Characterization of osteoadherin—a novel, cell binding keratan sulfate proteoglycan from bone
DOI:
https://doi.org/10.3109/17453679509157655Abstract
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
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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
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Acta Orthopaedica (Scandinavica) content is available freely online as from volume 1, 1930. The journal owner owns the copyright for all material published until volume 80, 2009. As of June 2009, the journal has however been published fully Open Access, meaning the authors retain copyright to their work. As of June 2009, articles have been published under CC-BY-NC or CC-BY licenses, unless otherwise specified.
