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Volumn 82, Issue , 2018, Pages 135-141

Aberrant apolipoprotein C-III glycosylation in glycogen storage disease type III and IX

Author keywords

Apolipoprotein C III; Diagnostic marker; Glycogen storage disorders; Hypertriglyceridemia; O glycosylation

Indexed keywords

APOLIPOPROTEIN C3; TRANSFERRIN;

EID: 85042766238     PISSN: 00260495     EISSN: 15328600     Source Type: Journal    
DOI: 10.1016/j.metabol.2018.01.004     Document Type: Article
Times cited : (10)

References (43)
  • 1
    • 33847354287 scopus 로고    scopus 로고
    • Transferrin and apolipoprotein C-III isofocusing are complementary in the diagnosis of N- and O-glycan biosynthesis defects
    • Wopereis, S., Grünewald, S., Huijben, K.M., Morava, E., Mollicone, R., van Engelen, B.G., et al. Transferrin and apolipoprotein C-III isofocusing are complementary in the diagnosis of N- and O-glycan biosynthesis defects. Clin Chem 53 (2007), 180–187.
    • (2007) Clin Chem , vol.53 , pp. 180-187
    • Wopereis, S.1    Grünewald, S.2    Huijben, K.M.3    Morava, E.4    Mollicone, R.5    van Engelen, B.G.6
  • 3
    • 37549056201 scopus 로고    scopus 로고
    • Group AD-tS: impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2
    • Kornak, U., Reynders, E., Dimopoulou, A., van Reeuwijk, J., Fischer, B., Rajab, A., et al. Group AD-tS: impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2. Nat Genet 40 (2008), 32–34.
    • (2008) Nat Genet , vol.40 , pp. 32-34
    • Kornak, U.1    Reynders, E.2    Dimopoulou, A.3    van Reeuwijk, J.4    Fischer, B.5    Rajab, A.6
  • 4
    • 25144464491 scopus 로고    scopus 로고
    • Clinical and biochemical presentation of siblings with COG-7 deficiency, a lethal multiple O- and N-glycosylation disorder
    • Spaapen, L.J., Bakker, J.A., van der Meer, S.B., Sijstermans, H.J., Steet, R.A., Wevers, R.A., et al. Clinical and biochemical presentation of siblings with COG-7 deficiency, a lethal multiple O- and N-glycosylation disorder. J Inherit Metab Dis 28 (2005), 707–714.
    • (2005) J Inherit Metab Dis , vol.28 , pp. 707-714
    • Spaapen, L.J.1    Bakker, J.A.2    van der Meer, S.B.3    Sijstermans, H.J.4    Steet, R.A.5    Wevers, R.A.6
  • 5
    • 33644853797 scopus 로고    scopus 로고
    • Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II
    • Foulquier, F., Vasile, E., Schollen, E., Callewaert, N., Raemaekers, T., Quelhas, D., et al. Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II. Proc Natl Acad Sci U S A 103 (2006), 3764–3769.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 3764-3769
    • Foulquier, F.1    Vasile, E.2    Schollen, E.3    Callewaert, N.4    Raemaekers, T.5    Quelhas, D.6
  • 6
    • 34249730324 scopus 로고    scopus 로고
    • A new inborn error of glycosylation due to a Cog8 deficiency reveals a critical role for the Cog1-Cog8 interaction in COG complex formation
    • Foulquier, F., Ungar, D., Reynders, E., Zeevaert, R., Mills, P., García-Silva, M.T., et al. A new inborn error of glycosylation due to a Cog8 deficiency reveals a critical role for the Cog1-Cog8 interaction in COG complex formation. Hum Mol Genet 16 (2007), 717–730.
    • (2007) Hum Mol Genet , vol.16 , pp. 717-730
    • Foulquier, F.1    Ungar, D.2    Reynders, E.3    Zeevaert, R.4    Mills, P.5    García-Silva, M.T.6
  • 7
    • 70350690698 scopus 로고    scopus 로고
    • Deficiency in COG5 causes a moderate form of congenital disorders of glycosylation
    • Paesold-Burda, P., Maag, C., Troxler, H., Foulquier, F., Kleinert, P., Schnabel, S., et al. Deficiency in COG5 causes a moderate form of congenital disorders of glycosylation. Hum Mol Genet 18 (2009), 4350–4356.
    • (2009) Hum Mol Genet , vol.18 , pp. 4350-4356
    • Paesold-Burda, P.1    Maag, C.2    Troxler, H.3    Foulquier, F.4    Kleinert, P.5    Schnabel, S.6
  • 8
    • 77956096967 scopus 로고    scopus 로고
    • Fatal outcome due to deficiency of subunit 6 of the conserved oligomeric Golgi complex leading to a new type of congenital disorders of glycosylation
    • Lübbehusen, J., Thiel, C., Rind, N., Ungar, D., Prinsen, B.H., de Koning, T.J., et al. Fatal outcome due to deficiency of subunit 6 of the conserved oligomeric Golgi complex leading to a new type of congenital disorders of glycosylation. Hum Mol Genet 19 (2010), 3623–3633.
    • (2010) Hum Mol Genet , vol.19 , pp. 3623-3633
    • Lübbehusen, J.1    Thiel, C.2    Rind, N.3    Ungar, D.4    Prinsen, B.H.5    de Koning, T.J.6
  • 9
    • 84926657074 scopus 로고    scopus 로고
    • Mutations in COG2 encoding a subunit of the conserved oligomeric golgi complex cause a congenital disorder of glycosylation
    • Kodera, H., Ando, N., Yuasa, I., Wada, Y., Tsurusaki, Y., Nakashima, M., et al. Mutations in COG2 encoding a subunit of the conserved oligomeric golgi complex cause a congenital disorder of glycosylation. Clin Genet 87 (2015), 455–460.
    • (2015) Clin Genet , vol.87 , pp. 455-460
    • Kodera, H.1    Ando, N.2    Yuasa, I.3    Wada, Y.4    Tsurusaki, Y.5    Nakashima, M.6
  • 10
    • 84925764199 scopus 로고    scopus 로고
    • N-glycomic changes in serum proteins in type 2 diabetes mellitus correlate with complications and with metabolic syndrome parameters
    • Testa, R., Vanhooren, V., Bonfigli, A.R., Boemi, M., Olivieri, F., Ceriello, A., et al. N-glycomic changes in serum proteins in type 2 diabetes mellitus correlate with complications and with metabolic syndrome parameters. PLoS One, 10, 2015, e0119983.
    • (2015) PLoS One , vol.10
    • Testa, R.1    Vanhooren, V.2    Bonfigli, A.R.3    Boemi, M.4    Olivieri, F.5    Ceriello, A.6
  • 11
    • 84905851466 scopus 로고    scopus 로고
    • Reduced apolipoprotein glycosylation in patients with the metabolic syndrome
    • Savinova, O.V., Fillaus, K., Jing, L., Harris, W.S., Shearer, G.C., Reduced apolipoprotein glycosylation in patients with the metabolic syndrome. PLoS One, 9, 2014, e104833.
    • (2014) PLoS One , vol.9
    • Savinova, O.V.1    Fillaus, K.2    Jing, L.3    Harris, W.S.4    Shearer, G.C.5
  • 12
    • 84901503862 scopus 로고    scopus 로고
    • The effect of malnutrition on protein glycosylation in children
    • Bilen, O., Altun, Z., Arslan, N., Onvural, B., Akan, P., Coker, C., The effect of malnutrition on protein glycosylation in children. Iran J Pediatr 24 (2014), 273–279.
    • (2014) Iran J Pediatr , vol.24 , pp. 273-279
    • Bilen, O.1    Altun, Z.2    Arslan, N.3    Onvural, B.4    Akan, P.5    Coker, C.6
  • 14
    • 0029153494 scopus 로고
    • Abnormal glycosylation of IgA: is it related to the pathogenesis of IgA nephropathy?
    • Allen, A.C., Abnormal glycosylation of IgA: is it related to the pathogenesis of IgA nephropathy?. Nephrol Dial Transplant 10 (1995), 1121–1124.
    • (1995) Nephrol Dial Transplant , vol.10 , pp. 1121-1124
    • Allen, A.C.1
  • 15
    • 77956792736 scopus 로고    scopus 로고
    • Analysis of N- and O-linked protein glycosylation in children with Prader-Willi syndrome
    • Munce, T., Heussler, H.S., Bowling, F.G., Analysis of N- and O-linked protein glycosylation in children with Prader-Willi syndrome. J Intellect Disabil Res 54 (2010), 929–937.
    • (2010) J Intellect Disabil Res , vol.54 , pp. 929-937
    • Munce, T.1    Heussler, H.S.2    Bowling, F.G.3
  • 16
    • 61849158775 scopus 로고    scopus 로고
    • O-glycoside biomarker of apolipoprotein C3: responsiveness to obesity, bariatric surgery, and therapy with metformin, to chronic or severe liver disease and to mortality in severe sepsis and graft vs host disease
    • Harvey, S.B., Zhang, Y., Wilson-Grady, J., Monkkonen, T., Nelsestuen, G.L., Kasthuri, R.S., et al. O-glycoside biomarker of apolipoprotein C3: responsiveness to obesity, bariatric surgery, and therapy with metformin, to chronic or severe liver disease and to mortality in severe sepsis and graft vs host disease. J Proteome Res 8 (2009), 603–612.
    • (2009) J Proteome Res , vol.8 , pp. 603-612
    • Harvey, S.B.1    Zhang, Y.2    Wilson-Grady, J.3    Monkkonen, T.4    Nelsestuen, G.L.5    Kasthuri, R.S.6
  • 18
    • 84866425378 scopus 로고    scopus 로고
    • Gene identification in the congenital disorders of glycosylation type I by whole-exome sequencing
    • Timal, S., Hoischen, A., Lehle, L., Adamowicz, M., Huijben, K., Sykut-Cegielska, J., et al. Gene identification in the congenital disorders of glycosylation type I by whole-exome sequencing. Hum Mol Genet 21 (2012), 4151–4161.
    • (2012) Hum Mol Genet , vol.21 , pp. 4151-4161
    • Timal, S.1    Hoischen, A.2    Lehle, L.3    Adamowicz, M.4    Huijben, K.5    Sykut-Cegielska, J.6
  • 19
    • 84939962655 scopus 로고    scopus 로고
    • Glycogen pathways in disease: new developments in a classical field of medical genetics
    • Kilimann, M.W., Oldfors, A., Glycogen pathways in disease: new developments in a classical field of medical genetics. J Inherit Metab Dis 38 (2015), 483–487.
    • (2015) J Inherit Metab Dis , vol.38 , pp. 483-487
    • Kilimann, M.W.1    Oldfors, A.2
  • 20
    • 85158008888 scopus 로고    scopus 로고
    • Inborn metabolic diseases: diagnosis and treatment
    • Springer
    • Saudubray, J.-M., Baumgartner, M.R., Walter, J.H., Inborn metabolic diseases: diagnosis and treatment. 2016, Springer, 121–135.
    • (2016) , pp. 121-135
    • Saudubray, J.-M.1    Baumgartner, M.R.2    Walter, J.H.3
  • 22
    • 84914146167 scopus 로고    scopus 로고
    • The natural history of glycogen storage disease types VI and IX: long-term outcome from the largest metabolic center in Canada
    • Roscher, A., Patel, J., Hewson, S., Nagy, L., Feigenbaum, A., Kronick, J., et al. The natural history of glycogen storage disease types VI and IX: long-term outcome from the largest metabolic center in Canada. Mol Genet Metab 113 (2014), 171–176.
    • (2014) Mol Genet Metab , vol.113 , pp. 171-176
    • Roscher, A.1    Patel, J.2    Hewson, S.3    Nagy, L.4    Feigenbaum, A.5    Kronick, J.6
  • 23
    • 80052553182 scopus 로고    scopus 로고
    • Liver glycogen storage diseases due to phosphorylase system deficiencies: diagnosis thanks to non invasive blood enzymatic and molecular studies
    • Davit-Spraul, A., Piraud, M., Dobbelaere, D., Valayannopoulos, V., Labrune, P., Habes, D., et al. Liver glycogen storage diseases due to phosphorylase system deficiencies: diagnosis thanks to non invasive blood enzymatic and molecular studies. Mol Genet Metab 104 (2011), 137–143.
    • (2011) Mol Genet Metab , vol.104 , pp. 137-143
    • Davit-Spraul, A.1    Piraud, M.2    Dobbelaere, D.3    Valayannopoulos, V.4    Labrune, P.5    Habes, D.6
  • 24
    • 0037603179 scopus 로고    scopus 로고
    • A novel mutation (G233D) in the glycogen phosphorylase gene in a patient with hepatic glycogen storage disease and residual enzyme activity
    • Tang, N.L., Hui, J., Young, E., Worthington, V., To, K.F., Cheung, K.L., et al. A novel mutation (G233D) in the glycogen phosphorylase gene in a patient with hepatic glycogen storage disease and residual enzyme activity. Mol Genet Metab 79 (2003), 142–145.
    • (2003) Mol Genet Metab , vol.79 , pp. 142-145
    • Tang, N.L.1    Hui, J.2    Young, E.3    Worthington, V.4    To, K.F.5    Cheung, K.L.6
  • 26
    • 84905218061 scopus 로고    scopus 로고
    • Galactose supplementation in phosphoglucomutase-1 deficiency; review and outlook for a novel treatable CDG
    • Morava, E., Galactose supplementation in phosphoglucomutase-1 deficiency; review and outlook for a novel treatable CDG. Mol Genet Metab 112 (2014), 275–279.
    • (2014) Mol Genet Metab , vol.112 , pp. 275-279
    • Morava, E.1
  • 29
    • 84938944596 scopus 로고    scopus 로고
    • Isoelectric focusing of serum apolipoprotein C-III as a sensitive screening method for the detection of O-glycosylation disturbances
    • Ondrušková N., Honzík, T., Kytnarová J., Matoulek, M., Zeman, J., Hansíková H., Isoelectric focusing of serum apolipoprotein C-III as a sensitive screening method for the detection of O-glycosylation disturbances. Prague Med Rep 116 (2015), 73–86.
    • (2015) Prague Med Rep , vol.116 , pp. 73-86
    • Ondrušková, N.1    Honzík, T.2    Kytnarová, J.3    Matoulek, M.4    Zeman, J.5    Hansíková, H.6
  • 30
    • 28444496685 scopus 로고    scopus 로고
    • Patients with unsolved congenital disorders of glycosylation type II can be subdivided in six distinct biochemical groups
    • Wopereis, S., Morava, E., Grünewald, S., Adamowicz, M., Huijben, K.M., Lefeber, D.J., et al. Patients with unsolved congenital disorders of glycosylation type II can be subdivided in six distinct biochemical groups. Glycobiology 15 (2005), 1312–1319.
    • (2005) Glycobiology , vol.15 , pp. 1312-1319
    • Wopereis, S.1    Morava, E.2    Grünewald, S.3    Adamowicz, M.4    Huijben, K.M.5    Lefeber, D.J.6
  • 31
    • 84863201152 scopus 로고    scopus 로고
    • Mass spectrometry of apolipoprotein C-III, a simple analytical method for mucin-type O-glycosylation and its application to an autosomal recessive cutis laxa type-2 (ARCL2) patient
    • Wada, Y., Kadoya, M., Okamoto, N., Mass spectrometry of apolipoprotein C-III, a simple analytical method for mucin-type O-glycosylation and its application to an autosomal recessive cutis laxa type-2 (ARCL2) patient. Glycobiology 22 (2012), 1140–1144.
    • (2012) Glycobiology , vol.22 , pp. 1140-1144
    • Wada, Y.1    Kadoya, M.2    Okamoto, N.3
  • 32
    • 84956671120 scopus 로고    scopus 로고
    • The association of human apolipoprotein C-III sialylation proteoforms with plasma triglycerides
    • Yassine, H.N., Trenchevska, O., Ramrakhiani, A., Parekh, A., Koska, J., Walker, R.W., et al. The association of human apolipoprotein C-III sialylation proteoforms with plasma triglycerides. PLoS One, 10, 2015, e0144138.
    • (2015) PLoS One , vol.10
    • Yassine, H.N.1    Trenchevska, O.2    Ramrakhiani, A.3    Parekh, A.4    Koska, J.5    Walker, R.W.6
  • 33
    • 79958838942 scopus 로고    scopus 로고
    • G6PC3 mutations are associated with a major defect of glycosylation: a novel mechanism for neutrophil dysfunction
    • Hayee, B., Antonopoulos, A., Murphy, E.J., Rahman, F.Z., Sewell, G., Smith, B.N., et al. G6PC3 mutations are associated with a major defect of glycosylation: a novel mechanism for neutrophil dysfunction. Glycobiology 21 (2011), 914–924.
    • (2011) Glycobiology , vol.21 , pp. 914-924
    • Hayee, B.1    Antonopoulos, A.2    Murphy, E.J.3    Rahman, F.Z.4    Sewell, G.5    Smith, B.N.6
  • 34
    • 84921926095 scopus 로고    scopus 로고
    • Pompe disease results in a Golgi-based glycosylation deficit in human induced pluripotent stem cell-derived cardiomyocytes
    • Raval, K.K., Tao, R., White, B.E., De Lange, W.J., Koonce, C.H., Yu, J., et al. Pompe disease results in a Golgi-based glycosylation deficit in human induced pluripotent stem cell-derived cardiomyocytes. J Biol Chem 290 (2015), 3121–3136.
    • (2015) J Biol Chem , vol.290 , pp. 3121-3136
    • Raval, K.K.1    Tao, R.2    White, B.E.3    De Lange, W.J.4    Koonce, C.H.5    Yu, J.6
  • 35
    • 84867426941 scopus 로고
    • Site-specific protein O-glycosylation modulates proprotein processing - deciphering specific functions of the large polypeptide GalNAc-transferase gene family
    • Schjoldager, K.T., Clausen, H., Site-specific protein O-glycosylation modulates proprotein processing - deciphering specific functions of the large polypeptide GalNAc-transferase gene family. Biochim Biophys Acta 2012 (1820), 2079–2094.
    • (1820) Biochim Biophys Acta , vol.2012 , pp. 2079-2094
    • Schjoldager, K.T.1    Clausen, H.2
  • 36
    • 84880665189 scopus 로고    scopus 로고
    • GALNT2 expression is reduced in patients with type 2 diabetes: possible role of hyperglycemia
    • Marucci, A., di Mauro, L., Menzaghi, C., Prudente, S., Mangiacotti, D., Fini, G., et al. GALNT2 expression is reduced in patients with type 2 diabetes: possible role of hyperglycemia. PLoS One, 8, 2013, e70159.
    • (2013) PLoS One , vol.8
    • Marucci, A.1    di Mauro, L.2    Menzaghi, C.3    Prudente, S.4    Mangiacotti, D.5    Fini, G.6
  • 38
    • 84904114675 scopus 로고    scopus 로고
    • Low density lipoprotein-containing circulating immune complexes: role in atherosclerosis and diagnostic value
    • Sobenin, I.A., Salonen, J.T., Zhelankin, A.V., Melnichenko, A.A., Kaikkonen, J., Bobryshev, Y.V., et al. Low density lipoprotein-containing circulating immune complexes: role in atherosclerosis and diagnostic value. Biomed Res Int, 2014, 2014, 205697.
    • (2014) Biomed Res Int , vol.2014 , pp. 205697
    • Sobenin, I.A.1    Salonen, J.T.2    Zhelankin, A.V.3    Melnichenko, A.A.4    Kaikkonen, J.5    Bobryshev, Y.V.6
  • 39
    • 0034680309 scopus 로고    scopus 로고
    • VLDL, apolipoproteins B, CIII, and E, and risk of recurrent coronary events in the cholesterol and recurrent events (CARE) trial
    • Sacks, F.M., Alaupovic, P., Moye, L.A., Cole, T.G., Sussex, B., Stampfer, M.J., et al. VLDL, apolipoproteins B, CIII, and E, and risk of recurrent coronary events in the cholesterol and recurrent events (CARE) trial. Circulation 102 (2000), 1886–1892.
    • (2000) Circulation , vol.102 , pp. 1886-1892
    • Sacks, F.M.1    Alaupovic, P.2    Moye, L.A.3    Cole, T.G.4    Sussex, B.5    Stampfer, M.J.6
  • 40
    • 85018321731 scopus 로고    scopus 로고
    • Association of apolipoprotein-CIII (apoC-III), endothelium-dependent vasodilation and peripheral neuropathy in a multi-ethnic population with type 2 diabetes
    • Pek, S.L.T., Sum, C.F., Yeoh, L.Y., Lee, S.B.M., Tang, W.E., Lim, S.C., et al. Association of apolipoprotein-CIII (apoC-III), endothelium-dependent vasodilation and peripheral neuropathy in a multi-ethnic population with type 2 diabetes. Metabolism 72 (2017), 75–82.
    • (2017) Metabolism , vol.72 , pp. 75-82
    • Pek, S.L.T.1    Sum, C.F.2    Yeoh, L.Y.3    Lee, S.B.M.4    Tang, W.E.5    Lim, S.C.6
  • 41
    • 84869486385 scopus 로고    scopus 로고
    • Identification of lysosomal sialidase NEU1 and plasma membrane sialidase NEU3 in human erythrocytes
    • D'Avila, F., Tringali, C., Papini, N., Anastasia, L., Croci, G., Massaccesi, L., et al. Identification of lysosomal sialidase NEU1 and plasma membrane sialidase NEU3 in human erythrocytes. J Cell Biochem 114 (2013), 204–211.
    • (2013) J Cell Biochem , vol.114 , pp. 204-211
    • D'Avila, F.1    Tringali, C.2    Papini, N.3    Anastasia, L.4    Croci, G.5    Massaccesi, L.6


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