A single amino acid deletion in the alpha 2(I) chain of type I collagen produces osteogenesis imperfecta type III.

Article Details

Citation

Molyneux K, Starman BJ, Byers PH, Dalgleish R

A single amino acid deletion in the alpha 2(I) chain of type I collagen produces osteogenesis imperfecta type III.

Hum Genet. 1993 Feb;90(6):621-8.

PubMed ID
8444468 [ View in PubMed
]
Abstract

RNase A protection analysis was used in the search for the cause of a non-lethal osteogenesis imperfecta (OI) phenotype (Sillence type III). Cleavage of the hybrid formed between a normal alpha 2(I) sequence and RNA isolated from the patient indicated the presence of a mismatch. The position of the mismatch was determined and the corresponding area of COL1A2 was amplified using the polymerase chain reaction. Sequencing of cloned amplified DNA revealed the deletion, which was not present in either parent, of the final three bases of exon 19 in one of the patient's two COL1A2 alleles. The deletion results in the loss of amino acid 255 (a valine encoded by the last codon of exon 19) of the triple helical region of half of the alpha 2(I) collagen chains but does not disrupt the splicing of the heterogeneous nuclear RNA (hnRNA). This provides further evidence that OI type III may result from autosomal dominant mutations rather than only from autosomal recessive mutations as had previously been believed.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Collagen alpha-2(I) chainP08123Details