Wnt/β-catenin inhibits dental pulp stem cell differentiation

被引:120
作者
Scheller, E. L. [1 ]
Chang, J. [2 ]
Wang, C. Y. [1 ,2 ]
机构
[1] Univ Michigan, Sch Dent, Mol Signalling Lab, Dept Biol & Mat Sci, Ann Arbor, MI 48109 USA
[2] Univ Calif Los Angeles, Sch Dent, Mol Signalling Lab, Div Oral Biol & Med, Los Angeles, CA 90095 USA
关键词
Wnt; mineralization; stem cell; dental pulp; osteopontin;
D O I
10.1177/154405910808700206
中图分类号
R78 [口腔科学];
学科分类号
1003 ;
摘要
Dental pulp stem cells (DPSCs) are a unique precursor population isolated from post-natal human dental pulp and have the ability to regenerate a reparative dentin-like complex. Canonical Wnt signaling plays a critical role in tooth development and stem cell self-renewal through beta-catenin. In this study, the regulation of odontoblast-like differentiation of DPSCs by canonical Wnt signaling was examined. DPSCs were stably transduced with canonical Wnt-1 or the active form of beta-catenin, with retrovirus-mediated infection. Northern blot analysis found that Wnt-1 strongly induced the expression of matricellular protein osteopontin, and modestly enhanced the expression of type I collagen in DPSCs. Unexpectedly, Wnt-1 inhibited alkaline phosphatase (ALP) activity and the formation of mineralized nodules in DPSCs. Moreover, overexpression of beta-catenin was also sufficient to suppress the differentiation and mineralization of DPSCs. In conclusion, our results suggest that canonical Wnt signaling negatively regulates the odontoblast-like differentiation of DPSCs. Abbreviations used: DPSC, dental pulp stem cell; ALP, alkaline phosphatase; BSP, bone sialoprotein; MSC, mesenchymal stem cell; beta-GP, beta-glycerophosphate; APC, adenomatous polyposis coli; GSK-3 beta, glycogen synthase kinase-3 beta; LRP, LDL receptor-related protein; Tcf, T-cell factor; LEF, lymphoid enhancer factor; FCS, fetal calf serum; AA, L-ascorbic acid 2-phosphate; alpha-MEM, alpha-modified Eagle's medium; PBS, phosphate-buffered saline; HA, hemagglutinin; ON, osteonectin; OPN, osteopontin.
引用
收藏
页码:126 / 130
页数:5
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