MAN1B1 Deficiency: An Unexpected CDG-II (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• MAN1B1 Deficiency: An Unexpected CDG-II (Articolo in rivista) (literal)

Anno

• 2013-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1371/journal.pgen.1003989 (literal)

Alternative label

• Daisy Rymen, Romain Peanne, María B Millón, Valérie Race, Luisa Sturiale, Domenico Garozzo, Philippa Mills, Peter Clayton, Carla G Asteggiano, Dulce Quelhas, Ali Cansu, Esmeralda Martins, Marie-Cécile Nassogne, Miguel Gonçalves-Rocha, Haluk Topaloglu, Jaak Jaeken, François Foulquier, Gert Matthijs (2013)
  MAN1B1 Deficiency: An Unexpected CDG-II
  in PLOS genetics (Online); PUBLIC LIBRARY OF SCIENCE, SAN FRANCISCO (Stati Uniti d'America)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Daisy Rymen, Romain Peanne, María B Millón, Valérie Race, Luisa Sturiale, Domenico Garozzo, Philippa Mills, Peter Clayton, Carla G Asteggiano, Dulce Quelhas, Ali Cansu, Esmeralda Martins, Marie-Cécile Nassogne, Miguel Gonçalves-Rocha, Haluk Topaloglu, Jaak Jaeken, François Foulquier, Gert Matthijs (literal)

Pagina inizio

• e1003989 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://www.plosgenetics.org/article/info%3Adoi%2F10.1371%2Fjournal.pgen.1003989#pgen-1003989-g007 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 9 (literal)

Rivista

• PLOS genetics (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 13 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 12 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Daisy Rymen, Romain Peanne, Valérie Race, Gert Matthijs Center for Human Genetics, University of Leuven, Leuven, Belgium Daisy Rymen, Jaak Jaeken Center for Metabolic Diseases, University Hospital Gasthuisberg, Leuven, Belgium María B. Millón, Carla G. Asteggiano Centro de Estudio Metabalopatías Congénitas, Faculdad de Ciencias Médicas, Universidad Nacional de Córdoba, Hospital de Niños de la Santísima Trinidad, Córdoba, Argentina Luisa Sturiale, Domenico Garozzo Institute of Chemistry and Technology of Polymers, CNR, Catania, Italy Philippa Mills, Peter Clayton Clinical & Molecular Genetics Unit, Institute of Child Health, University College and Great Ormond Street Hospital for Children NHS Trust, London, United Kingdom Dulce Quelhas, Miguel Gonçalves-Rocha Unidade de Genética Médica, Departamento de Genética Humana, Centro de Genética Médica - Dr. Jacinto Magalhães - INSA, IP. Porto, Portugal Ali Cansu Gazi University Faculty of Medicine, Department of Paediatric Neurology, Besevler/Ankara, Turkey Esmeralda Martins Unidade de Doenças Metabólicas, Hospital de Crianças Maria Pia, Porto, Portugal Marie-Cécile Nassogne Université Catholique de Louvain, Cliniques Universitaires Saint-Luc, Brussels, Belgium Haluk Topaloglu Department of Child Neurology, Hacettepe University Children's Hospital, Ankara, Turkey François Foulquier Structural and Functional Glycobiology Unit, UMR CNRS/USTL 8576, IFR 147, University of Lille 1, Villeneuve d'Ascq, France (literal)

Titolo

• MAN1B1 Deficiency: An Unexpected CDG-II (literal)

Abstract

• Congenital disorders of glycosylation (CDG) are a group of rare metabolic diseases, due to impaired protein and lipid glycosylation. In the present study, exome sequencing was used to identify MAN1B1 as the culprit gene in an unsolved CDG-II patient. Subsequently, 6 additional cases with MAN1B1-CDG were found. All individuals presented slight facial dysmorphism, psychomotor retardation and truncal obesity. Generally, MAN1B1 is believed to be an ER resident alpha-1,2-mannosidase acting as a key factor in glycoprotein quality control by targeting misfolded proteins for ER-associated degradation (ERAD). However, recent studies indicated a Golgi localization of the endogenous MAN1B1, suggesting a more complex role for MAN1B1 in quality control. We were able to confirm that MAN1B1 is indeed localized to the Golgi complex instead of the ER. Furthermore, we observed an altered Golgi morphology in all patients' cells, with marked dilatation and fragmentation. We hypothesize that part of the phenotype is associated to this Golgi disruption. In conclusion, we linked mutations in MAN1B1 to a Golgi glycosylation disorder. Additionally, our results support the recent findings on MAN1B1 localization. However, more work is needed to pinpoint the exact function of MAN1B1 in glycoprotein quality control, and to understand the pathophysiology of its deficiency. (literal)

Editore

• PUBLIC LIBRARY OF SCIENCE (Editore)

Prodotto di

• Istituto di chimica e tecnologia dei polimeri (ICTP) (Istituto)
• Glicomica e Proteomica per la ricerca di biomarcatori per la diagnosi e la terapia di patologie congenite, tumorali e infiammatorie. (PM.P06.013.001) (Modulo)

Autore CNR

• LUISELLA STURIALE (Persona)
• DOMENICO GAROZZO (Unità di personale interno)

Incoming links:

Autore CNR di

• DOMENICO GAROZZO (Unità di personale interno)
• LUISELLA STURIALE (Persona)

Prodotto

• Istituto di chimica e tecnologia dei polimeri (ICTP) (Istituto)
• Glicomica e Proteomica per la ricerca di biomarcatori per la diagnosi e la terapia di patologie congenite, tumorali e infiammatorie. (PM.P06.013.001) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• PLOS genetics (Rivista)

Editore di

• PUBLIC LIBRARY OF SCIENCE (Editore)