osteochondrodysplasias/arginine

A child with typical spondyloepiphyseal dysplasia congenita had a recurrent, heterozygous substitution of arginine 789 by cysteine in the triple helical domain of alpha 1 (II) chains of type II collagen. The amino substitution was due to the transition of cytosine 2913 to thymine in exon 41 of the

A child with spondyloepiphyseal dysplasia congenita was shown to be heterozygous for a mutation of the COL2A1 gene that encodes the alpha 1 (II) chain of type II collagen. The alpha 1 (II) chains extracted from cartilage contained disulfide-bonded dimeric and trimeric alpha 1 (II) chains.

OBJECTIVE To characterize a kindred of Chiloe Islanders with spondyloepiphyseal dysplasia tarda (SEDT), brachydactyly, precocious osteoarthritis (OA), and intraarticular calcification. METHODS Sixteen family members underwent a complete physical examination, anthropometric measurements, radiographic

BACKGROUND The majority of COL2A1 missense mutations are substitutions of obligatory glycine residues in the triple helical domain. Only a few non-glycine missense mutations have been reported and among these, the arginine to cysteine substitutions predominate. OBJECTIVE To investigate in more

Inherited point mutations in collagen II in humans affecting mainly cartilage are broadly classified as chondrodysplasias. Most mutations occur in the glycine (Gly) of the Gly-X-Y repeats leading to destabilization of the triple helix. Arginine to cysteine substitutions that occur at either the X or

OBJECTIVE To identify the genetic defect in a four-generation pedigree with X-linked recessive spondyloepiphyseal dysplasia tarda (SEDT) from Southwest China. METHODS Linkage analysis with one panel of fluorescently labeled microsatellite markers on chromosome X and mutation screening of SEDL gene

A missense mutation in the mouse Col2a1 gene has been discovered, resulting in a mouse phenotype with similarities to human spondyloepiphyseal dysplasia (SED) congenita. In addition, SED patients have been identified with a similar molecular mutation in human COL2A1. This mouse model offers a useful

Multiple epiphyseal dysplasia (MED) can result from mutations in matrilin-3, a structural protein of the cartilage extracellular matrix. We have previously shown that in a mouse model of MED the tibia growth plates were normal at birth but developed a progressive dysplasia characterised by the

OBJECTIVE To define the genetic basis of a family with an autosomal, dominantly inherited form of spondyloepiphyseal dysplasia (SED) associated with tall stature. METHODS A 6 generation family with early onset osteoarthritis (OA) associated with mild SED was studied. 14 individuals were examined

OBJECTIVE To define the clinical, pathological and molecular genetic characteristics of a family with mild spondyloepiphyseal dysplasia (SED) and precocious osteoarthritis. METHODS The proband was a 46-year-old man with precocious generalized OA, tall stature, mild chondrodysplasia and moderate

OBJECTIVE An arginine-to-cysteine substitution at position 519 of the COL2A1 gene causes early generalized osteoarthritis with mild chondrodysplasia in humans. In this study, a human COL2A1 gene with the same mutation was introduced into a murine genome having 1 or no alleles of the murine Col2a1

Identifying mutations that cause specific osteochondrodysplasias will provide novel insights into the function of genes that are essential for skeletal morphogenesis. We report here that an autosomal dominant form of Stickler syndrome, characterized by mild spondyloepiphyseal dysplasia,

Heterozygous COL2A1 variants cause a wide spectrum of skeletal dysplasia termed type II collagenopathies. We assessed the impact of this gene in our French series. A decision tree was applied to select 136 probands (71 Stickler cases, 21 Spondyloepiphyseal dysplasia congenita cases, 11 Kniest

Arginine519-cysteine mutation in the type II procollagen gene (COL2A1) is known to be associated with mild spondyloepiphyseal dysplasia (SED) and precocious generalized osteoarthritis (OA). Five families have now been identified with this mutation. To determine whether a common founder was

achondroplasia (ACH) and hypochondroplasia (HCH) into the routine practice. BACKGROUND Both disorders are usually caused by de novo gain-of-function type mutations in FGFR3 gene encoding the fibroblast growth factor receptor 3, which plays an important role in the metabolism of connective tissues.