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Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

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EHSP70 promotes osteogenesis of hMSCs through activating ERK signaling pathway

ABSTRACT: Heat shock proteins are highly conserved proteins that, when produced intracellularly, protect stress exposed cells. It has been suggested that extracellular Hsp70 has both protective and deleterious effects. Our study showed eHSP70 increased the ALP activity, promoted mineralization and up-regulated osteogenesis-related markers. We used microarrays to determine the differentially expressed genes and identify revelant pathways through pathway enrichment analysis. hMSCs were selected for RNA extraction and hybridization on Affymetrix microarrays after 3-day culture. The experimental group was treated with HSP70 (200ng/ml) during osteogenic differentiation and control group without it.

ORGANISM(S): Homo sapiens

SUBMITTER: Erman Chen

PROVIDER: E-GEOD-71080 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Extracellular heat shock protein 70 promotes osteogenesis of human mesenchymal stem cells through activation of the ERK signaling pathway.

Chen Erman E Xue Deting D Zhang Wei W Lin Feng F Pan Zhijun Z

FEBS letters 20151119 24 Pt B

Heat shock proteins have protective effects when cells are exposed to stress. However, the relationship between extracellular heat shock protein 70 (eHSP70) and osteogenesis of hMSCs has not been reported. The results of this study showed that HSP70 (200 ng/ml) increases alkaline phosphatase activity and promotes hMSC mineralization. Under osteogenic induction conditions, HSP70 significantly upregulated the expression of osteo-specific genes, such as the runt family transcription factor Runx2 an ...[more]

PMID: 26608032

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