Rose N J, Mackay K, Byers P H, Dalgleish R
Department of Genetics, University of Leicester, UK.
Hum Genet. 1995 Feb;95(2):215-8. doi: 10.1007/BF00209405.
In general, osteogenesis imperfecta (brittle bone disease) is caused by heterozygous mutations in the genes encoding the alpha 1 or alpha 2 chains of type I collagen (COL1A1 and COL1A2, respectively). In this study we screened these genes in a proband presenting with the severe form (type III) of osteogenesis imperfecta for mutations which might result in the phenotype. Single-strand conformation polymorphism mapping analysis was used to identify a region suspected of harbouring the mutation and subsequent sequence analysis revealed a heterozygous G to A transition in the alpha 2(I) gene of type I collagen in the individual. The resulting substitution of the glycine at position 238 of the alpha chain by serine is the most N-terminal yet reported for this chain.
一般来说，成骨不全症（脆骨病）是由分别编码I型胶原蛋白α1或α2链的基因（分别为COL1A1和COL1A2）中的杂合突变引起的。在本研究中，我们对一名患有严重形式（III型）成骨不全症的先证者进行了这些基因的筛查，以寻找可能导致该表型的突变。采用单链构象多态性图谱分析来鉴定疑似存在突变的区域，随后的序列分析揭示该个体I型胶原蛋白的α2（I）基因中存在一个从G到A的杂合转换。α链第238位的甘氨酸被丝氨酸取代，这是该链迄今报道的最靠近N端的替换。
