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Papers In Press, published online ahead of print September 13, 2004
Oral Medicine and Pathology, University of Pittsburgh, Pittsburgh, PA 15261
Corresponding Author: csfeir{at}pitt.edu
Extracellular matrix proteins (ECM) serve as both a structural support for cells and also as a dynamic bionetwork that directs cellular activities. ECM proteins such as those of the SIBLING family (Small Integrin-Binding Ligand Glycoprotein) could possess inherent growth factor activity. In this study, we demonstrate that exon 5 of Dentin Matrix Protein 3 (phosphophoryn (PP)), a non-collagenous dentin ECM protein and SIBLING protein family member, up-regulates osteoblast marker genes in primary human adult mesenchymal stem cells (hMSC), a mouse osteoblastic cell line (MC3T3-E1), and a mouse fibroblastic cell line (NIH3T3). Quantitative real-time PCR (qPCR) technology was used to quantify gene expression levels of bone markers such as Runx2, Osterix (Osx), bone/liver/kidney alkaline phosphatase (Alp), Osteocalcin (Ocn) and bone sialoprotein (Bsp) in response to recombinant PP (rPP) and transgenic PP (tPP) . PP up-regulated Runx2, Osx and Ocn gene expression. PP increased OCN protein production in hMSC and MC3T3-E1. ALP activity and calcium deposition was increased by PP in hMSC. Further, an avß3 integrin-blocking antibody significantly inhibited rPP-induced expression of Runx2 in hMSC, suggesting that signaling by PP is mediated through the integrin pathway. PP was also shown to activate p38, Erk1/2 and Jnk, three components of the MAP kinase pathway. These data demonstrate a novel signaling function for PP in cell differentiation beyond the hypothesized role of PP in biomineralization.
J. Biol. Chem, 10.1074/jbc.M404934200
Submitted on May 4, 2004
Revised on August 24, 2004
Accepted on September 13, 2004
Phosphophoryn regulates the gene expression and differentiation of NIH3T3, MC3T3-E1 and human mesenchymal stem cells via integrin/MAPK signaling pathway
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