Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-210.

Détails

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Etat: Public
Version: Author's accepted manuscript
ID Serval
serval:BIB_553E9AB0C92F
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-210.
Périodique
The New England journal of medicine
Auteur⸱e⸱s
Smits P., Bolton A.D., Funari V., Hong M., Boyden E.D., Lu L., Manning D.K., Dwyer N.D., Moran J.L., Prysak M., Merriman B., Nelson S.F., Bonafé L., Superti-Furga A., Ikegawa S., Krakow D., Cohn D.H., Kirchhausen T., Warman M.L., Beier D.R.
ISSN
1533-4406 (Electronic)
ISSN-L
0028-4793
Statut éditorial
Publié
Date de publication
21/01/2010
Peer-reviewed
Oui
Volume
362
Numéro
3
Pages
206-216
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Establishing the genetic basis of phenotypes such as skeletal dysplasia in model organisms can provide insights into biologic processes and their role in human disease.
We screened mutagenized mice and observed a neonatal lethal skeletal dysplasia with an autosomal recessive pattern of inheritance. Through genetic mapping and positional cloning, we identified the causative mutation.
Affected mice had a nonsense mutation in the thyroid hormone receptor interactor 11 gene (Trip11), which encodes the Golgi microtubule-associated protein 210 (GMAP-210); the affected mice lacked this protein. Golgi architecture was disturbed in multiple tissues, including cartilage. Skeletal development was severely impaired, with chondrocytes showing swelling and stress in the endoplasmic reticulum, abnormal cellular differentiation, and increased cell death. Golgi-mediated glycosylation events were altered in fibroblasts and chondrocytes lacking GMAP-210, and these chondrocytes had intracellular accumulation of perlecan, an extracellular matrix protein, but not of type II collagen or aggrecan, two other extracellular matrix proteins. The similarities between the skeletal and cellular phenotypes in these mice and those in patients with achondrogenesis type 1A, a neonatal lethal form of skeletal dysplasia in humans, suggested that achondrogenesis type 1A may be caused by GMAP-210 deficiency. Sequence analysis revealed loss-of-function mutations in the 10 unrelated patients with achondrogenesis type 1A whom we studied.
GMAP-210 is required for the efficient glycosylation and cellular transport of multiple proteins. The identification of a mutation affecting GMAP-210 in mice, and then in humans, as the cause of a lethal skeletal dysplasia underscores the value of screening for abnormal phenotypes in model organisms and identifying the causative mutations.

Mots-clé
Animals, Cell Differentiation, Cell Proliferation, Chondrocytes/cytology, Codon, Nonsense, Endoplasmic Reticulum/ultrastructure, Genes, Recessive, Glycosylation, Golgi Apparatus/ultrastructure, Humans, Mice, Mice, Mutant Strains, Nuclear Proteins/deficiency, Nuclear Proteins/genetics, Osteochondrodysplasias/genetics, Phenotype, Polymorphism, Single Nucleotide, Protein Processing, Post-Translational/physiology, Sequence Analysis, DNA
Pubmed
Web of science
Open Access
Oui
Création de la notice
02/02/2010 11:52
Dernière modification de la notice
20/08/2019 14:09
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