2008
DOI: 10.1016/j.cellsig.2007.11.012
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A novel collagen-binding peptide promotes osteogenic differentiation via Ca2+/calmodulin-dependent protein kinase II/ERK/AP-1 signaling pathway in human bone marrow-derived mesenchymal stem cells

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Cited by 64 publications
(49 citation statements)
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“…differentiation: Cbfa1/Runx2 and AP-1 Cbfa1/Runx2 and AP-1 are important transcription factors involved in osteogenic differentiation of hMSCs (Bjerre et al 2008;Haasper et al 2008;Shin et al 2008). Runx2 is essential not only in the osteogenic differentiation of hMSCs but also in the differentiation of osteoblasts and chondroblasts (Fu et al 2007).…”
Section: Transcription Factors Related To Osteogenicmentioning
confidence: 97%
See 1 more Smart Citation
“…differentiation: Cbfa1/Runx2 and AP-1 Cbfa1/Runx2 and AP-1 are important transcription factors involved in osteogenic differentiation of hMSCs (Bjerre et al 2008;Haasper et al 2008;Shin et al 2008). Runx2 is essential not only in the osteogenic differentiation of hMSCs but also in the differentiation of osteoblasts and chondroblasts (Fu et al 2007).…”
Section: Transcription Factors Related To Osteogenicmentioning
confidence: 97%
“…The increasing of Ca 2+ leads to the activation of CaMKII, which subsequently phosphorylates ERK1/2 ( Fig. 1) (Shin et al 2008). Therefore, Ca 2+ signal can lead to the activation of ERK1/2 signaling pathway, which is critical for osteoblastic differentiation.…”
Section: No and Pge2mentioning
confidence: 99%
“…CaMKII is expressed most abundantly in neurons, and is involved in regulating many aspects of neuronal function, including neurotransmitter synthesis and release, modulation of ion channel activity, cellular transport, cellular morphology and neurite extension, long-term plasticity, learning, memory consolidation, and memory erasure following retrieval [2][3][4][5][6][7]. Non-neuronal CaMKII has been implicated in the regulation of other biological processes, such as fertilisation [8], osteogenic differentiation [9], and the maintenance of vascular tone [10]. Aside from its abundance in the brain, intense interest in CaMKII arose from its ability to act as autophosphorylatable molecular switch (reviewed in [11,12]).…”
Section: Introductionmentioning
confidence: 99%
“…35,36 The bioactive scaffolds have been well documented to coordinate with some cytokines or growth factors in determining differentiation fates. 37,38 In the present study, our hypothesis was that the MAPK cascade can serve as a mediator by transducing the signals from the scaffolds into the cells, thereby regulating DPSC differentiation. Our findings confirmed this hypothesis, as we showed that ERK1/2 and p38 phosphorylations were higher in DPSCs cultured on DDM and CBB than in those cultured on SIS, whereas ERK1/2 and p38 phosphorylations were higher in DPSCs cultured on SIS than in those cultured on PLGA and Co-CS-HA.…”
mentioning
confidence: 99%