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Affinity of bone sialoprotein and several other bone and dentin acidic proteins to collagen fibrils

Affinity of bone sialoprotein and several other bone and dentin acidic proteins to collagen fibrils Bone and dentin contain several kinds of mineral-binding proteins and cell-attachment proteins. The authors examined the affinity of these proteins to type I collagen, a major matrix protein of the tissue. Bone sialoprotein (BSP), bone Gla protein (BGP), bone small proteoglycan II (PG II), osteonectin (ON), and dentin phosphophoryn (DPP) were labeled with fluorescein isothiocyanate and incubated with reconstituted type I collagen fibril. DPP, BGP, BSP, and PG II were absorbed significantly to the collagen fibril at physiological ionic strength with dissociation constants of 10-6–10-7 M. BSP and PG II enhanced the fibrillogenesis of collagen. These acidic proteins can affect the surface properties of collagen fibril, and BSP, having the cell-attachment sequence Arg-Gly-Asp, possibly mediates interaction between collagen fibril and cells. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Calcified Tissue International Springer Journals

Affinity of bone sialoprotein and several other bone and dentin acidic proteins to collagen fibrils

Fujisawa, K.; Kuboki, Y.
Calcified Tissue International , Volume 51 (6) – Aug 19, 2004
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References (34)

Publisher
Springer Journals
Copyright
Copyright © 1992 by Springer-Verlag New York Inc
Subject
Life Sciences; Biochemistry, general; Endocrinology; Orthopedics; Cell Biology
ISSN
0171-967X
eISSN
1432-0827
DOI
10.1007/BF00296677
Publisher site
See Article on Publisher Site

Abstract

Bone and dentin contain several kinds of mineral-binding proteins and cell-attachment proteins. The authors examined the affinity of these proteins to type I collagen, a major matrix protein of the tissue. Bone sialoprotein (BSP), bone Gla protein (BGP), bone small proteoglycan II (PG II), osteonectin (ON), and dentin phosphophoryn (DPP) were labeled with fluorescein isothiocyanate and incubated with reconstituted type I collagen fibril. DPP, BGP, BSP, and PG II were absorbed significantly to the collagen fibril at physiological ionic strength with dissociation constants of 10-6–10-7 M. BSP and PG II enhanced the fibrillogenesis of collagen. These acidic proteins can affect the surface properties of collagen fibril, and BSP, having the cell-attachment sequence Arg-Gly-Asp, possibly mediates interaction between collagen fibril and cells.

Journal

Calcified Tissue International – Springer Journals

Published: Aug 19, 2004

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