Proteomics based detection of differentially expressed proteins in human osteoblasts subjected to mechanical stress.

Proteomics based detection of differentially expressed proteins in human osteoblasts subjected to mechanical stress.
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DOI：
10.1139/bcb-2012-0021
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发表时间：
2013-04
期刊：
Biochemistry and cell biology = Biochimie et biologie cellulaire
影响因子：
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通讯作者：
Li Fei-Fei-Li-Fei-Fei-48004138;Fu-lin Chen;Huan Wang;Shi‐bin Yu;Ji-hong Cui;Yin Ding;Xue Feng
Li Fei-Fei-Li-Fei-Fei-48004138;Fu-lin Chen;Huan Wang;Shi‐bin Yu;Ji-hong Cui;Yin Ding;Xue Feng
中科院分区：
其他
文献类型：
--
作者：
Li Fei-Fei-Li-Fei-Fei-48004138;Fu-lin Chen;Huan Wang;Shi‐bin Yu;Ji-hong Cui;Yin Ding;Xue Feng

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Mechanical stress is essential for bone development. Mechanical stimuli are transduced to biochemical signals that regulate proliferation, differentiation, and cytoskeletal reorganization in osteoblasts. In this study, we used proteomics to evaluate differences in the protein expression profiles of untreated Saos-2 osteoblast cells and Saos-2 cells subjected to mechanical stress loading. Using 2-D electrophoresis, MALDI-TOF mass spectroscopy, and bioinformatics, we identified a total of 26 proteins differentially expressed in stress loaded cells compared with control cells. Stress loaded Saos-2 cells exhibited significant upregulation of 17 proteins and significant downregulation of 9 proteins compared with control cells. Proteins that were most significantly upregulated in mechanically loaded cells included those regulating osteogenesis, energy metabolism, and the stress response, such as eukaryotic initiation factor 2 (12-fold), mitochondrial ATP synthase (8-fold), and peptidylprolyl isomerase A (cyclophilin A)-like 3 (6.5-fold). Among the proteins that were significantly downregulated were those involved in specific signaling pathways and cell proliferation, such as protein phosphatase regulatory (inhibitor) subunit 12B (13.8-fold), l-lactate dehydrogenase B (9.4-fold), Chain B proteasome activator Reg (Alpha) PA28 (7.7-fold), and ubiquitin carboxyl-terminal esterase L1 (6.9-fold). Our results provide a platform to understand the molecular mechanisms underlying mechanotransduction.