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Volumn 8, Issue 3, 2013, Pages

Unfolded Protein Response and Activated Degradative Pathways Regulation in GNE Myopathy

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; CALNEXIN; CALRETICULIN; GLUCOSE REGULATED PROTEIN 78; GLUCOSE REGULATED PROTEIN 94; PROTEASOME; TAU PROTEIN; UBIQUITIN; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE 2 EPIMERASE; VALOSIN CONTAINING PROTEIN; ADENOSINE TRIPHOSPHATASE; CDC48 PROTEIN; CELL CYCLE PROTEIN; CHAPERONE; ENDOPLASMIN; HEAT SHOCK PROTEIN; MEMBRANE PROTEIN; MOLECULAR CHAPERONE GRP78; MULTIENZYME COMPLEX; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE - N-ACETYLMANNOSAMINE KINASE;

EID: 84874612520     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0058116     Document Type: Article
Times cited : (34)

References (34)
  • 1
    • 0019481203 scopus 로고
    • Familial distal myopathy with rimmed vacuole and lamellar (myeloid) body formation
    • Nonaka I, Sunohara N, Ishiura S, Satoyoshi E, (1981) Familial distal myopathy with rimmed vacuole and lamellar (myeloid) body formation. J Neurol Sci 51: 141-155.
    • (1981) J Neurol Sci , vol.51 , pp. 141-155
    • Nonaka, I.1    Sunohara, N.2    Ishiura, S.3    Satoyoshi, E.4
  • 2
    • 0021320516 scopus 로고
    • "Rimmed vacuole myopathy" sparing the quadriceps. A unique disorder in Iranian Jews
    • Argov Z, Yarom R, (1984) "Rimmed vacuole myopathy" sparing the quadriceps. A unique disorder in Iranian Jews. J Neurol Sci 64: 33-43.
    • (1984) J Neurol Sci , vol.64 , pp. 33-43
    • Argov, Z.1    Yarom, R.2
  • 3
    • 17944366749 scopus 로고    scopus 로고
    • The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy
    • Eisenberg I, Avidan N, Potikha T, Hochner H, Chen M, et al. (2001) The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is mutated in recessive hereditary inclusion body myopathy. Nat Genet 29: 83-87.
    • (2001) Nat Genet , vol.29 , pp. 83-87
    • Eisenberg, I.1    Avidan, N.2    Potikha, T.3    Hochner, H.4    Chen, M.5
  • 4
    • 0036217154 scopus 로고    scopus 로고
    • Nonaka myopathy is caused by mutations in the UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase gene (GNE)
    • Kayashima T, Matsuo H, Satoh A, Ohta T, Yoshiura K, et al. (2002) Nonaka myopathy is caused by mutations in the UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase gene (GNE). J Hum Genet 47: 77-79.
    • (2002) J Hum Genet , vol.47 , pp. 77-79
    • Kayashima, T.1    Matsuo, H.2    Satoh, A.3    Ohta, T.4    Yoshiura, K.5
  • 5
    • 0030827890 scopus 로고    scopus 로고
    • A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase
    • Stasche R, Hinderlich S, Weise C, Effertz K, Lucka L, et al. (1997) A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase. J Biol Chem 272: 24319-24324.
    • (1997) J Biol Chem , vol.272 , pp. 24319-24324
    • Stasche, R.1    Hinderlich, S.2    Weise, C.3    Effertz, K.4    Lucka, L.5
  • 6
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • Varki A, (1997) Sialic acids as ligands in recognition phenomena. Faseb J 11: 248-255.
    • (1997) Faseb J , vol.11 , pp. 248-255
    • Varki, A.1
  • 7
    • 12144287262 scopus 로고    scopus 로고
    • Reduction of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase activity and sialylation in distal myopathy with rimmed vacuoles
    • Noguchi S, Keira Y, Murayama K, Ogawa M, Fujita M, et al. (2004) Reduction of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase activity and sialylation in distal myopathy with rimmed vacuoles. J Biol Chem 279: 11402-11407.
    • (2004) J Biol Chem , vol.279 , pp. 11402-11407
    • Noguchi, S.1    Keira, Y.2    Murayama, K.3    Ogawa, M.4    Fujita, M.5
  • 8
    • 1242292943 scopus 로고    scopus 로고
    • Hypoglycosylation of alpha-dystroglycan in patients with hereditary IBM due to GNE mutations
    • Huizing M, Rakocevic G, Sparks SE, Mamali I, Shatunov A, et al. (2004) Hypoglycosylation of alpha-dystroglycan in patients with hereditary IBM due to GNE mutations. Mol Genet Metab 81: 196-202.
    • (2004) Mol Genet Metab , vol.81 , pp. 196-202
    • Huizing, M.1    Rakocevic, G.2    Sparks, S.E.3    Mamali, I.4    Shatunov, A.5
  • 9
    • 20244374708 scopus 로고    scopus 로고
    • Distal myopathy with rimmed vacuoles: impaired O-glycan formation in muscular glycoproteins
    • Tajima Y, Uyama E, Go S, Sato C, Tao N, et al. (2005) Distal myopathy with rimmed vacuoles: impaired O-glycan formation in muscular glycoproteins. Am J Pathol 166: 1121-1130.
    • (2005) Am J Pathol , vol.166 , pp. 1121-1130
    • Tajima, Y.1    Uyama, E.2    Go, S.3    Sato, C.4    Tao, N.5
  • 10
    • 13444262055 scopus 로고    scopus 로고
    • alpha-Dystroglycan does not play a major pathogenic role in autosomal recessive hereditary inclusion-body myopathy
    • Broccolini A, Gliubizzi C, Pavoni E, Gidaro T, Morosetti R, et al. (2005) alpha-Dystroglycan does not play a major pathogenic role in autosomal recessive hereditary inclusion-body myopathy. Neuromuscul Disord 15: 177-184.
    • (2005) Neuromuscul Disord , vol.15 , pp. 177-184
    • Broccolini, A.1    Gliubizzi, C.2    Pavoni, E.3    Gidaro, T.4    Morosetti, R.5
  • 11
    • 0036797633 scopus 로고    scopus 로고
    • Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanisms
    • Askanas V, Engel WK, (2002) Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanisms. Curr Opin Neurol 15: 525-531.
    • (2002) Curr Opin Neurol , vol.15 , pp. 525-531
    • Askanas, V.1    Engel, W.K.2
  • 12
    • 0037197835 scopus 로고    scopus 로고
    • Inclusion body myositis-like phenotype induced by transgenic overexpression of beta APP in skeletal muscle
    • Sugarman MC, Yamasaki TR, Oddo S, Echegoyen JC, Murphy MP, et al. (2002) Inclusion body myositis-like phenotype induced by transgenic overexpression of beta APP in skeletal muscle. Proc Natl Acad Sci U S A 99: 6334-6339.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 6334-6339
    • Sugarman, M.C.1    Yamasaki, T.R.2    Oddo, S.3    Echegoyen, J.C.4    Murphy, M.P.5
  • 13
    • 79955506304 scopus 로고    scopus 로고
    • Clinical and molecular genetic analysis in Chinese patients with distal myopathy with rimmed vacuoles
    • Li H, Chen Q, Liu F, Zhang X, Liu T,et al. Clinical and molecular genetic analysis in Chinese patients with distal myopathy with rimmed vacuoles. J Hum Genet 56: 335-338.
    • J Hum Genet , vol.56 , pp. 335-338
    • Li, H.1    Chen, Q.2    Liu, F.3    Zhang, X.4    Liu, T.5
  • 14
    • 24144489814 scopus 로고    scopus 로고
    • Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers
    • Fratta P, Engel WK, McFerrin J, Davies KJ, Lin SW, et al. (2005) Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers. Am J Pathol 167: 517-526.
    • (2005) Am J Pathol , vol.167 , pp. 517-526
    • Fratta, P.1    Engel, W.K.2    McFerrin, J.3    Davies, K.J.4    Lin, S.W.5
  • 15
    • 35548931584 scopus 로고    scopus 로고
    • Characterization of hereditary inclusion body myopathy myoblasts: possible primary impairment of apoptotic events
    • Amsili S, Shlomai Z, Levitzki R, Krause S, Lochmuller H, et al. (2007) Characterization of hereditary inclusion body myopathy myoblasts: possible primary impairment of apoptotic events. Cell Death Differ 14: 1916-1924.
    • (2007) Cell Death Differ , vol.14 , pp. 1916-1924
    • Amsili, S.1    Shlomai, Z.2    Levitzki, R.3    Krause, S.4    Lochmuller, H.5
  • 16
    • 34250826506 scopus 로고    scopus 로고
    • Autophagy in a mouse model of distal myopathy with rimmed vacuoles or hereditary inclusion body myopathy
    • Malicdan MC, Noguchi S, Nishino I, (2007) Autophagy in a mouse model of distal myopathy with rimmed vacuoles or hereditary inclusion body myopathy. Autophagy 3: 396-398.
    • (2007) Autophagy , vol.3 , pp. 396-398
    • Malicdan, M.C.1    Noguchi, S.2    Nishino, I.3
  • 18
    • 64449088789 scopus 로고    scopus 로고
    • Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis
    • Vattemi G, Nogalska A, King Engel W, D'Agostino C, Checler F, et al. (2009) Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis. Acta Neuropathol 117: 569-574.
    • (2009) Acta Neuropathol , vol.117 , pp. 569-574
    • Vattemi, G.1    Nogalska, A.2    King Engel, W.3    D'Agostino, C.4    Checler, F.5
  • 19
    • 1542784578 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle
    • Vattemi G, Engel WK, McFerrin J, Askanas V, (2004) Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am J Pathol 164: 1-7.
    • (2004) Am J Pathol , vol.164 , pp. 1-7
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 20
    • 35549010650 scopus 로고    scopus 로고
    • A Gne knockout mouse expressing human GNE D176V mutation develops features similar to distal myopathy with rimmed vacuoles or hereditary inclusion body myopathy
    • Malicdan MC, Noguchi S, Nonaka I, Hayashi YK, Nishino I, (2007) A Gne knockout mouse expressing human GNE D176V mutation develops features similar to distal myopathy with rimmed vacuoles or hereditary inclusion body myopathy. Hum Mol Genet 16: 2669-2682.
    • (2007) Hum Mol Genet , vol.16 , pp. 2669-2682
    • Malicdan, M.C.1    Noguchi, S.2    Nonaka, I.3    Hayashi, Y.K.4    Nishino, I.5
  • 21
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander R, Jarosch E, Urban J, Volkwein C, Sommer T, (2000) A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2: 379-384.
    • (2000) Nat Cell Biol , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 22
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, et al. (2000) Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101: 249-258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5
  • 23
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L, Usherwood YK, Chung KT, Hendershot LM, (2002) A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13: 4456-4469.
    • (2002) Mol Biol Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 24
    • 33645239012 scopus 로고    scopus 로고
    • Roles of heat shock protein gp96 in the ER quality control: redundant or unique function?
    • Yang Y, Li Z, (2005) Roles of heat shock protein gp96 in the ER quality control: redundant or unique function? Mol Cell 20: 173-182.
    • (2005) Mol Cell , vol.20 , pp. 173-182
    • Yang, Y.1    Li, Z.2
  • 25
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch E, Taxis C, Volkwein C, Bordallo J, Finley D, et al. (2002) Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4: 134-139.
    • (2002) Nat Cell Biol , vol.4 , pp. 134-139
    • Jarosch, E.1    Taxis, C.2    Volkwein, C.3    Bordallo, J.4    Finley, D.5
  • 26
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich E, Kerem A, Frohlich KU, Diamant N, Bar-Nun S, (2002) AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 22: 626-634.
    • (2002) Mol Cell Biol , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frohlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 27
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey UB, Nie Z, Batlevi Y, McCray BA, Ritson GP, et al. (2007) HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 447: 859-863.
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1    Nie, Z.2    Batlevi, Y.3    McCray, B.A.4    Ritson, G.P.5
  • 28
    • 38949096081 scopus 로고    scopus 로고
    • Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome
    • Ding WX, Yin XM, (2008) Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome. Autophagy 4: 141-150.
    • (2008) Autophagy , vol.4 , pp. 141-150
    • Ding, W.X.1    Yin, X.M.2
  • 29
    • 0034919522 scopus 로고    scopus 로고
    • Expression of the lysosome-associated membrane proteins in myopathies with rimmed vacuoles
    • Tsuruta Y, Furuta A, Furuta K, Yamada T, Kira J, et al. (2001) Expression of the lysosome-associated membrane proteins in myopathies with rimmed vacuoles. Acta Neuropathol 101: 579-584.
    • (2001) Acta Neuropathol , vol.101 , pp. 579-584
    • Tsuruta, Y.1    Furuta, A.2    Furuta, K.3    Yamada, T.4    Kira, J.5
  • 30
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G, Lamark T, Brech A, Outzen H, Perander M, et al. (2005) p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 171: 603-614.
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5
  • 31
    • 35948958216 scopus 로고    scopus 로고
    • HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration
    • Pandey UB, Batlevi Y, Baehrecke EH, Taylor JP, (2007) HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration. Autophagy 3: 643-645.
    • (2007) Autophagy , vol.3 , pp. 643-645
    • Pandey, U.B.1    Batlevi, Y.2    Baehrecke, E.H.3    Taylor, J.P.4
  • 32
    • 77950487987 scopus 로고    scopus 로고
    • Korolchuk VI, Menzies FM, Rubinsztein DC Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems
    • Korolchuk VI, Menzies FM, Rubinsztein DC Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems. FEBS Lett 584: 1393-1398.
    • FEBS Lett , vol.584 , pp. 1393-1398
  • 33
    • 82355175806 scopus 로고    scopus 로고
    • Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis
    • D'Agostino C, Nogalska A, Cacciottolo M, King Engel W, Askanas V, (2011) Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis. Acta Neuropathol 122: 627-636.
    • (2011) Acta Neuropathol , vol.122 , pp. 627-636
    • D'Agostino, C.1    Nogalska, A.2    Cacciottolo, M.3    King Engel, W.4    Askanas, V.5
  • 34
    • 68349097450 scopus 로고    scopus 로고
    • p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis
    • Nogalska A, Terracciano C, D'Agostino C, King Engel W, Askanas V, (2009) p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis. Acta Neuropathol 118: 407-413.
    • (2009) Acta Neuropathol , vol.118 , pp. 407-413
    • Nogalska, A.1    Terracciano, C.2    D'Agostino, C.3    King Engel, W.4    Askanas, V.5


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