A novel Gly to Arg substitution at position 388 of the alpha1 chain of type I collagen in lethal form of osteogenesis imperfecta

• Autorzy: Galicka A. , Wolczynski S. , Lesniewicz R. , Chyczewski L. , Gindzienski A.
• Języki publikacji: EN

Abstrakty

EN

Cultured skin fibroblasts from a proband with a lethal form of osteogenesis imperfecta produce two forms of type I collagen chains, with normal and delayed elec- trophoretic migration; collagen of the proband's mother was normal. Peptide map­ping experiments localized the structural defect in the proband to a 1(I) CB8 peptide in which residues 123 to 402 are spaned. Direct sequencing of amplified cDNA covering this region revealed a G to A single base change in one allele of the al(I) chain, that converted glycine 388 to arginine. Restriction enzyme digestion of the RT-PCR prod­uct was consistent with a heterozygous COL1A1 mutation. The novel mutation con­forms to the linear gradient of clinical severity for the αl(I) chain and results in re­duced thermal stability by 3°C and intracellular retention of abnormal molecules.

Słowa kluczowe

EN

thermal stability; skin; osteogenesis; peptide; lethal form; intracellular retention; mutation; collagen chain; collagen; abnormal molecule; fibroblast

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2002
• Tom: 49
• Numer: 2
• Opis fizyczny: p.443-450,fig.

Twórcy

autor

Galicka A.

• Medical Academy of Bialystok, 15-230 Bialystok 8, Poland

autor

Wolczynski S.

autor

Lesniewicz R.

autor

Chyczewski L.

autor

Gindzienski A.

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