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Vol. 189, No. 1-4, 2009
Issue release date: December 2008
Section title: Paper
Cells Tissues Organs 2009;189:138–143
(DOI:10.1159/000151728)

Activation of the Mitogen-Activated Protein Kinase Pathway by Bone Sialoprotein Regulates Osteoblast Differentiation

Gordon J.A.R. · Hunter G.K. · Goldberg H.A.
Department of Biochemistry and Schulich Dentistry, CIHR Group in Skeletal Development and Remodeling, Schulich School of Medicine & Dentistry, University of Western Ontario, London, Ont., Canada

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Article / Publication Details

First-Page Preview
Abstract of Paper

Published online: 8/26/2008
Issue release date: December 2008

Number of Print Pages: 6
Number of Figures: 3
Number of Tables: 0

ISSN: 1422-6405 (Print)
eISSN: 1422-6421 (Online)

For additional information: http://www.karger.com/CTO

Abstract

Bone sialoprotein (BSP) is an abundant protein in the extracellular matrix of bone that has been suggested to have several different physiological functions, including the nucleation of hydroxyapatite (HA), promotion of cell attachment and binding of collagen. Studies in our lab have demonstrated that increased expression of BSP in osteoblast cells can increase expression of the osteoblast-related genes Runx2 and Osx as well as alkaline phosphatase and osteocalcin and increase matrix mineralization. To determine the molecular mechanisms responsible for the BSP-mediated increase in osteoblastic differentiation, several functional domain mutants of BSP were expressed in primary rat bone osteoblastic cells, including the contiguous glutamic acid sequences (polyGlu) and the arginine-glycine-aspartic acid (RGD) motif. Markers of osteoblast differentiation, including matrix mineralization and alkaline phosphatase staining, were increased in cells expressing BSP mutants of the polyGlu sequences but not in cells expressing RGD-mutated BSP. We also determined the dependence on integrin-associated pathways in promoting BSP-mediated differentiation responses in osteoblasts by demonstrating the activation of focal adhesion kinase, MAP kinase-associated proteins ERK1/2, ribosomal s6 kinase 2 and the AP-1 protein cFos. Thus, the mechanism regulating osteoblast differentiation by BSP was determined to be dependent on integrin-mediated intracellular signaling pathways.


  

Author Contacts

Dr. Harvey A. Goldberg
CIHR Group in Skeletal Development and Remodeling
Schulich School of Medicine & Dentistry, University of Western Ontario
Dental Sciences Building, London, ON N6A 5C1 (Canada)
Tel. +1 519 661 2182, Fax +1 519 850 2459, E-Mail hagoldbe@uwo.ca

  

Article Information

Published online: August 26, 2008
Number of Print Pages : 6
Number of Figures : 3, Number of Tables : 0, Number of References : 24

  

Publication Details

Cells Tissues Organs (in vivo, in vitro)

Vol. 189, No. 1-4, Year 2009 (Cover Date: December 2008)

Journal Editor: Denker H.-W. (Essen), English A.W. (Atlanta, Ga.)
ISSN: 1422-6405 (Print), eISSN: 1422-6421 (Online)

For additional information: http://www.karger.com/CTO


Article / Publication Details

First-Page Preview
Abstract of Paper

Published online: 8/26/2008
Issue release date: December 2008

Number of Print Pages: 6
Number of Figures: 3
Number of Tables: 0

ISSN: 1422-6405 (Print)
eISSN: 1422-6421 (Online)

For additional information: http://www.karger.com/CTO


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