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2003 | 50 | 2 | 481-488
Article title

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

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Abstracts
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 α2 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 α2 chain at position 92. Pericellular processing of type I procollagen by the twin's fibroblasts yielded a later appearance of the intermediate pC-α1(I) form as compared with control cells.
Publisher

Year
Volume
50
Issue
2
Pages
481-488
Physical description
Dates
published
2003
received
2003-03-04
revised
2003-05-26
accepted
2003-06-10
Contributors
author
  • Department of Medical Chemistry, Medical Academy of Bialystok, Bialystok, Poland
  • Department of Gynaecological Endocrinology, Medical Academy of Bialystok, Bialystok, Poland
  • Department of Medical Chemistry, Medical Academy of Bialystok, Bialystok, Poland
References
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv50i2p481kz
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