Protein phosphatase 2A plays an important role in migration of bone marrow stroma cells

Administration of bone marrow stroma cells (BMSCs) has the potential to ameliorate degenerative disorders and to repair injured sites. The homing of transplanted BMSCs to damaged tissues is a critical property of engraftment. Therefore, it is important to understand signal molecules controlling migr...

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Published in:Molecular and cellular biochemistry 2016-01, Vol.412 (1-2), p.173-180
Main Authors: Chen, Weiqian, Wang, Shizhen, Xia, Jun, Huang, Zan, Tu, Xin, Shen, Zhenya
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Biomedical and Life Sciences
Bone marrow
Cardiology
Cell adhesion & migration
Cell Movement - drug effects
Cell Movement - physiology
Chemokine CXCL12 - physiology
Enzymes
Gene Knockdown Techniques
Life Sciences
Medical Biochemistry
Mesenchymal Stromal Cells - cytology
Okadaic Acid - pharmacology
Oncology
Phosphatases
Protein expression
Protein Phosphatase 2 - genetics
Protein Phosphatase 2 - physiology
Rats
Rats, Sprague-Dawley
Ribonucleic acid
RNA
Stem cells
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Summary:Administration of bone marrow stroma cells (BMSCs) has the potential to ameliorate degenerative disorders and to repair injured sites. The homing of transplanted BMSCs to damaged tissues is a critical property of engraftment. Therefore, it is important to understand signal molecules controlling migration of BMSCs. Here, we demonstrate that serine-threonine protein phosphatase 2A (PP2A) is responsive to migration of BMSCs. Pharmacological Inhibition of PP2A, using okadaic acid (OA), leads to attenuated cell migration in rat primary BMSCs both in the absence or presence of stromal cell-derived factor-1 (SDF-1). Consistent with the above findings, knockdown of the main catalytic subunit PP2Acα using small interfering RNA also attenuates chemotaxis of BMSCs. On the other hand, cell viability of BMSCs remains unchanged with OA treatment or knockdown of PP2Acα subunit. Moreover, we observed an upregulation of PP2A-B55β in transcription level after SDF-1 treatment, indicating their potential role as the functioning regulatory subunit of PP2A phosphatase in BMSCs migration model. Collectively, these data provide first insight into the modulation of BMSCs migration by PP2A phosphatase activity and lay a foundation for exploring PP2A signaling as a modulating target for BMSCs transplantation.
ISSN:0300-8177
1573-4919
DOI:10.1007/s11010-015-2624-7