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

• Autorzy: Galicka A. , Wolczynski S. , Gindzienski A.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

skin; bone; extracellular matrix; protein; collagen chain; collagen; osteogenesis imperfecta; fibroblast; tissue

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 2
• Opis fizyczny: p.481-488,fig.

Twórcy

autor

Galicka A.

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

autor

Wolczynski S.

autor

Gindzienski A.

Bibliografia

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