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Volumn 294, Issue 1-2, 2010, Pages 95-101

Neuronal NOS is dislocated during muscle atrophy in amyotrophic lateral sclerosis

Author keywords

Amyotrophic lateral sclerosis (ALS); Motor neuron disease (MND); Muscle atrophy; Neuronal nitric oxide synthase (nNOS); Superoxide dismutase (SOD1)

Indexed keywords

ATROGIN 1; NEURONAL NITRIC OXIDE SYNTHASE; COPPER ZINC SUPEROXIDE DISMUTASE; FBXO32 PROTEIN, MOUSE; MESSENGER RNA; MUSCLE PROTEIN; NOS1 PROTEIN, HUMAN; NOS1 PROTEIN, MOUSE; SUPEROXIDE DISMUTASE; TRIM63 PROTEIN, MOUSE; UBIQUITIN PROTEIN LIGASE;

EID: 77953287436     PISSN: 0022510X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jns.2010.03.022     Document Type: Article
Times cited : (23)

References (43)
  • 1
    • 34250209501 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Mitchell J.D., and Borasio G.D. Amyotrophic lateral sclerosis. Lancet 369 (2007) 2031-2041
    • (2007) Lancet , vol.369 , pp. 2031-2041
    • Mitchell, J.D.1    Borasio, G.D.2
  • 3
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: insights from genetics
    • Pasinelli P., and Brown R.H. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat Rev Neurosci 7 (2006) 710-723
    • (2006) Nat Rev Neurosci , vol.7 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 4
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen D.R., Siddique T., Patterson D., Figlewicz D.A., Sapp P., Hentati A., et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362 (1993) 59-62
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3    Figlewicz, D.A.4    Sapp, P.5    Hentati, A.6
  • 5
    • 0029005002 scopus 로고
    • Variance of age at onset in a Japanese family with amyotrophic lateral sclerosis associated with a novel Cu/Zn superoxide dismutase mutation
    • Aoki M., Abe K., Houi K., Ogasawara M., Matsubara Y., Kobayashi T., et al. Variance of age at onset in a Japanese family with amyotrophic lateral sclerosis associated with a novel Cu/Zn superoxide dismutase mutation. Ann Neurol 37 (1995) 676-679
    • (1995) Ann Neurol , vol.37 , pp. 676-679
    • Aoki, M.1    Abe, K.2    Houi, K.3    Ogasawara, M.4    Matsubara, Y.5    Kobayashi, T.6
  • 7
    • 0035575761 scopus 로고    scopus 로고
    • Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: associated mutations develop motor neuron disease
    • Nagai M., Aoki M., Miyoshi I., Kato M., Pasinelli P., Kasai N., et al. Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: associated mutations develop motor neuron disease. J Neurosci 21 (2001) 9246-9254
    • (2001) J Neurosci , vol.21 , pp. 9246-9254
    • Nagai, M.1    Aoki, M.2    Miyoshi, I.3    Kato, M.4    Pasinelli, P.5    Kasai, N.6
  • 9
    • 49349083891 scopus 로고    scopus 로고
    • Accumulation of chondroitin sulfate proteoglycans in the microenvironment of spinal motor neurons in amyotrophic lateral sclerosis transgenic rats
    • Mizuno H., Warita H., Aoki M., and Itoyama Y. Accumulation of chondroitin sulfate proteoglycans in the microenvironment of spinal motor neurons in amyotrophic lateral sclerosis transgenic rats. J Neurosci Res 86 (2008) 2512-2523
    • (2008) J Neurosci Res , vol.86 , pp. 2512-2523
    • Mizuno, H.1    Warita, H.2    Aoki, M.3    Itoyama, Y.4
  • 10
    • 35848963197 scopus 로고    scopus 로고
    • Intrathecal delivery of hepatocyte growth factor from amyotrophic lateral sclerosis onset suppresses disease progression in rat amyotrophic lateral sclerosis model
    • Ishigaki A., Aoki M., Nagai M., Warita H., Kato S., Kato M., et al. Intrathecal delivery of hepatocyte growth factor from amyotrophic lateral sclerosis onset suppresses disease progression in rat amyotrophic lateral sclerosis model. J Neuropathol Exp Neurol 66 (2007) 1037-1044
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 1037-1044
    • Ishigaki, A.1    Aoki, M.2    Nagai, M.3    Warita, H.4    Kato, S.5    Kato, M.6
  • 11
    • 17644368923 scopus 로고    scopus 로고
    • Mechanical signal transduction in skeletal muscle growth and adaptation
    • Tidball J.G. Mechanical signal transduction in skeletal muscle growth and adaptation. J Appl Physiol 98 (2005) 1900-1908
    • (2005) J Appl Physiol , vol.98 , pp. 1900-1908
    • Tidball, J.G.1
  • 12
    • 0035348487 scopus 로고    scopus 로고
    • Space shuttle flight (STS-90) enhances degradation of rat myosin heavy chain in association with activation of ubiquitin-proteasome pathway
    • Ikemoto M., Nikawa T., Takeda S., Watanabe C., Kitano T., Baldwin K.M., et al. Space shuttle flight (STS-90) enhances degradation of rat myosin heavy chain in association with activation of ubiquitin-proteasome pathway. FASEB J 15 (2001) 1279-1281
    • (2001) FASEB J , vol.15 , pp. 1279-1281
    • Ikemoto, M.1    Nikawa, T.2    Takeda, S.3    Watanabe, C.4    Kitano, T.5    Baldwin, K.M.6
  • 13
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine S.C., Latres E., Baumhueter S., Lai V.K., Nunez L., Clarke B.A., et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294 (2001) 1704-1708
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3    Lai, V.K.4    Nunez, L.5    Clarke, B.A.6
  • 14
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • Gomes M.D., Lecker S.H., Jagoe R.T., Navon A., and Goldberg A.L. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc Natl Acad Sci U S A 98 (2001) 14440-14445
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3    Navon, A.4    Goldberg, A.L.5
  • 15
    • 0035736260 scopus 로고    scopus 로고
    • Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
    • Bodine S.C., Stitt T.N., Gonzalez M., Kline W.O., Stover G.L., Bauerlein R., et al. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat Cell Biol 3 (2001) 1014-1019
    • (2001) Nat Cell Biol , vol.3 , pp. 1014-1019
    • Bodine, S.C.1    Stitt, T.N.2    Gonzalez, M.3    Kline, W.O.4    Stover, G.L.5    Bauerlein, R.6
  • 16
    • 14844336534 scopus 로고    scopus 로고
    • Muscle-specific expression of IGF-1 blocks angiotensin II-induced skeletal muscle wasting
    • Song Y.H., Li Y., Du J., Mitch W.E., Rosenthal N., and Delafontaine P. Muscle-specific expression of IGF-1 blocks angiotensin II-induced skeletal muscle wasting. J Clin Invest 115 (2005) 451-458
    • (2005) J Clin Invest , vol.115 , pp. 451-458
    • Song, Y.H.1    Li, Y.2    Du, J.3    Mitch, W.E.4    Rosenthal, N.5    Delafontaine, P.6
  • 17
    • 0035735902 scopus 로고    scopus 로고
    • Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways
    • Rommel C., Bodine S.C., Clarke B.A., Rossman R., Nunez L., Stitt T.N., et al. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nat Cell Biol 3 (2001) 1009-1013
    • (2001) Nat Cell Biol , vol.3 , pp. 1009-1013
    • Rommel, C.1    Bodine, S.C.2    Clarke, B.A.3    Rossman, R.4    Nunez, L.5    Stitt, T.N.6
  • 18
    • 13244298415 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway
    • Latres E., Amini A.R., Amini A.A., Griffiths J., Martin F.J., Wei Y., et al. Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway. J Biol Chem 280 (2005) 2737-2744
    • (2005) J Biol Chem , vol.280 , pp. 2737-2744
    • Latres, E.1    Amini, A.R.2    Amini, A.A.3    Griffiths, J.4    Martin, F.J.5    Wei, Y.6
  • 19
    • 5444262078 scopus 로고    scopus 로고
    • IKKbeta/NF-kappaB activation causes severe muscle wasting in mice
    • Cai D., Frantz J.D., Tawa Jr. N.E., Melendez P.A., Oh B.C., Lidov H.G., et al. IKKbeta/NF-kappaB activation causes severe muscle wasting in mice. Cell 119 (2004) 285-298
    • (2004) Cell , vol.119 , pp. 285-298
    • Cai, D.1    Frantz, J.D.2    Tawa Jr., N.E.3    Melendez, P.A.4    Oh, B.C.5    Lidov, H.G.6
  • 20
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • Sandri M., Sandri C., Gilbert A., Skurk C., Calabria E., Picard A., et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 117 (2004) 399-412
    • (2004) Cell , vol.117 , pp. 399-412
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3    Skurk, C.4    Calabria, E.5    Picard, A.6
  • 21
    • 0031802331 scopus 로고    scopus 로고
    • Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-kappaB activation in response to tumor necrosis factor alpha
    • Li Y.P., Schwartz R.J., Waddell I.D., Holloway B.R., and Reid M.B. Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-kappaB activation in response to tumor necrosis factor alpha. FASEB J 12 (1998) 871-880
    • (1998) FASEB J , vol.12 , pp. 871-880
    • Li, Y.P.1    Schwartz, R.J.2    Waddell, I.D.3    Holloway, B.R.4    Reid, M.B.5
  • 22
    • 27644471080 scopus 로고    scopus 로고
    • Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia
    • Acharyya S., Butchbach M.E., Sahenk Z., Wang H., Saji M., Carathers M., et al. Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia. Cancer Cell 8 (2005) 421-432
    • (2005) Cancer Cell , vol.8 , pp. 421-432
    • Acharyya, S.1    Butchbach, M.E.2    Sahenk, Z.3    Wang, H.4    Saji, M.5    Carathers, M.6
  • 23
    • 4043154377 scopus 로고    scopus 로고
    • Cancer cachexia is regulated by selective targeting of skeletal muscle gene products
    • Acharyya S., Ladner K.J., Nelsen L.L., Damrauer J., Reiser P.J., Swoap S., et al. Cancer cachexia is regulated by selective targeting of skeletal muscle gene products. J Clin Invest 114 (2004) 370-378
    • (2004) J Clin Invest , vol.114 , pp. 370-378
    • Acharyya, S.1    Ladner, K.J.2    Nelsen, L.L.3    Damrauer, J.4    Reiser, P.J.5    Swoap, S.6
  • 24
    • 34848913758 scopus 로고    scopus 로고
    • NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS
    • Suzuki N., Motohashi N., Uezumi A., Fukada S., Yoshimura T., Itoyama Y., et al. NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS. J Clin Invest 117 (2007) 2468-2476
    • (2007) J Clin Invest , vol.117 , pp. 2468-2476
    • Suzuki, N.1    Motohashi, N.2    Uezumi, A.3    Fukada, S.4    Yoshimura, T.5    Itoyama, Y.6
  • 25
    • 33645897980 scopus 로고    scopus 로고
    • Alteration of familial ALS-linked mutant SOD1 solubility with disease progression: its modulation by the proteasome and Hsp70
    • Koyama S., Arawaka S., Chang-Hong R., Wada M., Kawanami T., Kurita K., et al. Alteration of familial ALS-linked mutant SOD1 solubility with disease progression: its modulation by the proteasome and Hsp70. Biochem Biophys Res Commun 343 (2006) 719-730
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 719-730
    • Koyama, S.1    Arawaka, S.2    Chang-Hong, R.3    Wada, M.4    Kawanami, T.5    Kurita, K.6
  • 26
    • 0035955486 scopus 로고    scopus 로고
    • Marked reduction of the Cu/Zn superoxide dismutase polypeptide in a case of familial amyotrophic lateral sclerosis with the homozygous mutation
    • Kato M., Aoki M., Ohta M., Nagai M., Ishizaki F., Nakamura S., et al. Marked reduction of the Cu/Zn superoxide dismutase polypeptide in a case of familial amyotrophic lateral sclerosis with the homozygous mutation. Neurosci Lett 312 (2001) 165-168
    • (2001) Neurosci Lett , vol.312 , pp. 165-168
    • Kato, M.1    Aoki, M.2    Ohta, M.3    Nagai, M.4    Ishizaki, F.5    Nakamura, S.6
  • 27
    • 33644832749 scopus 로고    scopus 로고
    • Development of a rat model of amyotrophic lateral sclerosis expressing a human SOD1 transgene
    • Aoki M., Kato S., Nagai M., and Itoyama Y. Development of a rat model of amyotrophic lateral sclerosis expressing a human SOD1 transgene. Neuropathology 25 (2005) 365-370
    • (2005) Neuropathology , vol.25 , pp. 365-370
    • Aoki, M.1    Kato, S.2    Nagai, M.3    Itoyama, Y.4
  • 28
    • 65349153034 scopus 로고    scopus 로고
    • Mitochondrial alterations in transgenic mice with an H46R mutant Cu/Zn superoxide dismutase gene
    • Sasaki S., Aoki M., Nagai M., Kobayashi M., and Itoyama Y. Mitochondrial alterations in transgenic mice with an H46R mutant Cu/Zn superoxide dismutase gene. J Neuropathol Exp Neurol 68 (2009) 365-373
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 365-373
    • Sasaki, S.1    Aoki, M.2    Nagai, M.3    Kobayashi, M.4    Itoyama, Y.5
  • 29
    • 0029149471 scopus 로고
    • Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy
    • Brenman J.E., Chao D.S., Xia H., Aldape K., and Bredt D.S. Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell 82 (1995) 743-752
    • (1995) Cell , vol.82 , pp. 743-752
    • Brenman, J.E.1    Chao, D.S.2    Xia, H.3    Aldape, K.4    Bredt, D.S.5
  • 30
    • 33645807350 scopus 로고    scopus 로고
    • Human skeletal muscle atrophy in amyotrophic lateral sclerosis reveals a reduction in Akt and an increase in atrogin-1
    • Leger B., Vergani L., Soraru G., Hespel P., Derave W., Gobelet C., et al. Human skeletal muscle atrophy in amyotrophic lateral sclerosis reveals a reduction in Akt and an increase in atrogin-1. FASEB J 20 (2006) 583-585
    • (2006) FASEB J , vol.20 , pp. 583-585
    • Leger, B.1    Vergani, L.2    Soraru, G.3    Hespel, P.4    Derave, W.5    Gobelet, C.6
  • 31
    • 22844439444 scopus 로고    scopus 로고
    • Sequential changes of nitric oxide levels in the temporal lobes of kainic acid-treated mice following application of nitric oxide synthase inhibitors and phenobarbital
    • Kato N., Sato S., Yokoyama H., Kayama T., and Yoshimura T. Sequential changes of nitric oxide levels in the temporal lobes of kainic acid-treated mice following application of nitric oxide synthase inhibitors and phenobarbital. Epilepsy Res 65 (2005) 81-91
    • (2005) Epilepsy Res , vol.65 , pp. 81-91
    • Kato, N.1    Sato, S.2    Yokoyama, H.3    Kayama, T.4    Yoshimura, T.5
  • 32
    • 29344465714 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2
    • Kim S.F., Huri D.A., and Snyder S.H. Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2. Science 310 (2005) 1966-1970
    • (2005) Science , vol.310 , pp. 1966-1970
    • Kim, S.F.1    Huri, D.A.2    Snyder, S.H.3
  • 34
    • 0036144231 scopus 로고    scopus 로고
    • Peroxynitrite triggers a phenotypic transformation in spinal cord astrocytes that induces motor neuron apoptosis
    • Cassina P., Peluffo H., Pehar M., Martinez-Palma L., Ressia A., Beckman J.S., et al. Peroxynitrite triggers a phenotypic transformation in spinal cord astrocytes that induces motor neuron apoptosis. J Neurosci Res 67 (2002) 21-29
    • (2002) J Neurosci Res , vol.67 , pp. 21-29
    • Cassina, P.1    Peluffo, H.2    Pehar, M.3    Martinez-Palma, L.4    Ressia, A.5    Beckman, J.S.6
  • 36
    • 0032544340 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase inhibitor, 7-nitroindazole, delays motor dysfunction and spinal motoneuron degeneration in the Wobbler mouse
    • Ikeda K., Iwasaki Y., and Kinoshita M. Neuronal nitric oxide synthase inhibitor, 7-nitroindazole, delays motor dysfunction and spinal motoneuron degeneration in the Wobbler mouse. J Neurol Sci 160 (1998) 9-15
    • (1998) J Neurol Sci , vol.160 , pp. 9-15
    • Ikeda, K.1    Iwasaki, Y.2    Kinoshita, M.3
  • 37
    • 0032954386 scopus 로고    scopus 로고
    • Lack of involvement of neuronal nitric oxide synthase in the pathogenesis of a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Facchinetti F., Sasaki M., Cutting F.B., Zhai P., MacDonald J.E., Reif D., et al. Lack of involvement of neuronal nitric oxide synthase in the pathogenesis of a transgenic mouse model of familial amyotrophic lateral sclerosis. Neuroscience 90 (1999) 1483-1492
    • (1999) Neuroscience , vol.90 , pp. 1483-1492
    • Facchinetti, F.1    Sasaki, M.2    Cutting, F.B.3    Zhai, P.4    MacDonald, J.E.5    Reif, D.6
  • 38
    • 56549102799 scopus 로고    scopus 로고
    • Intranasal delivery of insulin and a nitric oxide synthase inhibitor in an experimental model of amyotrophic lateral sclerosis
    • Martinez J.A., Francis G.J., Liu W.Q., Pradzinsky N., Fine J., Wilson M., et al. Intranasal delivery of insulin and a nitric oxide synthase inhibitor in an experimental model of amyotrophic lateral sclerosis. Neuroscience 157 (2008) 908-925
    • (2008) Neuroscience , vol.157 , pp. 908-925
    • Martinez, J.A.1    Francis, G.J.2    Liu, W.Q.3    Pradzinsky, N.4    Fine, J.5    Wilson, M.6
  • 39
    • 1642460628 scopus 로고    scopus 로고
    • Transmission of arterial baroreflex signals depends on neuronal nitric oxide synthase
    • Talman W.T., and Dragon D.N. Transmission of arterial baroreflex signals depends on neuronal nitric oxide synthase. Hypertension 43 (2004) 820-824
    • (2004) Hypertension , vol.43 , pp. 820-824
    • Talman, W.T.1    Dragon, D.N.2
  • 41
    • 0034809375 scopus 로고    scopus 로고
    • The influence of nitric oxide synthase 1 on blood flow and interstitial nitric oxide in the kidney
    • Kakoki M., Zou A.P., and Mattson D.L. The influence of nitric oxide synthase 1 on blood flow and interstitial nitric oxide in the kidney. Am J Physiol Regul Integr Comp Physiol 281 (2001) R91-R97
    • (2001) Am J Physiol Regul Integr Comp Physiol , vol.281
    • Kakoki, M.1    Zou, A.P.2    Mattson, D.L.3
  • 42
    • 0032502351 scopus 로고    scopus 로고
    • N5-(1-Imino-3-butenyl)-l-ornithine. A neuronal isoform selective mechanism-based inactivator of nitric oxide synthase
    • Babu B.R., and Griffith O.W. N5-(1-Imino-3-butenyl)-l-ornithine. A neuronal isoform selective mechanism-based inactivator of nitric oxide synthase. J Biol Chem 273 (1998) 8882-8889
    • (1998) J Biol Chem , vol.273 , pp. 8882-8889
    • Babu, B.R.1    Griffith, O.W.2
  • 43
    • 33847048132 scopus 로고    scopus 로고
    • Conditional neuronal nitric oxide synthase overexpression impairs myocardial contractility
    • Burkard N., Rokita A.G., Kaufmann S.G., Hallhuber M., Wu R., Hu K., et al. Conditional neuronal nitric oxide synthase overexpression impairs myocardial contractility. Circ Res 100 (2007) e32-e44
    • (2007) Circ Res , vol.100
    • Burkard, N.1    Rokita, A.G.2    Kaufmann, S.G.3    Hallhuber, M.4    Wu, R.5    Hu, K.6


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