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Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with osteogenesis imperfecta type I-IV.
Hum Mutat. 2006 Jul; 27(7):716.HM

Abstract

Osteogenesis Imperfecta (OI) is a heterogeneous group of inherited disorders characterized by increased bone fragility, with clinical severity ranging from mild to lethal. To date, seven types of OI have been described, based on clinical phenotype and histological findings. Most patients with a clinical diagnosis of OI type I-IV have a mutation in the COL1A1 or COL1A2 genes which encode the two alpha chains of type I collagen, the major component of the bone matrix. Analysis of COL1A1 and COL1A2 in a cohort of 83 unrelated patients with OI type I-IV identified a total of 62 mutations. Thirty-eight appear novel, 26 in COL1A1, and 12 in COL1A2, and these are described here. The largest group consists of point mutations affecting glycine residues in the triple helical domain of the two alpha chains, predicted to disrupt protein folding and structure. This is in accordance with previously published data. A doublet GC deletion, an unusual 398 base deletion predicted to completely remove exon 20 of COL1A2, and a point mutation resulting in substitution of a conserved cysteine in the C-terminal propeptide are described. In addition rare mutations at the cleavage sites of the C-propeptide and the N-terminal signal peptide are described.

Authors+Show Affiliations

Sheffield Molecular Genetics Service, Sheffield Children's NHS Trust, Sheffield, United Kingdom. rebecca.pollitt@sch.nhs.ukNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

16786509

Citation

Pollitt, Rebecca, et al. "Mutation Analysis of COL1A1 and COL1A2 in Patients Diagnosed With Osteogenesis Imperfecta Type I-IV." Human Mutation, vol. 27, no. 7, 2006, p. 716.
Pollitt R, McMahon R, Nunn J, et al. Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with osteogenesis imperfecta type I-IV. Hum Mutat. 2006;27(7):716.
Pollitt, R., McMahon, R., Nunn, J., Bamford, R., Afifi, A., Bishop, N., & Dalton, A. (2006). Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with osteogenesis imperfecta type I-IV. Human Mutation, 27(7), 716.
Pollitt R, et al. Mutation Analysis of COL1A1 and COL1A2 in Patients Diagnosed With Osteogenesis Imperfecta Type I-IV. Hum Mutat. 2006;27(7):716. PubMed PMID: 16786509.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with osteogenesis imperfecta type I-IV. AU - Pollitt,Rebecca, AU - McMahon,Robert, AU - Nunn,Janice, AU - Bamford,Robert, AU - Afifi,Amal, AU - Bishop,Nicholas, AU - Dalton,Ann, PY - 2006/6/21/pubmed PY - 2006/8/8/medline PY - 2006/6/21/entrez SP - 716 EP - 716 JF - Human mutation JO - Hum Mutat VL - 27 IS - 7 N2 - Osteogenesis Imperfecta (OI) is a heterogeneous group of inherited disorders characterized by increased bone fragility, with clinical severity ranging from mild to lethal. To date, seven types of OI have been described, based on clinical phenotype and histological findings. Most patients with a clinical diagnosis of OI type I-IV have a mutation in the COL1A1 or COL1A2 genes which encode the two alpha chains of type I collagen, the major component of the bone matrix. Analysis of COL1A1 and COL1A2 in a cohort of 83 unrelated patients with OI type I-IV identified a total of 62 mutations. Thirty-eight appear novel, 26 in COL1A1, and 12 in COL1A2, and these are described here. The largest group consists of point mutations affecting glycine residues in the triple helical domain of the two alpha chains, predicted to disrupt protein folding and structure. This is in accordance with previously published data. A doublet GC deletion, an unusual 398 base deletion predicted to completely remove exon 20 of COL1A2, and a point mutation resulting in substitution of a conserved cysteine in the C-terminal propeptide are described. In addition rare mutations at the cleavage sites of the C-propeptide and the N-terminal signal peptide are described. SN - 1098-1004 UR - https://www.unboundmedicine.com/medline/citation/16786509/Mutation_analysis_of_COL1A1_and_COL1A2_in_patients_diagnosed_with_osteogenesis_imperfecta_type_I_IV_ L2 - https://doi.org/10.1002/humu.9430 DB - PRIME DP - Unbound Medicine ER -