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      A regulatory role of Piezo1 in apoptosis of periodontal tissue and periodontal ligament fibroblasts during orthodontic tooth movement

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          Abstract

          Investigation on the effect of Piezo1 on periodontal tissue and periodontal ligament fibroblasts (PDLFs) under mechanical stress and the underlying mechanism. The orthodontic tooth movement rat model was established via an orthodontic spiral tension spring. PDLFs were cultured and subjected to 2.0 g/cm 2 static compressive loading. Blocked the Piezo1 via Piezo1 inhibitor, GsMTx4. TUNEL staining and flow cytometry determined the apoptosis rate of periodontal tissue and PDLFs in rats. Expression of Piezo1, p‐p38 and ERK1/2 was analysed by immunofluorescence assay and western blotting. Piezo1 inhibitor GsMTx4 relieved the increased expression of Piezo1, ERK1/2 and p‐p38, and alleviated apoptosis in periodontal tissue and PDLFs under compressive loading. Piezo1 inhibition can alleviate force‐induced apoptosis and damage in rats' periodontal tissue and PDLFs, and regulate the p38/ERK1/2 signalling pathway.

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          Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels.

          B Coste, J Mathur, M. Schmidt … (2010)
          Mechanical stimuli drive many physiological processes, including touch and pain sensation, hearing, and blood pressure regulation. Mechanically activated (MA) cation channel activities have been recorded in many cells, but the responsible molecules have not been identified. We characterized a rapidly adapting MA current in a mouse neuroblastoma cell line. Expression profiling and RNA interference knockdown of candidate genes identified Piezo1 (Fam38A) to be required for MA currents in these cells. Piezo1 and related Piezo2 (Fam38B) are vertebrate multipass transmembrane proteins with homologs in invertebrates, plants, and protozoa. Overexpression of mouse Piezo1 or Piezo2 induced two kinetically distinct MA currents. Piezos are expressed in several tissues, and knockdown of Piezo2 in dorsal root ganglia neurons specifically reduced rapidly adapting MA currents. We propose that Piezos are components of MA cation channels.
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            Mechanical stretch triggers rapid epithelial cell division through Piezo1

            SA Gudipaty, J Lindblom, PD Loftus … (2017)
            Despite acting as a barrier for the organs they encase, epithelial cells turnover at some of the fastest rates in the body. Yet, epithelial cell division must be tightly linked to cell death to preserve barrier function and prevent tumour formation. How do the number of dying cells match those dividing to maintain constant numbers? We previously found that when epithelial cells become too crowded, they activate the stretch-activated channel Piezo1 to trigger extrusion of cells that later die 1 . Conversely, what controls epithelial cell division to balance cell death at steady state? Here, we find that cell division occurs in regions of low cell density, where epithelial cells are stretched. By experimentally stretching epithelia, we find that mechanical stretch itself rapidly stimulates cell division through activation of the same Piezo1 channel. To do so, stretch triggers cells paused in early G2 to activate calcium-dependent ERK1/2 phosphorylation that activates cyclin B transcription necessary to drive cells into mitosis. Although both epithelial cell division and cell extrusion require Piezo1 at steady state, the type of mechanical force controls the outcome: stretch induces cell division whereas crowding induces extrusion. How Piezo1-dependent calcium transients activate two opposing processes may depend on where and how Piezo1 is activated since it accumulates in different subcellular sites with increasing cell density. In sparse epithelial regions where cells divide, Piezo1 localizes to the plasma membrane and cytoplasm whereas in dense regions where cells extrude, it forms large cytoplasmic aggregates. Because Piezo1 senses both mechanical crowding and stretch, it may act as a homeostatic sensor to control epithelial cell numbers, triggering extrusion/apoptosis in crowded regions and cell division in sparse regions.
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              The mechanosensitive ion channel Piezo1 is inhibited by the peptide GsMTx4.

              Chilman Bae, P Gottlieb, Frederick Sachs (2011)
              Cells can respond to mechanical stress by gating mechanosensitive ion channels (MSCs). The cloning of Piezo1, a eukaryotic cation selective MSC, defines a new system for studying mechanical transduction at the cellular level. Because Piezo1 has electrophysiological properties similar to those of endogenous cationic MSCs that are selectively inhibited by the peptide GsMTx4, we tested whether the peptide targets Piezo1 activity. Extracellular GsMTx4 at micromolar concentrations reversibly inhibited ∼80% of the mechanically induced current of outside-out patches from transfected HEK293 cells. The inhibition was voltage insensitive, and as seen with endogenous MSCs, the mirror image d enantiomer inhibited like the l. The rate constants for binding and unbinding based on Piezo1 current kinetics provided association and dissociation rates of 7.0 × 10(5) M(-1) s(-1) and 0.11 s(-1), respectively, and a K(D) of ∼155 nM, similar to values previously reported for endogenous MSCs. Consistent with predicted gating modifier behavior, GsMTx4 produced an ∼30 mmHg rightward shift in the pressure-gating curve and was active on closed channels. In contrast, streptomycin, a nonspecific inhibitor of cationic MSCs, showed the use-dependent inhibition characteristic of open channel block. The peptide did not block currents of the mechanical channel TREK-1 on outside-out patches. Whole-cell Piezo1 currents were also reversibly inhibited by GsMTx4, and although the off rate was nearly identical to that of outside-out patches, differences were observed for the on rate. The ability of GsMTx4 to target the mechanosensitivity of Piezo1 supports the use of this channel in high-throughput screens for pharmacological agents and diagnostic assays. © 2011 American Chemical Society
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                Author and article information

                Contributors
                Journal
                Title: Australian Endodontic Journal
                Abbreviated Title: Aust Endodontic J
                Publisher: Wiley
                ISSN (Print): 1329-1947
                ISSN (Electronic): 1747-4477
                Publication date Created: September 2023
                Publication date (Electronic): December 02 2022
                Publication date (Print): September 2023
                Volume: 49
                Issue: S1
                Pages: 228-237
                Affiliations
                [1 ] Department of Stomatology Taizhou Central Hospital (Taizhou University Hospital) Taizhou China
                Article
                DOI: 10.1111/aej.12721
                PubMed ID: 36461169
                SO-VID: 048164e6-20c4-49c3-906d-ab70a7e19def
                Copyright © © 2023
                License:

                http://onlinelibrary.wiley.com/termsAndConditions#vor

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