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Effect of angiotensin II and angiotensin‐(1–7) on proliferation of stem cells from human dental apical papilla
The effects of the renin–angiotensin system (RAS) on stem cells isolated from human dental apical papilla (SCAPs) are completely unknown. Therefore, the aim of this study was to identify RAS components expressed in SCAPs and the effects of angiotensin (Ang) II and Ang‐(1–7) on cell proliferation. SC...
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Published in: | Journal of cellular physiology 2021-01, Vol.236 (1), p.366-378 |
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Main Authors: | , , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | The effects of the renin–angiotensin system (RAS) on stem cells isolated from human dental apical papilla (SCAPs) are completely unknown. Therefore, the aim of this study was to identify RAS components expressed in SCAPs and the effects of angiotensin (Ang) II and Ang‐(1–7) on cell proliferation. SCAPs were collected from third molar teeth of adolescents and maintained in cell culture. Messenger RNA expression and protein levels of angiotensin‐converting enzyme (ACE), ACE2, and Mas, Ang II type I (AT1) and type II (AT2) receptors were detected in SCAPs. Treatment with either Ang II or Ang‐(1–7) increased the proliferation of SCAPs. These effects were inhibited by PD123319, an AT2 antagonist. While Ang II augmented mTOR phosphorylation, Ang‐(1–7) induced ERK1/2 phosphorylation. In conclusion, SCAPs produce the main RAS components and both Ang II and Ang‐(1–7) treatments induced cell proliferation mediated by AT2 activation through different intracellular mechanisms.
Effects of angiotensin(Ang) II and Ang‐(1–7) on the stem cells isolated from human dental apical papilla (SCAPs). SCAPs express the main renin‐angiotensin system components, and both Ang II and Ang‐(1–7) induced cell proliferation mediated by AT2 receptor activation through different intracellular mechanisms. While Ang II induced mTOR phosphorylation, Ang‐(1–7) decreased phosphorylation of AKT and increased phospho‐ERK1/2. |
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ISSN: | 0021-9541 1097-4652 |
DOI: | 10.1002/jcp.29862 |