Missense and silent mutations in COL2A1 result in Stickler syndrome but via different molecular mechanisms
| Autor: | Allan J. Richards, Arabella V. Poulson, Martin P. Snead, Maureen Laidlaw, John D. Scott, Sarah P Meredith, Pallavi Shankar |
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| Rok vydání: | 2007 |
| Předmět: |
Adult
Male Silent mutation Heterozygote Collagen helix DNA Mutational Analysis Nonsense-mediated decay Mutation Missense Biology medicine.disease_cause Exon Osteoarthritis Genetics medicine Humans Missense mutation Stickler syndrome Collagen Type II Cells Cultured Genetics (clinical) Genes Dominant Mutation Polymorphism Genetic Mosaicism Palate Homozygote Retinal Detachment Exons Syndrome Fibroblasts medicine.disease Molecular biology Pedigree Vitreous Body Alternative Splicing Amino Acid Substitution Female Haploinsufficiency |
| Zdroj: | Human Mutation. 28:639-639 |
| ISSN: | 1098-1004 1059-7794 |
| Popis: | Stickler syndrome due to mutations in COL2A1 is usually the result of premature termination codons and nonsense mediated decay resulting in haploinsufficiency of type II collagen. Here we present two missense mutations and one apparently silent mutation that each result in Stickler syndrome, but via different molecular mechanisms. One alters the translation initiating ATG codon. The second mutation is a unique glycine substitution in the minor collagen helix of the procollagen. To our knowledge a glycine substitution has not previously been reported in this region of fibrillar procollagens. The third mutation appears to be a silent change altering a GGC codon to GGT both for glycine, but use of a splicing reporter assay demonstrates that it results in missplicing and a shift in the reading frame. |
| Databáze: | OpenAIRE |
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