Advanced search
1 file | 853.04 KB

Mutations in the region encoding the von Willebrand factor A domain of matrilin-3 are associated with multiple epiphyseal dysplasia

(2001) NATURE GENETICS. 28(4). p.393-396
Author
Organization
Abstract
Multiple epiphyseal dysplasia (MED) is a relatively mild and clinically variable osteochondrodysplasia, primarily characterized by delayed and irregular ossification of the epiphyses and early-onset osteoarthritis(1-3). Mutations in the genes encoding cartilage oligomeric matrix protein (COMP) and type IX collagen (COL9A2 and COL9A3) have previously been shown to cause different forms of MED (refs. 4-13). These dominant forms of MED (EDM1-3) are caused by mutations in the genes encoding structural proteins of the cartilage extracellular matrix (ECM); these proteins interact with high affinity in vitro(14,15). A recessive form of MED (EDM4) has also been reported; it is caused by a mutation in the diastrophic dysplasia sulfate transporter gene(16) (SLC26A). A genomewide screen of family with autosomal-dominant MED not linked to the EDM1-3 genes(17) provides significant genetic evidence for a MED locus on the short arm of chromosome 2 (2p24-p23), and a search for candidate genes identified MATN3 (ref. 18), encoding matrilin-3, within the critical region. Matrilin-3 is an oligomeric protein that is present in the cartilage ECM. We have identified two different missense mutations in the exon encoding the von Willebrand factor A (vWFA) domain of matrilin-3 in two unrelated families with MED (EDM5). These are the first mutations to be identified in any of the genes encoding the matrilin family of proteins and confirm a role for matrilin-3 in the development and homeostasis of cartilage and bone.
Keywords
MYOPATHY, STATURE, IDENTIFICATION, COMP, CHAIN, GENE, PSEUDOACHONDROPLASIA, CARTILAGE, COLLAGEN-IX, OLIGOMERIC MATRIX PROTEIN

Downloads

    • full text
    • |
    • UGent only
    • |
    • PDF
    • |
    • 853.04 KB

Citation

Please use this url to cite or link to this publication:

Chicago
Chapman, Kathryn L, Geert Mortier, Kay Chapman, John Loughlin, Michael E Grant, and Michael D Briggs. 2001. “Mutations in the Region Encoding the Von Willebrand Factor A Domain of Matrilin-3 Are Associated with Multiple Epiphyseal Dysplasia.” Nature Genetics 28 (4): 393–396.
APA
Chapman, K. L., Mortier, G., Chapman, K., Loughlin, J., Grant, M. E., & Briggs, M. D. (2001). Mutations in the region encoding the von Willebrand factor A domain of matrilin-3 are associated with multiple epiphyseal dysplasia. NATURE GENETICS, 28(4), 393–396.
Vancouver
1.
Chapman KL, Mortier G, Chapman K, Loughlin J, Grant ME, Briggs MD. Mutations in the region encoding the von Willebrand factor A domain of matrilin-3 are associated with multiple epiphyseal dysplasia. NATURE GENETICS. 2001;28(4):393–6.
MLA
Chapman, Kathryn L, Geert Mortier, Kay Chapman, et al. “Mutations in the Region Encoding the Von Willebrand Factor A Domain of Matrilin-3 Are Associated with Multiple Epiphyseal Dysplasia.” NATURE GENETICS 28.4 (2001): 393–396. Print.
@article{169326,
  abstract     = {Multiple epiphyseal dysplasia (MED) is a relatively mild and clinically variable osteochondrodysplasia, primarily characterized by delayed and irregular ossification of the epiphyses and early-onset osteoarthritis(1-3). Mutations in the genes encoding cartilage oligomeric matrix protein (COMP) and type IX collagen (COL9A2 and COL9A3) have previously been shown to cause different forms of MED (refs. 4-13). These dominant forms of MED (EDM1-3) are caused by mutations in the genes encoding structural proteins of the cartilage extracellular matrix (ECM); these proteins interact with high affinity in vitro(14,15). A recessive form of MED (EDM4) has also been reported; it is caused by a mutation in the diastrophic dysplasia sulfate transporter gene(16) (SLC26A). A genomewide screen of family with autosomal-dominant MED not linked to the EDM1-3 genes(17) provides significant genetic evidence for a MED locus on the short arm of chromosome 2 (2p24-p23), and a search for candidate genes identified MATN3 (ref. 18), encoding matrilin-3, within the critical region. Matrilin-3 is an oligomeric protein that is present in the cartilage ECM. We have identified two different missense mutations in the exon encoding the von Willebrand factor A (vWFA) domain of matrilin-3 in two unrelated families with MED (EDM5). These are the first mutations to be identified in any of the genes encoding the matrilin family of proteins and confirm a role for matrilin-3 in the development and homeostasis of cartilage and bone.},
  author       = {Chapman, Kathryn L and Mortier, Geert and Chapman, Kay and Loughlin, John and Grant, Michael E and Briggs, Michael D},
  issn         = {1061-4036},
  journal      = {NATURE GENETICS},
  keyword      = {MYOPATHY,STATURE,IDENTIFICATION,COMP,CHAIN,GENE,PSEUDOACHONDROPLASIA,CARTILAGE,COLLAGEN-IX,OLIGOMERIC MATRIX PROTEIN},
  language     = {eng},
  number       = {4},
  pages        = {393--396},
  title        = {Mutations in the region encoding the von Willebrand factor A domain of matrilin-3 are associated with multiple epiphyseal dysplasia},
  url          = {http://dx.doi.org/10.1038/ng573},
  volume       = {28},
  year         = {2001},
}

Altmetric
View in Altmetric
Web of Science
Times cited: