed counter-current chromatography coupled with evaporative light scattering detection. J. Sep. Sci. 34, 1116-1122
    • (2011) J. Sep. Sci. , vol.34 , pp. 1116-1122
    • Shehzad, O.1    Ha, I.J.2    Park, Y.3    Ha, Y.W.4    Kim, Y.S.5
  • 35
    • 0037428164 scopus 로고    scopus 로고
    • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70
    • Young, J. C., Hoogenraad, N. J., and Hartl, F. U. (2003) Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell 112, 41-50
    • (2003) Cell , vol.112 , pp. 41-50
    • Young, J.C.1    Hoogenraad, N.J.2    Hartl, F.U.3
  • 36
    • 0030784465 scopus 로고    scopus 로고
    • Extracts of Ginkgo biloba and ginsenosides exert cerebral vasorelaxation via a nitric oxide pathway
    • Chen, X., Salwinski, S., and Lee, T. J. (1997) Extracts of Ginkgo biloba and ginsenosides exert cerebral vasorelaxation via a nitric oxide pathway. Clin. Exp. Pharmacol. Physiol. 24, 958-959
    • (1997) Clin. Exp. Pharmacol. Physiol. , vol.24 , pp. 958-959
    • Chen, X.1    Salwinski, S.2    Lee, T.J.3
  • 37
    • 33846997212 scopus 로고    scopus 로고
    • Ginsenoside Re promotes human sperm capacitation through nitric oxide-dependent pathway
    • Zhang, H., Zhou, Q., Li, X., Zhao, W., Wang, Y., Liu, H., and Li, N. (2007) Ginsenoside Re promotes human sperm capacitation through nitric oxide-dependent pathway. Mol. Reprod. Dev. 74, 497-501
    • (2007) Mol. Reprod. Dev. , vol.74 , pp. 497-501
    • Zhang, H.1    Zhou, Q.2    Li, X.3    Zhao, W.4    Wang, Y.5    Liu, H.6    Li, N.7
  • 39
    • 33749543406 scopus 로고    scopus 로고
    • Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular β-amyloid-induced inhibition of complex IV and limit apoptosis
    • Veereshwarayya, V., Kumar, P., Rosen, K. M., Mestril, R., and Querfurth, H. W. (2006) Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular β-amyloid-induced inhibition of complex IV and limit apoptosis. J. Biol. Chem. 281, 29468-29478
    • (2006) J. Biol. Chem. , vol.281 , pp. 29468-29478
    • Veereshwarayya, V.1    Kumar, P.2    Rosen, K.M.3    Mestril, R.4    Querfurth, H.W.5
  • 40
    • 0035799352 scopus 로고    scopus 로고
    • Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation
    • Lin, K. M., Lin, B., Lian, I. Y., Mestril, R., Scheffler, I. E., and Dillmann, W. H. (2001) Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation. Circulation 103, 1787-1792
    • (2001) Circulation , vol.103 , pp. 1787-1792
    • Lin, K.M.1    Lin, B.2    Lian, I.Y.3    Mestril, R.4    Scheffler, I.E.5    Dillmann, W.H.6
  • 43
    • 0032810909 scopus 로고    scopus 로고
    • β-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria
    • Canevari, L., Clark, J. B., and Bates, T. E. (1999) β-Amyloid fragment 25-35 selectively decreases complex IV activity in isolated mitochondria. FEBS Lett. 457, 131-134
    • (1999) FEBS Lett. , vol.457 , pp. 131-134
    • Canevari, L.1    Clark, J.B.2    Bates, T.E.3
  • 44
    • 33644778691 scopus 로고    scopus 로고
    • Amyloid-beta peptide binds with heme to form a peroxidase. Relationship to the cytopathologies of Alzheimer's disease
    • Atamna, H., and Boyle, K. (2006) Amyloid-beta peptide binds with heme to form a peroxidase. Relationship to the cytopathologies of Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 103, 3381-3386
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 3381-3386
    • Atamna, H.1    Boyle, K.2
  • 45
    • 33845670719 scopus 로고    scopus 로고
    • Nitric oxide regulates mitochondrial oxidative stress protection via the transcriptional coactivator PGC-1α
    • Borniquel, S., Valle, I., Cadenas, S., Lamas, S., and Monsalve, M. (2006) Nitric oxide regulates mitochondrial oxidative stress protection via the transcriptional coactivator PGC-1α. FASEB J. 20, 1889-1891
    • (2006) FASEB J. , vol.20 , pp. 1889-1891
    • Borniquel, S.1    Valle, I.2    Cadenas, S.3    Lamas, S.4    Monsalve, M.5
  • 48
    • 0036244508 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite interactions with mitochondria
    • Radi, R., Cassina, A., and Hodara, R. (2002) Nitric oxide and peroxynitrite interactions with mitochondria. Biol. Chem. 383, 401-409
    • (2002) Biol. Chem. , vol.383 , pp. 401-409
    • Radi, R.1    Cassina, A.2    Hodara, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.