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Studies on type I collagen in skin fibroblasts cultured from twins with lethal osteogenesis imperfecta

100%

Galicka A., Wolczynski S., Gindzienski A.

Acta Biochimica Polonica

2003

tom 50

nr 2

Studies on type I procollagen produced by skin fibroblasts cultured from twins with lethal type II of osteogenesis imperfecta (OI) showed that biosynthesis of collagen (measured by l-[5- 3H]proline incorporation into proteins susceptible to the action of bacterial collagenase) was slightly increased as compared to the control healthy infant. SDS/PAGE showed that the fibroblasts synthesized and secreted only normal type I procollagen. Electrophoretic analysis of collagen chains and CNBr peptides showed the same pattern of electrophoretic migration as in the controls. The lack of posttranslational overmodification of the collagen molecule suggested a molecular defect near the amino terminus of the collagen helix. Digestion of OI type I collagen with trypsin at 30°C for 5 min generated a shorter than normal a2 chain which melted at 36°C. Direct sequencing of an asymmetric PCR product revealed a heterozygous single nucleotide change C->G causing a substitution of histidine by aspartic acid in the a2 chain at position 92. Pericellular processing of type I procollagen by the twin's fibroblasts yielded a later appearance of the intermediate pC-ai(I) form as compared with control cells.

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

80%

Galicka A., Wolczynski S., Lesniewicz R., Chyczewski L., Gindzienski A.

Acta Biochimica Polonica

2002

tom 49

nr 2

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.

Ograniczanie wyników

2 Acta Biochimica Polonica

2 Galicka A.

2 Gindzienski A.

2 Wolczynski S.

1 Chyczewski L.

1 Lesniewicz R.

1 2003

1 2002

Wyniki wyszukiwania

Studies on type I collagen in skin fibroblasts cultured from twins with lethal osteogenesis imperfecta

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