Characterization of osteoadherin—a novel, cell binding keratan sulfate proteoglycan from bone

Authors

  • Mikael Wendel
  • Yngve Sommarin
  • Dick Heinegård

DOI:

https://doi.org/10.3109/17453679509157655

Abstract

The extracellular matrix of bone is mineralized with crystals of hydroxyapatite. The spatial orientation of the mineral crystals are dependent on the most abundant bone matrix protein, type I collagen. Bone also contains a number of non-collagenous proteins that appear to have important roles in various aspects of tissue homeostasis (Heinegård and Oldberg 1993, Young et al. 1992). During the last two decades several proteins have been isolated from bone tissue and characterized. Much interest has been focused on osteocalcin, matrix gla-protein, osteonectin, osteo-pontin, bone sialoprotein, and the small proteoglycans; decorin and biglycan. Still, in most cases very little is known about their functions in the tissue.

Downloads

Download data is not yet available.

Downloads

Published

1995-01-01

How to Cite

Wendel, M., Sommarin, Y., & Heinegård, D. (1995). Characterization of osteoadherin—a novel, cell binding keratan sulfate proteoglycan from bone. Acta Orthopaedica, 66(sup266), 77–77. https://doi.org/10.3109/17453679509157655