Extracellular matrix formation by osteoblasts from patients with osteogenesis imperfecta

Neal S. Fedarko, Martin Moerike, Rolf Brenner, Pamela Gehron Robey, Ulrich Vetter

Research output: Contribution to journalArticlepeer-review

Abstract

Extracellular matrix proteins synthesized by bone cells isolated from 16 patients with different forms of osteogenesis imperfecta (OI) were analyzed in vitro. Specific components of the extracellular matrix by OI and age‐matched cultures were investigated by steady‐state radiolabeling followed by quantitation of label into specific proteins and comparison of OI cultures to those of age‐matched controls. The in vitro proliferation of OI bone cells was found to be lower than that of control cells. In seven patients, abnormalities of the α1(I) and/or α2(I) chains of type I collagen were detected by gel electrophoresis. In two of these patients, the mutations in the COLIA1 and COLIA2 genes have been previously identified. Although the amount of total protein synthesized by the cells in culture was the same for OI bone cells and age‐matched control cells, OI bone cells showed a significantly reduced synthesis of not only collagen but also other bone matrix glycoproteins. The synthesis of osteonectin (SPARC/BM40) and three proteoglycans [a large chondroitin sulfate proteoglycan, biglycan (PGI), and decorin (PGII)] was found to be decreased in OI cells. The reduction was most pronounced at the developmental age at which these macromolecules reach maximal levels during normal development.

Original languageEnglish (US)
Pages (from-to)921-930
Number of pages10
JournalJournal of Bone and Mineral Research
Volume7
Issue number8
DOIs
StatePublished - Aug 1992
Externally publishedYes

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Orthopedics and Sports Medicine

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