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Calcified Tissue International

, Volume 60, Issue 6, pp 554–560 | Cite as

Increased Turnover of Small Proteoglycans Synthesized by Human Osteoblasts During Cultivation with Ascorbate and β-Glycerophosphate

  • P.  Blumberg
  • R.  Brenner
  • S.  Budny
  • H.  Kresse
Article

Abstract.

The small proteoglycan decorin had been localized previously at the d-band in the gap zone of collagen fibrils in nonmineralizing tissues. In bone matrix this zone is proteoglycan free and is at least in some species the place where mineralization along collagen fibrils starts. To study the metabolism of the small proteoglycans decorin and biglycan under mineralizing conditions, osteoblasts from human nasal bone were cultured for several weeks in the presence or absence of β-glycerophosphate and ascorbate. An immediate consequence of the treatment was a reduced expression of decorin, as judged by immune precipitation, whereas the biosynthesis of biglycan was not affected. Pulse-chase experiments were performed with osteoblasts embedded in floating type I collagen gels. In the presence of β-glycerophosphate and ascorbate, a more rapid turnover of both proteoglycans was noted; the one of biglycan reached statistical significance. Indirect evidence for an enhanced rate of proteoglycan endocytosis was obtained. This effect was not seen in cultured skin fibroblasts. Thus, osteoblasts respond rapidly to mineralizing conditions with alterations of small proteoglycan biosynthesis and turnover.

Key words

Decorin — Biglycan — Collagen gel — Osteoblasts — Vomer. 

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Copyright information

© Springer-Verlag New York Inc. 1997

Authors and Affiliations

  • P.  Blumberg
    • 1
  • R.  Brenner
    • 2
  • S.  Budny
    • 1
  • H.  Kresse
    • 1
  1. 1.Institute of Physiological Chemistry and Pathobiochemistry, University of MünsterMünsterGermany
  2. 2.Children's Hospital, University of BonnBonnGermany

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