메뉴 건너뛰기




Volumn 8, Issue 12, 2013, Pages

Sialylation and muscle performance: Sialic acid is a marker of muscle ageing

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOCONJUGATE; GLYCOPROTEIN; MONOSACCHARIDE; N ACETYLGLUCOSAMINE; SIALIC ACID; URIDINE DIPHOSPHATE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE 2 EPIMERASE;

EID: 84892573566     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0080520     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 0030827128 scopus 로고    scopus 로고
    • A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
    • Hinderlich S, Stäsche R, Zeitler R, Reutter W (1997) A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase. J Biol Chem 272: 24313-24318.
    • (1997) J Biol Chem , vol.272 , pp. 24313-24318
    • Hinderlich, S.1    Stäsche, R.2    Zeitler, R.3    Reutter, W.4
  • 2
    • 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
    • Stäsche 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: 24319-24.
    • (1997) J Biol Chem , vol.272 , pp. 24319-24324
    • Stäsche, R.1    Hinderlich, S.2    Weise, C.3    Effertz, K.4    Lucka, L.5
  • 3
    • 77449115880 scopus 로고    scopus 로고
    • Advances in the biology and chemistry of sialic acids
    • Chen X, Varki A (2010) Advances in the biology and chemistry of sialic acids. ACS Chem Biol 5: 163-176.
    • (2010) ACS Chem Biol , vol.5 , pp. 163-176
    • Chen, X.1    Varki, A.2
  • 4
    • 70349878950 scopus 로고    scopus 로고
    • Sialic acids as regulators of molecular and cellular interactions
    • Schauer R (2010) Sialic acids as regulators of molecular and cellular interactions. Curr Opin Struct Biol 19: 507-514.
    • (2010) Curr Opin Struct Biol , vol.19 , pp. 507-514
    • Schauer, R.1
  • 5
    • 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
  • 6
    • 0037058765 scopus 로고    scopus 로고
    • Distal myopathy with rimmed vacuoles is allelic to hereditary inclusion body myopathy
    • Nishino I, Noguchi S, Murayama K, Driss A, Sugie K, et al. (2002) Distal myopathy with rimmed vacuoles is allelic to hereditary inclusion body myopathy. Neurology 59: 1689-1693.
    • (2002) Neurology , vol.59 , pp. 1689-1693
    • Nishino, I.1    Noguchi, S.2    Murayama, K.3    Driss, A.4    Sugie, K.5
  • 7
    • 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
  • 8
    • 0029826654 scopus 로고    scopus 로고
    • The spectrum of familial inclusion body myopathies in 13 families and a description of a quadriceps-sparing phenotype in non-Iranian Jews
    • Sivakumar K, Dalakas MC (1996) The spectrum of familial inclusion body myopathies in 13 families and a description of a quadriceps-sparing phenotype in non-Iranian Jews. Neurology 47: 977-984.
    • (1996) Neurology , vol.47 , pp. 977-984
    • Sivakumar, K.1    Dalakas, M.C.2
  • 9
    • 4544304099 scopus 로고    scopus 로고
    • Novel GNE mutations in Italian families with autosomal recessive hereditary inclusionbody myopathy
    • Broccolini A, Ricci E, Cassandrini D, Gliubizzi C, Bruno C, et al. (2004) Novel GNE mutations in Italian families with autosomal recessive hereditary inclusionbody myopathy. Hum Mutat 23: 632.
    • (2004) Hum Mutat , vol.23 , pp. 632
    • Broccolini, A.1    Ricci, E.2    Cassandrini, D.3    Gliubizzi, C.4    Bruno, C.5
  • 10
    • 0037058770 scopus 로고    scopus 로고
    • An Italian family with autosomal recessive inclusion-body myopathy and mutations in the GNE gene
    • Broccolini A, Pescatori M, D'Amico A, Sabino A, Silvestri G, et al. (2005) An Italian family with autosomal recessive inclusion-body myopathy and mutations in the GNE gene. Neurology 59: 1808-1809.
    • (2005) Neurology , vol.59 , pp. 1808-1809
    • Broccolini, A.1    Pescatori, M.2    D'Amico, A.3    Sabino, A.4    Silvestri, G.5
  • 11
    • 18744392293 scopus 로고    scopus 로고
    • Mutations spectrum of GNE in hereditary inclusion body myopathy sparing the quadriceps
    • Eisenberg I, Grabov-Nardini G, Hochner H, Korner M, Sadeh M, et al. (2003) Mutations spectrum of GNE in hereditary inclusion body myopathy sparing the quadriceps. Hum Mutat 21: 99.
    • (2003) Hum Mutat , vol.21 , pp. 99
    • Eisenberg, I.1    Grabov-Nardini, G.2    Hochner, H.3    Korner, M.4    Sadeh, M.5
  • 12
    • 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
  • 14
    • 34547895110 scopus 로고    scopus 로고
    • GNE protein expression and subcellular distribution are unaltered in HIBM
    • Krause S, Aleo A, Hinderlich S, Merlini L, Tournev I, et al. (2007) GNE protein expression and subcellular distribution are unaltered in HIBM. Neurology 69: 655-659.
    • (2007) Neurology , vol.69 , pp. 655-659
    • Krause, S.1    Aleo, A.2    Hinderlich, S.3    Merlini, L.4    Tournev, I.5
  • 15
    • 33847650003 scopus 로고    scopus 로고
    • Reduced sialylation status in UDP-N-acetylglucosamine-2-epimerase/N- acetylmannosamine kinase (GNE)-deficient mice
    • Gagiannis D, Orthmann A, Danssmann I, Schwarzkopf M, Weidemann W, et al. (2007) Reduced sialylation status in UDP-N-acetylglucosamine-2-epimerase/N- acetylmannosamine kinase (GNE)-deficient mice. Glycoconj J 24: 125-130.
    • (2007) Glycoconj J , vol.24 , pp. 125-130
    • Gagiannis, D.1    Orthmann, A.2    Danssmann, I.3    Schwarzkopf, M.4    Weidemann, W.5
  • 16
    • 0019312895 scopus 로고
    • Characterization of the asialoglycoprotein receptor on isolated rat hepatocytes
    • Weigel PH (1980) Characterization of the asialoglycoprotein receptor on isolated rat hepatocytes. J Biol Chem 255: 6111-20.
    • (1980) J Biol Chem , vol.255 , pp. 6111-6120
    • Weigel, P.H.1
  • 17
    • 63649163810 scopus 로고    scopus 로고
    • The asialoglycoprotein receptor regulates levels of plasma glycoproteins terminating with sialic acid alpha2,6-galactose
    • Steirer LM, Park EI, Townsend RR, Baenziger JU (2009) The asialoglycoprotein receptor regulates levels of plasma glycoproteins terminating with sialic acid alpha2,6-galactose. J Biol Chem 284: 3777-83.
    • (2009) J Biol Chem , vol.284 , pp. 3777-3783
    • Steirer, L.M.1    Park, E.I.2    Townsend, R.R.3    Baenziger, J.U.4
  • 18
    • 0024227110 scopus 로고
    • Adult polyglucosan body myopathy with subclinical peripheral neuropathy: Case report and review of diseases associated with polyglucosan body accumulation
    • Weis J, Schröder JM (1988) Adult polyglucosan body myopathy with subclinical peripheral neuropathy: case report and review of diseases associated with polyglucosan body accumulation. Clin Neuropathol 7: 271-279.
    • (1988) Clin Neuropathol , vol.7 , pp. 271-279
    • Weis, J.1    Schröder, J.M.2
  • 19
    • 34249086216 scopus 로고    scopus 로고
    • The UspA1 protein of Moraxella catarrhalis induces CEACAM-1-dependent apoptosis in alveolar epithelial cells
    • N'Guessan PD, Vigelahn M, Bachmann S, Zabel S, Opitz B, et al. (2007) The UspA1 protein of Moraxella catarrhalis induces CEACAM-1-dependent apoptosis in alveolar epithelial cells. J Infect Dis 195: 1651-1660.
    • (2007) J Infect Dis , vol.195 , pp. 1651-1660
    • N'Guessan, P.D.1    Vigelahn, M.2    Bachmann, S.3    Zabel, S.4    Opitz, B.5
  • 20
    • 0035077631 scopus 로고    scopus 로고
    • Biosynthesis of N-Acetylneuraminic Acid in Cells Lacking UDP-N-Acetylglucosamine 2-Epimerase/N-Acetylmannosamine Kinase
    • Hinderlich S, Berger M, Keppler OT, Pawlita M, Reutter W (2001) Biosynthesis of N-Acetylneuraminic Acid in Cells Lacking UDP-N-Acetylglucosamine 2-Epimerase/N-Acetylmannosamine Kinase. Biol Chem 382: 291-297.
    • (2001) Biol Chem , vol.382 , pp. 291-297
    • Hinderlich, S.1    Berger, M.2    Keppler, O.T.3    Pawlita, M.4    Reutter, W.5
  • 21
    • 33645870439 scopus 로고    scopus 로고
    • NCAM is hyposialylated in hereditary inclusion body myopathy due to GNE mutations
    • Ricci E, Broccolini A, Gidaro T, Morosetti R, Gliubizzi C, et al. (2006) NCAM is hyposialylated in hereditary inclusion body myopathy due to GNE mutations. Neurology 66: 755-758.
    • (2006) Neurology , vol.66 , pp. 755-758
    • Ricci, E.1    Broccolini, A.2    Gidaro, T.3    Morosetti, R.4    Gliubizzi, C.5
  • 22
    • 80155192629 scopus 로고    scopus 로고
    • GNE is involved in the early development of skeletal and cardiac muscle
    • Milman Krentsis I, Sela I, Eiges R, Blanchard V, Berger M, et al. (2011) GNE is involved in the early development of skeletal and cardiac muscle. PLoS One 6: e21389.
    • (2011) PLoS One , vol.6
    • Milman Krentsis, I.1    Sela, I.2    Eiges, R.3    Blanchard, V.4    Berger, M.5
  • 24
    • 0028198903 scopus 로고
    • Expression of NCAM and its polysialylated isoforms during mdx mouse muscle regeneration and in vitro myogenesis
    • Dubois C, Figarella-Branger D, Pastoret C, Rampini C, Karpati G, et al. (1994) Expression of NCAM and its polysialylated isoforms during mdx mouse muscle regeneration and in vitro myogenesis. Neuromuscul Disord 4:171-182.
    • (1994) Neuromuscul Disord , vol.4 , pp. 171-182
    • Dubois, C.1    Figarella-Branger, D.2    Pastoret, C.3    Rampini, C.4    Karpati, G.5
  • 25
    • 0033150540 scopus 로고    scopus 로고
    • Figarella-Branger D, Pellissier JF, Bianco N, Karpati G (1999) Sequence of expression of MyoD1 and various cell surface and cytoskeletal proteins in regenerating mouse muscle fibers following treatment with sodium dihydrogen phosphate. J Neurol Sci 165: 106-115. Corrected and republished in: J Neurol Sci 170: 151-160
    • Figarella-Branger D, Pellissier JF, Bianco N, Karpati G (1999) Sequence of expression of MyoD1 and various cell surface and cytoskeletal proteins in regenerating mouse muscle fibers following treatment with sodium dihydrogen phosphate. J Neurol Sci 165: 106-115. Corrected and republished in: J Neurol Sci 170: 151-160
  • 26
    • 79956223758 scopus 로고    scopus 로고
    • Defective polysialylation and sialylation induce opposite effects on gating of the skeletal Na+ channel NaV1.4 in Chinese hamster ovary cells
    • Ahrens J, Foadi N, Eberhardt A, Haeseler G, Dengler R, et al. (2011) Defective polysialylation and sialylation induce opposite effects on gating of the skeletal Na+ channel NaV1.4 in Chinese hamster ovary cells. Pharmacology 87: 311-317.
    • (2011) Pharmacology , vol.87 , pp. 311-317
    • Ahrens, J.1    Foadi, N.2    Eberhardt, A.3    Haeseler, G.4    Dengler, R.5
  • 27
    • 84863710488 scopus 로고    scopus 로고
    • Preferential reduction of the alpha-2-6-sialylation from cell surface Nglycans of human diploid fibroblastic cells by in vitro aging
    • Tadokoro T, Yamamoto K, Kuwahara I, Fujisawa H, Ikekita M, et al. (2006) Preferential reduction of the alpha-2-6-sialylation from cell surface Nglycans of human diploid fibroblastic cells by in vitro aging. Glycoconj J 23: 443-452.
    • (2006) Glycoconj J , vol.23 , pp. 443-452
    • Tadokoro, T.1    Yamamoto, K.2    Kuwahara, I.3    Fujisawa, H.4    Ikekita, M.5
  • 28
    • 71049144353 scopus 로고    scopus 로고
    • Sialic acid feeding aged rats rejuvenates stimulated salivation and colon enteric neuron chemotypes
    • Sprenger N, Julita M, Donnicola D, Jann A (2009) Sialic acid feeding aged rats rejuvenates stimulated salivation and colon enteric neuron chemotypes. Glycobiology 19: 1492-1502.
    • (2009) Glycobiology , vol.19 , pp. 1492-1502
    • Sprenger, N.1    Julita, M.2    Donnicola, D.3    Jann, A.4
  • 29
    • 51249117834 scopus 로고    scopus 로고
    • Lectin-based proteomic profiling of aged skeletal muscle: Decreased pyruvate kinase isozyme M1 exhibits drastically increased levels of N-glycosylation
    • O'Connell K, Doran P, Gannon J, Ohlendieck K (2008) Lectin-based proteomic profiling of aged skeletal muscle: decreased pyruvate kinase isozyme M1 exhibits drastically increased levels of N-glycosylation. Eur J Cell Biol 87: 793-805.
    • (2008) Eur J Cell Biol , vol.87 , pp. 793-805
    • O'Connell, K.1    Doran, P.2    Gannon, J.3    Ohlendieck, K.4
  • 30
    • 56149107232 scopus 로고    scopus 로고
    • Muscle weakness correlates with muscle atrophy and precedes the development of inclusion body or rimmed vacuoles in the mouse model of DMRV/hIBM
    • Malicdan MC, Noguchi S, Hayashi YK, Nishino I (2008) Muscle weakness correlates with muscle atrophy and precedes the development of inclusion body or rimmed vacuoles in the mouse model of DMRV/hIBM. Physiol Genomics 35: 106-115.
    • (2008) Physiol Genomics , vol.35 , pp. 106-115
    • Malicdan, M.C.1    Noguchi, S.2    Hayashi, Y.K.3    Nishino, I.4
  • 31
    • 1242293860 scopus 로고    scopus 로고
    • Tubular aggregates are from whole sarcoplasmic reticulum origin: Alterations in calcium binding protein expression in mouse skeletal muscle during aging
    • Chevessier F, Marty I, Paturneau-Jouas M, Hantaï D, Verdière-Sahuqué M (2004) Tubular aggregates are from whole sarcoplasmic reticulum origin: alterations in calcium binding protein expression in mouse skeletal muscle during aging. Neuromuscul Disord 14: 208-216.
    • (2004) Neuromuscul Disord , vol.14 , pp. 208-216
    • Chevessier, F.1    Marty, I.2    Paturneau-Jouas, M.3    Hantaï, D.4    Verdière-Sahuqué, M.5
  • 32
    • 0033058675 scopus 로고    scopus 로고
    • Transgenic mouse models of muscle aging
    • Musarò A, Rosenthal N (1999) Transgenic mouse models of muscle aging. Exp Gerontol 34: 147-156.
    • (1999) Exp Gerontol , vol.34 , pp. 147-156
    • Musarò, A.1    Rosenthal, N.2
  • 33
    • 16644399758 scopus 로고    scopus 로고
    • Early onset of lipofuscin accumulation in dystrophin-deficient skeletal muscles of DMD patients and mdx mice
    • Nakae Y, Stoward PJ, Kashiyama T, Shono M, Akagi A, et al. (2004) Early onset of lipofuscin accumulation in dystrophin-deficient skeletal muscles of DMD patients and mdx mice. J Mol Histol 35: 489-499.
    • (2004) J Mol Histol , vol.35 , pp. 489-499
    • Nakae, Y.1    Stoward, P.J.2    Kashiyama, T.3    Shono, M.4    Akagi, A.5
  • 34
    • 0023465842 scopus 로고
    • Comparative morphological study of age related mitochondrial changes of the lymphocytes and skeletal muscle cells
    • Beregi E, Regius O (1987) Comparative morphological study of age related mitochondrial changes of the lymphocytes and skeletal muscle cells. Acta Morphol Hung 35: 219-224.
    • (1987) Acta Morphol Hung , vol.35 , pp. 219-224
    • Beregi, E.1    Regius, O.2
  • 35
    • 0023882449 scopus 로고
    • Age-related changes in the skeletal muscle cells
    • Beregi E, Regius O, Hüttl T, Göbl Z (1988) Age-related changes in the skeletal muscle cells. Z Gerontol 21: 83-86.
    • (1988) Z Gerontol , vol.21 , pp. 83-86
    • Beregi, E.1    Regius, O.2    Hüttl, T.3    Göbl, Z.4
  • 36
    • 0031899498 scopus 로고    scopus 로고
    • Comparative structural analysis of neuromuscular junctions in mice at different ages
    • Boaro SN, Soares JC, König B Jr (1998) Comparative structural analysis of neuromuscular junctions in mice at different ages. Ann Anat 180: 173-179.
    • (1998) Ann Anat , vol.180 , pp. 173-179
    • Boaro, S.N.1    Soares, J.C.2    König Jr., B.3
  • 37
    • 0020787427 scopus 로고
    • Intramolecular heterogeneity of degradation in plasma membrane glycoproteins: Evidence for a general characteristic
    • Tauber R, Park CS, Reutter W (1983) Intramolecular heterogeneity of degradation in plasma membrane glycoproteins: evidence for a general characteristic. Proc Natl Acad Sci U S A 80: 4026-9.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 4026-4029
    • Tauber, R.1    Park, C.S.2    Reutter, W.3
  • 38
    • 0036464654 scopus 로고    scopus 로고
    • Acidic and neutral sialidase in the erythrocyte membrane of type 2 diabetic patients
    • Venerando B, Fiorilli A, Croci G, Tringali C, Goi G, et al. (2002) Acidic and neutral sialidase in the erythrocyte membrane of type 2 diabetic patients. Blood 99: 1064-70.
    • (2002) Blood , vol.99 , pp. 1064-1070
    • Venerando, B.1    Fiorilli, A.2    Croci, G.3    Tringali, C.4    Goi, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.