Abstract
The purpose of this study was to describe a family with spondyloepiphyseal dysplasia caused by a novel type II collagen gene (COL2A1) mutation and the family’s phenotypic diversity. Clinical and radiographic examinations of skeletal dysplasia were conducted on seven affected family members across two generations. The entire coding region of COL2A1, including the flanking intron regions, was analyzed with PCR and direct sequencing. The stature of the subjects ranged from extremely short to within normal height range. Hip deformity and advanced osteoarthritis were noted in all the subjects, ranging from severe coxa plana to mild acetabular dysplasia. Atlantoaxial subluxation combined with a hypoplastic odontoid process was found in three of the subjects. Various degrees of platyspondyly were confirmed in all subjects. Genetically, a novel COL2A1 mutation (c.1349G>C, p.Gly450Ala) was identified in all the affected family members; however, it was not present in the one unaffected family member tested. We described a family with spondyloepiphyseal dysplasia and a novel COL2A1 mutation (c.1349G>C, p.Gly450Ala). Phenotypes were diverse even among individuals with the same mutation and within the same family.
Highlights
The purpose of this study was to describe a family with spondyloepiphyseal dysplasia caused by a novel type II collagen gene (COL2A1) mutation and the family’s phenotypic diversity
Clinical and radiographic examinations of skeletal dysplasia were conducted on seven affected family members across two generations
We described a family with spondyloepiphyseal dysplasia and a novel COL2A1 mutation (c.1349G4C, p.Gly450Ala)
Summary
A novel type II collagen gene mutation in a family with spondyloepiphyseal dysplasia and extensive intrafamilial phenotypic diversity. The purpose of this study was to describe a family with spondyloepiphyseal dysplasia caused by a novel type II collagen gene (COL2A1) mutation and the family’s phenotypic diversity. We describe a Japanese family with SED caused by a novel COL2A1 mutation This mutation predominantly affected the hip joint and spine of the affected individuals in this family. Plain radiographs showed joint space narrowing without acetabular dysplasia and atlantoaxial subluxation and platyspondyly in her thoracolumbar spine (Figure 1a–c) It was predicted to cause an amino-acid substitution from a glycine to an alanine at codon 450 (p.Gly450Ala) and to disrupt a well-regulated Gly–X–Y motif in the triple helical domain This novel mutation was identified in all the other six affected individuals, but was not found in the one normal individual.
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