Profiling the Changes in Signaling Pathways in Ascorbic Acid/beta-Glycerophosphate-Induced Osteoblastic Differentiation

Author(s)

Chaves Neto, Antonio Hernandes ^[1] ; Queiroz, Karla Cristiana ^{[1, 2]} ; Milani, Renato ^[1] ; Paredes-Gamero, Edgar Julian ^[3] ; Justo, Giselle Zenker ^{[3, 1]} ; Peppelenbosch, Maikel P. ^[2] ; Ferreira, Carmen Verissima ^[1]

Affiliation

^[1] Univ Estadual Campinas, Inst Biol, Dept Bioquim, BR-13083970 Campinas, SP - Brazil

^[2] Univ Groningen, Dept Cell Biol, Univ Med Ctr Groningen, NL-9713 AV Groningen - Netherlands

^[3] Univ Fed Sao Paulo, Dept Bioquim, Sao Paulo - Brazil

• Document type: Journal article
• Source: Journal of Cellular Biochemistry; v. 112, n. 1, p. 71-77, JAN 2011.
• Web of Science Citations: 7

Abstract

Despite numerous reports on the ability of ascorbic acid and beta-glycerophosphate (AA/beta-GP) to induce osteoblast differentiation, little is known about the molecular mechanisms involved in this phenomenon. In this work, we used a peptide array containing specific consensus sequences (potential substrates) for protein kinases and traditional biochemical techniques to examine the signaling pathways modulated during AA/beta-GP-induced osteoblast differentiation. The kinomic profile obtained after 7 days of treatment with AA/beta-GP identified 18 kinase substrates with significantly enhanced or reduced phosphorylation. Peptide substrates for Akt, PI3K, PKC, BCR, ABL, PRKG1, PAK1, PAK2, ERK1, ERBB2, and SYK showed a considerable reduction in phosphorylation, whereas enhanced phosphorylation was observed in substrates for CHKB, CHKA, PKA, FAK, ATM, PKA, and VEGFR-1. These findings confirm the potential usefulness of peptide microarrays for identifying kinases known to be involved in bone development in vivo and in vitro and show that this technique can be used to investigate kinases whose function in osteoblastic differentiation is poorly understood. J. Cell. Biochem. 112: 71-77, 2011. (C) 2010 Wiley-Liss, Inc. (AU)