journal article·2022-09-14

Piezo1 Response to Shear Stress Is Controlled by the Components of the Extracellular Matrix

Austin Lai, Peter Thurgood, Charles D. Cox, Chanly Chheang, Karlheinz Peter, Anthony Jaworowski, Khashayar Khoshmanesh, Sara Baratchi

ACS Applied Materials & Interfaces· Volume 14· Issue 36
Publisher page

Abstract

Piezo1 is a recently discovered Ca2+ permeable ion channel that has emerged as an integral sensor of hemodynamic forces within the cardiovascular system, contributing to vascular development and blood pressure regulation. However, how the composition of the extracellular matrix (ECM) affects the mechanosensitivity of Piezo1 in response to hemodynamic forces remains poorly understood. Using a combination of microfluidics and calcium imaging techniques, we probe the shear stress sensitivity of single HEK293T cells engineered to stably express Piezo1 in the presence of different ECM proteins. Our experiments show that Piezo1 sensitivity to shear stress is not dependent on the presence of ECM proteins. However, different ECM proteins regulate the sensitivity of Piezo1 depending on the shear stress level. Under high shear stress, fibronectin sensitizes Piezo1 response to shear, while under low shear stress, Piezo1 mechanosensitivity is improved in the presence of collagen types I and IV and laminin. Moreover, we report that α5β1 and αvβ3 integrins are involved in Piezo1 sensitivity at high shear, while αvβ3 and αvβ5 integrins are involved in regulating the Piezo1 response at low shear stress. These results demonstrate that the ECM/integrin interactions influence Piezo1 mechanosensitivity and could represent a mechanism whereby extracellular forces are transmitted to Piezo1 channels, providing new insights into the mechanism by which Piezo1 senses shear stress.
Source: europepmc · Quality: candidate unverified · Source record ↗

Research context

OpenAlex topics: Erythrocyte Function and Pathophysiology · Blood properties and coagulation · Ion channel regulation and function

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

School of Health & Biomedical Sciences, RMIT University, Bundoora, Victoria 3082, Australia

School of Engineering, RMIT University, Melbourne, Victoria 3000, Australia

Molecular Cardiology and Biophysics Division, Victor Chang Cardiac Research Institute, Sydney, New South Wales 2010, Australia

Baker Heart and Diabetes Institute, Melbourne, Victoria 3004, Australia

Department of Cardiometabolic Health, The University of Melbourne, Parkville, Victoria 3010, Australia

Funding

Department of Health, Australian Government · Department of Education and Training

References (52)

Show source-provided references
1. 10.3389/fphys.2018.0082410.3389/fphys.2018.00824 ↗
2. 10.1038/nrm259610.1038/nrm2596 ↗
3. 10.1016/j.molmed.2017.07.00710.1016/j.molmed.2017.07.007 ↗
4. 10.1038/nrm.2017.9210.1038/nrm.2017.92 ↗
5. 10.1146/annurev-biochem-081720-02324410.1146/annurev-biochem-081720-023244 ↗
6. 10.1097/j.pain.000000000000235610.1097/j.pain.0000000000002356 ↗
7. 10.1038/nature1325110.1038/nature13251 ↗
8. 10.1111/brv.1281410.1111/brv.12814 ↗
9. 10.1161/circulationaha.120.04553610.1161/circulationaha.120.045536 ↗
10. 10.1038/s41551-021-00716-x10.1038/s41551-021-00716-x ↗
11. 10.1016/bs.ctm.2016.11.00110.1016/bs.ctm.2016.11.001 ↗
12. 10.1016/j.celrep.2016.10.03310.1016/j.celrep.2016.10.033 ↗
13. 10.1038/ncomms1036610.1038/ncomms10366 ↗
14. 10.1126/science.119327010.1126/science.1193270 ↗
15. 10.1113/jp27440410.1113/jp274404 ↗
16. 10.1038/nature2545310.1038/nature25453 ↗
17. 10.1038/s41467-017-00429-310.1038/s41467-017-00429-3 ↗
18. 10.1126/science.aau632410.1126/science.aau6324 ↗
19. 10.1038/nature1370110.1038/nature13701 ↗
20. 10.1016/j.biocel.2003.12.00310.1016/j.biocel.2003.12.003 ↗
21. 10.1002/jemt.1023810.1002/jemt.10238 ↗
22. 10.1038/nrm259510.1038/nrm2595 ↗
23. 10.1073/pnas.191124311710.1073/pnas.1911243117 ↗
24. 10.1016/j.bbamem.2013.07.01510.1016/j.bbamem.2013.07.015 ↗
25. 10.3389/fnmol.2017.0009610.3389/fnmol.2017.00096 ↗
26. 10.7554/eLife.2107410.7554/eLife.21074 ↗
27. 10.1016/j.neuron.2018.09.04610.1016/j.neuron.2018.09.046 ↗
28. 10.1021/acs.nanolett.7b0017710.1021/acs.nanolett.7b00177 ↗
29. 10.1039/d1lc00927c10.1039/d1lc00927c ↗
30. 10.1007/s00018-015-2018-810.1007/s00018-015-2018-8 ↗
31. 10.7554/eLife.1061610.7554/eLife.10616 ↗
32. 10.1038/nrm115510.1038/nrm1155 ↗
33. 10.1016/s0143-4160(96)90084-610.1016/s0143-4160(96)90084-6 ↗
34. 10.1002/jcp.3005610.1002/jcp.30056 ↗
35. 10.1038/nrm389610.1038/nrm3896 ↗
36. 10.1002/jcp.104163012110.1002/jcp.1041630121 ↗
37. 10.1111/j.1432-1033.1993.tb18017.x10.1111/j.1432-1033.1993.tb18017.x ↗
38. 10.1074/jbc.m10405820010.1074/jbc.m104058200 ↗
39. 10.1074/jbc.m31190120010.1074/jbc.m311901200 ↗
40. 10.3389/fphys.2018.0052410.3389/fphys.2018.00524 ↗
41. 10.1161/01.res.0000191547.64391.e310.1161/01.res.0000191547.64391.e3 ↗
42. 10.1242/dev.0103710.1242/dev.01037 ↗
43. 10.1111/j.1600-0714.1981.tb01242.x10.1111/j.1600-0714.1981.tb01242.x ↗
44. 10.1152/ajpcell.00171.201510.1152/ajpcell.00171.2015 ↗
45. 10.1016/j.ajpath.2015.05.01310.1016/j.ajpath.2015.05.013 ↗
46. 10.1073/pnas.98.3.104210.1073/pnas.98.3.1042 ↗
47. 10.1091/mbc.7.7.102510.1091/mbc.7.7.1025 ↗
48. 10.7554/eLife.5411310.7554/eLife.54113 ↗
49. 10.1242/jcs.115.17.341510.1242/jcs.115.17.3415 ↗
50. 10.1038/nrm287110.1038/nrm2871 ↗
51. 10.1084/jem.2018048310.1084/jem.20180483 ↗
52. 10.1371/journal.pone.004034610.1371/journal.pone.0040346 ↗