Abstract
Mechanosensing and mechanotransduction are vital processes in mechanobiology and play critical roles in regulating cellular behavior and fate. There is increasing evidence that purinergic P2 receptors, members of the purinergic family, play a crucial role in cellular mechanotransduction. Thus, information on the specific mechanism of P2 receptor-mediated mechanotransduction would be valuable. In this review, we focus on purinergic P2 receptor signaling pathways and describe in detail the interaction of P2 receptors with other mechanosensitive molecules, including transient receptor potential channels, integrins, caveolae-associated proteins and hemichannels. In addition, we review the activation of purinergic P2 receptors and the role of various P2 receptors in the regulation of various pathophysiological processes induced by mechanical stimuli.
Highlights
Mechanotransduction refers to the conversion by cells of external mechanical signals into internal biochemical signals (Maurer and Lammerding, 2019)
Multiple mechanosensitive molecules, including transient receptor potential (TRP) channels, integrins, caveolaeassociated proteins, hemichannels and piezo1, have been identified that are involved in P2 receptors (P2Rs)-mediated mechanotransduction
Under the action of fluid, endogenously released Adenosine triphosphate (ATP) affected the opening of the transient receptor potential vanilloid 4 (TRPV4) and transient receptor potential canonical 1 (TRPC1) by activating P2X4R, thereby regulating the intracellular Ca2+ concentration of endothelial cells (Li et al, 2015)
Summary
Mechanotransduction refers to the conversion by cells of external mechanical signals into internal biochemical signals (Maurer and Lammerding, 2019). The response of cells to mechanical stimuli involves activation of P2Rs and subsequent initiation of intracellular downstream signaling. Multiple mechanosensitive molecules, including transient receptor potential (TRP) channels, integrins, caveolaeassociated proteins, hemichannels and piezo1, have been identified that are involved in P2Rs-mediated mechanotransduction.
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