Activation of the mitogen-activated protein kinase pathway by bone sialoprotein regulates osteoblast differentiation

Cells, Tissues, Organs
Jonathan A R GordonHarvey A Goldberg

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 kina...Continue Reading

Citations

Feb 19, 2010·Tissue Engineering. Part B, Reviews·Lilia Araida Hidalgo-Bastida, Sarah H Cartmell
Jan 15, 2016·Matrix Biology : Journal of the International Society for Matrix Biology·Wafa BouleftourLuc Malaval
Jun 5, 2016·Biological Trace Element Research·Miao SongLi Gao
Feb 4, 2011·Proceedings of the Institution of Mechanical Engineers. Part H, Journal of Engineering in Medicine·M J P Biggs, M J Dalby
Aug 10, 2021·Frontiers in Bioengineering and Biotechnology·Zhikai LinMaria B Asparuhova

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