CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta
Article Abstract:
The Cartilage Association Protein (CRTAP) which copurifies with a collagen prolyl 3-hydroxylase activity is involved in osteogenesis imperfecta and mutations are associated with brittle bones in patients with a spectrum of mild to severe recessive osteogenesis imperfecta. Hence altered CRTAP function and prolyl 3-hydroxylation contribute to the connective tissue disease.
author: Schwarze, Ulrike, Byers, Peter H., Bachinger, Hans Peter, Hicks, John, Lee, Brendan, Boyce, Brendan F., Yuqing Chen, Morello, Roy, Bertin, Terry K., Eyre, David R., Yao, Zhenqiang, Monticone, Massimiliano, Castagnola, Patrizio, Rauch, Frank, Glorieux, Francis H., Vranka, Janice, Pace, James M., Weis, Mary Ann, Fernandes, Russell J.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
Science & research, Analysis, Causes of, Hydroxylation
Human Ehlers-Danlos syndrome type VII C and bovine dermatosparaxis are caused by mutations in the procollagen I N-proteinase gene
Article Abstract:
Bovine dermatosparaxis and human Ehlers-Danlos syndrome (EDS) type VIIC, a recessively inherited connective-tissue disorder, are discussed in relation to the finding that they are both caused by mutations in the procollagen I N-proteinase (pNPI) gene and the resulting lack of activity of pNPI. Bovine cDNA was used to isolate human pNPI to identify the mutations.
author: Schwarze, Ulrike, Byers, Peter H., Prockop, Darwin J., Cohn, Daniel H., Krakow, Deborah, Reardon, W., Colige, Alain, Sieron, Aleksander L., Li, Shi-Wu, Petty, Elizabeth, Wertelecki, Wladimir, Wilcox, William, Lapiere, Charles M., Nusgens, Betty V.
Publisher: University of Chicago Press
Publication Name: American Journal of Human Genetics
Subject: Biological sciences
ISSN: 0002-9297
Year: 1999
United Kingdom, Belgium, Cattle
Redefinition of exon 7 in the COL1A1 (ital) gene of Type I collagen by an intron 8 splice-donor-site mutation in a form of osteogenesis imperfecta: influence of intron splice order on outcome of splice-site mutation
Article Abstract:
Identification of a point mutation in the 5' donor sequence of intron 8 of the Type I collagen gene, COL1A1 (ital) in a form of osteogenesis imperfecta, and unexpected splice outcomes, among them redefinition of the upstream exon 7, are discussed. Implications about the influence of intron splice order on outcome of splice-site mutation were seen.
author: Schwarze, Ulrike, Byers, Peter H., Starman, Barbra J.
Publisher: University of Chicago Press
Publication Name: American Journal of Human Genetics
Subject: Biological sciences
ISSN: 0002-9297
Year: 1999
Gene mutations, Gene mutation, Collagen, RNA splicing, Introns
subjects list: Research, Osteogenesis imperfecta, Connective tissue diseases, Statistical Data Included, United States, Usage, Genetic aspects, Chromosome mapping, Genetic disorders
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