| First Author | Allen A | Year | 2022 |
| Journal | Int J Mol Sci | Volume | 23 |
| Issue | 9 | PubMed ID | 35563101 |
| Mgi Jnum | J:332309 | Mgi Id | MGI:7280056 |
| Doi | 10.3390/ijms23094710 | Citation | Allen A, et al. (2022) Mechanical Load and Piezo1 Channel Regulated Myosin II Activity in Mouse Lenses. Int J Mol Sci 23(9) |
| abstractText | The cytoarchitecture and tensile characteristics of ocular lenses play a crucial role in maintaining their transparency and deformability, respectively, which are properties required for the light focusing function of ocular lens. Calcium-dependent myosin-II-regulated contractile characteristics and mechanosensitive ion channel activities are presumed to influence lens shape change and clarity. Here, we investigated the effects of load-induced force and the activity of Piezo channels on mouse lens myosin II activity. Expression of the Piezo1 channel was evident in the mouse lens based on immunoblot and immufluorescence analyses and with the use of a Piezo1(-tdT) transgenic mouse model. Under ex vivo conditions, change in lens shape induced by the load decreased myosin light chain (MLC) phosphorylation. While the activation of Piezo1 by Yoda1 for one hour led to an increase in the levels of phosphorylated MLC, Yoda1 treatment for an extended period led to opacification in association with increased calpain activity and degradation of membrane proteins in ex vivo mouse lenses. In contrast, inhibition of Piezo1 by GsMTx4 decreased MLC phosphorylation but did not affect the lens tensile properties. This exploratory study reveals a role for the mechanical load and Piezo1 channel activity in the regulation of myosin II activity in lens, which could be relevant to lens shape change during accommodation. |
