메뉴 건너뛰기




Volumn 23, Issue 21, 2012, Pages 4175-4187

A zebrafish model of PMM2-CDG reveals altered neurogenesis and a substrate-accumulation mechanism for N-linked glycosylation deficiency

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE DIPHOSPHATE MANNOSE; LIPOOLIGOSACCHARIDE; MANNOSE 1 PHOSPHATE; MANNOSE 6 PHOSPHATE; MANNOSE PHOSPHATE; MANNOSE PHOSPHATE ISOMERASE; PHOSPHOMANNOMUTASE; UNCLASSIFIED DRUG;

EID: 84868248946     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E12-05-0411     Document Type: Article
Times cited : (44)

References (44)
  • 2
    • 84872093842 scopus 로고    scopus 로고
    • A zebrafish model of congenital disorders of glycosylation with phosphomannose isomerase deficiency reveals an early opportunity for corrective mannose supplementation
    • DOI: 10.1242/dmm.010116
    • Chu J, Mir A, Gao N, Rosa S, Monson C, Sharma V, Steet R, Freeze HH, Lehrman MA, Sadler KC (2012). A zebrafish model of congenital disorders of glycosylation with phosphomannose isomerase deficiency reveals an early opportunity for corrective mannose supplementation. Dis Model Mech, DOI: 10.1242/dmm.010116.
    • (2012) Dis Model Mech
    • Chu, J.1    Mir, A.2    Gao, N.3    Rosa, S.4    Monson, C.5    Sharma, V.6    Steet, R.7    Freeze, H.H.8    Lehrman, M.A.9    Sadler, K.C.10
  • 4
    • 43449103089 scopus 로고    scopus 로고
    • The skeletal manifestations of the congenital disorders of glycosylation
    • DOI 10.1111/j.1399-0004.2008.01015.x
    • Coman D, Irving M, Kannu P, Jaeken J, Savarirayan R (2008). The skeletal manifestations of the congenital disorders of glycosylation. Clin Genet 73, 507-515. (Pubitemid 351663929)
    • (2008) Clinical Genetics , vol.73 , Issue.6 , pp. 507-515
    • Coman, D.1    Irving, M.2    Kannu, P.3    Jaeken, J.4    Savarirayan, R.5
  • 7
    • 0034491915 scopus 로고    scopus 로고
    • Defect in N-glycosylation of proteins is tissue-dependent in Congenital Disorders of Glycosylation Ia
    • Dupre T, Barnier A, de Lonlay P, Cormier-Daire V, Durand G, Codogno P, Seta N (2000). Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia. Glycobiology 10, 1277-1281. (Pubitemid 32124325)
    • (2000) Glycobiology , vol.10 , Issue.12 , pp. 1277-1281
    • Dupre, T.1    Barnier, A.2    De Lonlay, P.3    Cormier-Daire, V.4    Durand, G.5    Codogno, P.6    Seta, N.7
  • 8
    • 33749208029 scopus 로고    scopus 로고
    • Morphants: A new systematic vertebrate functional genomics approach
    • DOI 10.1002/1097-0061(200012)17:4 <302::AID-YEA53>3.0.CO;2-#
    • Ekker SC (2000). Morphants: a new systematic vertebrate functional genomics approach. Yeast 17, 302-306. (Pubitemid 32051423)
    • (2000) Comparative and Functional Genomics , vol.17 , Issue.4 , pp. 302-306
    • Ekker, S.C.1
  • 9
    • 27744602432 scopus 로고    scopus 로고
    • Neuromuscular synapses can form in vivo by incorporation of initially aneural postsynaptic specializations
    • DOI 10.1242/dev.02044
    • Flanagan-Steet H, Fox MA, Meyer D, Sanes JR (2005). Neuromuscular synapses can form in vivo by incorporation of initially aneural postsynaptic specializations. Development 132, 4471-4481. (Pubitemid 41632226)
    • (2005) Development , vol.132 , Issue.20 , pp. 4471-4481
    • Flanagan-Steet, H.1    Fox, M.A.2    Meyer, D.3    Sanes, J.R.4
  • 10
    • 73649091413 scopus 로고    scopus 로고
    • Altered chondrocyte differentiation and extracellular matrix homeostasis in a zebrafish model for mucolipidosis II
    • Flanagan-Steet H, Sias C, Steet R (2009). Altered chondrocyte differentiation and extracellular matrix homeostasis in a zebrafish model for mucolipidosis II. Am J Pathol 175, 2063-2075.
    • (2009) Am J Pathol , vol.175 , pp. 2063-2075
    • Flanagan-Steet, H.1    Sias, C.2    Steet, R.3
  • 11
    • 0035716899 scopus 로고    scopus 로고
    • Update and perspectives on congenital disorders of glycosylation
    • Freeze HH (2001). Update and perspectives on congenital disorders of glycosylation. Glycobiology 11, 129R-143R. (Pubitemid 34162761)
    • (2001) Glycobiology , vol.11 , Issue.12
    • Freeze, H.H.1
  • 12
    • 70249111204 scopus 로고    scopus 로고
    • Towards a therapy for phosphomannomutase 2 deficiency, the defect in CDG-Ia patients
    • Freeze HH (2009). Towards a therapy for phosphomannomutase 2 deficiency, the defect in CDG-Ia patients. Biochim Biophys Acta 1792, 835-840.
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 835-840
    • Freeze, H.H.1
  • 14
    • 33751017369 scopus 로고    scopus 로고
    • Non-radioactive analysis of lipid-linked oligosaccharide compositions by fluorophore-assisted carbohydrate electrophoresis
    • DOI 10.1016/S0076-6879(06)15001-6, PII S0076687906150016, Glycobiology
    • Gao N, Lehrman MA (2006). Non-radioactive analysis of lipid-linked oligosaccharide compositions by fluorophore-assisted carbohydrate electrophoresis. Methods Enzymol 415, 3-20. (Pubitemid 44751087)
    • (2006) Methods in Enzymology , vol.415 , pp. 3-20
    • Gao, N.1    Lehrman, M.A.2
  • 15
    • 24044524496 scopus 로고    scopus 로고
    • Analysis of glycosylation in CDG-Ia fibroblasts by fluorophore-assisted carbohydrate electrophoresis: Implications for extracellular glucose and intracellular mannose 6-phosphate
    • DOI 10.1074/jbc.M500510200
    • Gao N, Shang J, Lehrman MA (2005). Analysis of glycosylation in CDG-Ia fibroblasts by fluorophore-assisted carbohydrate electrophoresis: implications for extracellular glucose and intracellular mannose 6-phosphate. J Biol Chem 280, 17901-17909. (Pubitemid 41389031)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 17901-17909
    • Gao, N.1    Shang, J.2    Lehrman, M.A.3
  • 16
    • 80052199103 scopus 로고    scopus 로고
    • Mannose-6-phosphate regulates destruction of lipidlinked oligosaccharides
    • Gao N et al. (2011). Mannose-6-phosphate regulates destruction of lipidlinked oligosaccharides. Mol Biol Cell 22, 2994-3009.
    • (2011) Mol Biol Cell , vol.22 , pp. 2994-3009
    • Gao, N.1
  • 17
    • 71749102704 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: An update on defects affecting the biosynthesis of dolichol-linked oligosaccharides
    • Haeuptle MA, Hennet T (2009). Congenital disorders of glycosylation: an update on defects affecting the biosynthesis of dolichol-linked oligosaccharides. Hum Mutat 30, 1628-1641.
    • (2009) Hum Mutat , vol.30 , pp. 1628-1641
    • Haeuptle, M.A.1    Hennet, T.2
  • 18
    • 79953198270 scopus 로고    scopus 로고
    • Improvement of dolichol-linked oligosaccharide biosynthesis by the squalene synthase inhibitor zaragozic acid
    • Haeuptle MA, Welti M, Troxler H, Hulsmeier AJ, Imbach T, Hennet T (2011). Improvement of dolichol-linked oligosaccharide biosynthesis by the squalene synthase inhibitor zaragozic acid. J Biol Chem 286, 6085-6091.
    • (2011) J Biol Chem , vol.286 , pp. 6085-6091
    • Haeuptle, M.A.1    Welti, M.2    Troxler, H.3    Hulsmeier, A.J.4    Imbach, T.5    Hennet, T.6
  • 20
    • 84861568354 scopus 로고    scopus 로고
    • Identification of intercellular cell adhesion molecule 1 (ICAM-1) as a hypo-glycosylation marker in congenital disorders of glycosylation cells
    • He P, Ng BG, Losfeld ME, Zhu W, Freeze HH (2012). Identification of intercellular cell adhesion molecule 1 (ICAM-1) as a hypo-glycosylation marker in congenital disorders of glycosylation cells. J Biol Chem 287, 18210-18217.
    • (2012) J Biol Chem , vol.287 , pp. 18210-18217
    • He, P.1    Ng, B.G.2    Losfeld, M.E.3    Zhu, W.4    Freeze, H.H.5
  • 21
    • 61849174783 scopus 로고    scopus 로고
    • Exogenous mannose does not raise steady state mannose-6-phosphate pools of normal or N-glycosylation-deficient human fibroblasts
    • Higashidani A, Bode L, Nishikawa A, Freeze HH (2009). Exogenous mannose does not raise steady state mannose-6-phosphate pools of normal or N-glycosylation-deficient human fibroblasts. Mol Genet Metab 96, 268-272.
    • (2009) Mol Genet Metab , vol.96 , pp. 268-272
    • Higashidani, A.1    Bode, L.2    Nishikawa, A.3    Freeze, H.H.4
  • 24
    • 0035089105 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: Glycosylation defects in man and biological models for their study
    • DOI 10.1515/BC.2001.024
    • Marquardt T, Freeze H (2001). Congenital disorders of glycosylation: glycosylation defects in man and biological models for their study. Biol Chem 382, 161-177. (Pubitemid 32248677)
    • (2001) Biological Chemistry , vol.382 , Issue.2 , pp. 161-177
    • Marquardt, T.1    Freeze, H.2
  • 25
    • 0029986521 scopus 로고    scopus 로고
    • Carbohydrate-deficient glycoprotein syndrome type I: Determination of the oligosaccharide structure of newly synthesized glycoproteins by analysis of calnexin binding
    • DOI 10.1007/BF01799441
    • Marquardt T, Ullrich K, Niehues R, Koch HG, Harms E (1996). Carbohydratedeficient glycoprotein syndrome type I: determination of the oligosaccharide structure of newly synthesized glycoproteins by analysis of calnexin binding. J Inherit Metab Dis 19, 246-250. (Pubitemid 26137526)
    • (1996) Journal of Inherited Metabolic Disease , vol.19 , Issue.2 , pp. 246-250
    • Marquardt, T.1    Ullrich, K.2    Niehues, R.3    Koch, H.-G.4    Harms, E.5
  • 26
    • 0028962872 scopus 로고
    • Carbohydrate-deficient glycoprotein syndrome (CDGS)-glycosylation, folding and intracellular transport of newly synthesized glycoproteins
    • Marquardt T, Ullrich K, Zimmer P, Hasilik A, Deufel T, Harms E (1995). Carbohydrate-deficient glycoprotein syndrome (CDGS)-glycosylation, folding and intracellular transport of newly synthesized glycoproteins. Eur J Cell Biol 66, 268-273.
    • (1995) Eur J Cell Biol , vol.66 , pp. 268-273
    • Marquardt, T.1    Ullrich, K.2    Zimmer, P.3    Hasilik, A.4    Deufel, T.5    Harms, E.6
  • 27
    • 0031005847 scopus 로고    scopus 로고
    • Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type 1 syndrome (Jaeken syndrome)
    • Matthijs G, Schollen E, Pardon E, Veiga-Da-Cunha M, Jaeken J, Cassiman JJ, Van Schaftingen E (1997). Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type I syndrome (Jaeken syndrome). Nat Genet 16, 88-92. (Pubitemid 27198162)
    • (1997) Nature Genetics , vol.16 , Issue.1 , pp. 88-92
    • Matthijs, G.1    Schollen, E.2    Pardon, E.3    Veiga-Da-Cunha, M.4    Jaeken, J.5    Cassiman, J.-J.6    Van Schaftingen, E.7
  • 28
    • 0031836642 scopus 로고    scopus 로고
    • Mannose supplementation in carbohydrate-deficient glycoprotein syndrome type I and phosphomannomutase deficiency [1]
    • DOI 10.1007/s004310050889
    • Mayatepek E, Kohlmuller D (1998). Mannose supplementation in carbohydrate-deficient glycoprotein syndrome type I and phosphomannomutase deficiency. Eur J Pediatr 157, 605-606. (Pubitemid 28311493)
    • (1998) European Journal of Pediatrics , vol.157 , Issue.7 , pp. 605-606
    • Mayatepek, E.1    Kohlmuller, D.2
  • 30
    • 81455136719 scopus 로고    scopus 로고
    • The feelgood mutation in zebrafish dysregulates COPII-dependent secretion of select extracellular matrix proteins in skeletal morphogenesis
    • Melville DB, Montero-Balaguer M, Levic DS, Bradley K, Smith JR, Hatzopoulos AK, Knapik EW (2011). The feelgood mutation in zebrafish dysregulates COPII-dependent secretion of select extracellular matrix proteins in skeletal morphogenesis. Dis Mech Model 4, 763-776.
    • (2011) Dis Mech Model , vol.4 , pp. 763-776
    • Melville, D.B.1    Montero-Balaguer, M.2    Levic, D.S.3    Bradley, K.4    Smith, J.R.5    Hatzopoulos, A.K.6    Knapik, E.W.7
  • 32
    • 68549115664 scopus 로고    scopus 로고
    • Neuroepithelial cells require fucosylated glycans to guide the migration of vagus motor neuron progenitors in the developing zebrafish hindbrain
    • Ohata S, Kinoshita S, Aoki R, Tanaka H, Wada H, Tsuruoka-Kinoshita S, Tsuboi T, Watabe S, Okamoto H (2009). Neuroepithelial cells require fucosylated glycans to guide the migration of vagus motor neuron progenitors in the developing zebrafish hindbrain. Development 136, 1653-1663.
    • (2009) Development , vol.136 , pp. 1653-1663
    • Ohata, S.1    Kinoshita, S.2    Aoki, R.3    Tanaka, H.4    Wada, H.5    Tsuruoka-Kinoshita, S.6    Tsuboi, T.7    Watabe, S.8    Okamoto, H.9
  • 33
    • 0029984537 scopus 로고    scopus 로고
    • Mannose corrects altered N-glycosylation in carbohydrate-deficient glycoprotein syndrome fibroblasts
    • Panneerselvam K, Freeze HH (1996). Mannose corrects altered N-glycosylation in carbohydrate-deficient glycoprotein syndrome fibroblasts. J Clin Invest 97, 1478-1487. (Pubitemid 26097038)
    • (1996) Journal of Clinical Investigation , vol.97 , Issue.6 , pp. 1478-1487
    • Panneerselvam, K.1    Freeze, H.H.2
  • 35
    • 84897928868 scopus 로고    scopus 로고
    • Seizures and stupor during intravenous mannose therapy in a patient with CDG syndrome type 1b (MPI-CDG)
    • DOI: 10.1007/s10545-010-9252-x
    • Schroeder AS, Kappler M, Bonfert M, Borggraefe I, Schoen C, Reiter K (2011). Seizures and stupor during intravenous mannose therapy in a patient with CDG syndrome type 1b (MPI-CDG). J Inherit Metab Dis, DOI: 10.1007/s10545-010- 9252-x.
    • (2011) J Inherit Metab Dis
    • Schroeder, A.S.1    Kappler, M.2    Bonfert, M.3    Borggraefe, I.4    Schoen, C.5    Reiter, K.6
  • 36
    • 1642350828 scopus 로고    scopus 로고
    • Metformin-stimulated mannose transport in dermal fibroblasts
    • DOI 10.1074/jbc.M310837200
    • Shang J, Lehrman MA (2004). Metformin-stimulated mannose transport in dermal fibroblasts. J Biol Chem 279, 9703-9712. (Pubitemid 38372568)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.11 , pp. 9703-9712
    • Shang, J.1    Lehrman, M.A.2
  • 37
    • 33847339711 scopus 로고    scopus 로고
    • Translation attenuation by PERK balances ER glycoprotein synthesis with lipid-linked oligosaccharide flux
    • DOI 10.1083/jcb.200607007
    • Shang J, Gao N, Kaufman RJ, Ron D, Harding H P, Lehrman MA (2007). Translation attenuation by PERK balances ER glycoprotein synthesis with lipid-linked oligosaccharide flux. J Cell Biol 176, 605-616. (Pubitemid 46333976)
    • (2007) Journal of Cell Biology , vol.176 , Issue.5 , pp. 605-616
    • Shang, J.1    Gao, N.2    Kaufman, R.J.3    Ron, D.4    Harding, H.P.5    Lehrman, M.A.6
  • 38
    • 0036020877 scopus 로고    scopus 로고
    • Extension of lipid-linked oligosaccharides is a high-priority aspect of the unfolded protein response: Endoplasmic reticulum stress in Type I congenital disorder of glycosylation fibroblasts
    • Shang J, Korner C, Freeze H, Lehrman MA (2002). Extension of lipid-linked oligosaccharides is a high-priority aspect of the unfolded protein response: endoplasmic reticulum stress in type I congenital disorder of glycosylation fibroblasts. Glycobiology 12, 307-317. (Pubitemid 34812049)
    • (2002) Glycobiology , vol.12 , Issue.5 , pp. 307-317
    • Shang, J.1    Korner, C.2    Freeze, H.3    Lehrman, M.A.4
  • 39
    • 80655144748 scopus 로고    scopus 로고
    • Phosphomannose isomerase inhibitors improve N-glycosylation in selected phosphomannomutase-deficient fibroblasts
    • Sharma V, Ichikawa M, He P, Scott DA, Bravo Y, Dahl R, Ng BG, Cosford ND, Freeze HH (2011). Phosphomannose isomerase inhibitors improve N-glycosylation in selected phosphomannomutase-deficient fibroblasts. J Biol Chem 286, 39431-39438.
    • (2011) J Biol Chem , vol.286 , pp. 39431-39438
    • Sharma, V.1    Ichikawa, M.2    He, P.3    Scott, D.A.4    Bravo, Y.5    Dahl, R.6    Ng, B.G.7    Cosford, N.D.8    Freeze, H.H.9
  • 41
    • 33746578432 scopus 로고    scopus 로고
    • Targeted disruption of the mouse phosphomannomutase 2 gene causes early embryonic lethality
    • DOI 10.1128/MCB.02391-05
    • Thiel C, Lubke T, Matthijs G, von Figura K, Korner C (2006). Targeted disruption of the mouse phosphomannomutase 2 gene causes early embryonic lethality. Mol Cell Biol 26, 5615-5620. (Pubitemid 44134320)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.15 , pp. 5615-5620
    • Thiel, C.1    Lubke, T.2    Matthijs, G.3    Von Figura, K.4    Korner, C.5
  • 42
    • 38149126474 scopus 로고    scopus 로고
    • High-resolution in situ hybridization to wholemount zebrafish embryos
    • Thisse C, Thisse B (2008). High-resolution in situ hybridization to wholemount zebrafish embryos. Nat Protoc 3, 59-69.
    • (2008) Nat Protoc , vol.3 , pp. 59-69
    • Thisse, C.1    Thisse, B.2
  • 43
    • 0029585865 scopus 로고
    • Phosphomannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I
    • DOI 10.1016/0014-5793(95)01357-1
    • Van Schaftingen E, Jaeken J (1995). Phosphomannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I. FEBS Lett 377, 318-320. (Pubitemid 26027149)
    • (1995) FEBS Letters , vol.377 , Issue.3 , pp. 318-320
    • Van Schaftingen, E.1    Jaeken, J.2
  • 44
    • 84861427459 scopus 로고    scopus 로고
    • Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery
    • Zielinska DF, Gnad F, Schropp K, Wisniewski JR, Mann M (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46, 542-548.
    • (2012) Mol Cell , vol.46 , pp. 542-548
    • Zielinska, D.F.1    Gnad, F.2    Schropp, K.3    Wisniewski, J.R.4    Mann, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.