Glycine to tryptophan substitution in type I collagen in a patient with OI type III: a unique collagen mutation
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چکیده
منابع مشابه
Glycine to tryptophan substitution in type I collagen in a patient with OI type III: a unique collagen mutation.
We report a unique glycine substitution in type I collagen and highlight the clinical and biochemical consequences. The proband is a 9 year old Turkish boy with severely deforming osteogenesis imperfecta (OI). Biochemical analysis of (pro) collagen type I from a skin fibroblast culture showed both normal and overmodified alpha chains. Molecular analysis showed a G>T transversion in the COL1A2 g...
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Platelet interaction with type III collagen is mediated by several platelet receptors that recognize specific sequences in collagen. We previously described an octapeptide KP*GEP*GPK within the alpha(1)III-CB4 fragment that binds to platelets and specifically inhibits platelet aggregation induced by type III collagen. In this study, we demonstrated that the octapeptide prevented platelet contac...
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Type I collagen is the most abundant and ubiquitously distributed of the collagen family of proteins. It is a heterotrimer comprising two alpha1(I) chains and one alpha2(I) chain which are encoded by the unlinked loci COL1A1 and COL1A2 respectively. Mutations at these loci result primarily in the connective tissue disorders osteogenesis imperfecta and Ehlers-Danlos syndrome types VIIA and VIIB....
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ژورنال
عنوان ژورنال: Journal of Medical Genetics
سال: 2000
ISSN: 1468-6244
DOI: 10.1136/jmg.37.5.371