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Src Kinase Controls Signaling Pathways In Sensory Neuron Triggered By Low-Power Infrared Radiation

DOI:10.1139/cjpp-2018-0602 期刊:Canadian Journal of Physiology and Pharmacology 出版年份:2019 更新时间:2025-11-21 11:24:58
摘要: Low-power (non-thermal) infrared (IR) radiation with the wavelength of 10.6 μm activates the Na,K-ATPase transducer function in sensory neurons, which is manifested in decrease of NaV1.8 channel voltage sensitivity at the cellular membrane level and in inhibition of growth of chick embryo dorsal root ganglia neurites at the tissue level. It is shown that the effect of low-power IR radiation is totally blocked by a specific Src kinase inhibitor PP2. Upon irradiation on the background of PP2, the effective charge of NaV1.8 channel activation gating system does not differ from its control value in patch-clamp experiments, and the area index of sensory ganglia neurites growth remains unchanged as compared to the control in organotypic tissue culture. The data obtained demonstrate that Src kinase is involved in intracellular signaling pathways triggered by CO2 laser low-power IR radiation by the transducer-activated mechanism. This is the first indication that in primary sensory neuron the signals of low-power IR radiation are sensed, amplified and transduced by the Na,K-ATPase/Src complex and not by G proteins.
作者: Vera B. Plakhova,Valentina A. Penniyaynen,Igor L. Yachnev,Ilya V. Rogachevskii,Svetlana A. Podzorova,Boris V. Krylov
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Investigating the role of Src kinase in intracellular signaling pathways triggered by low-power infrared radiation in sensory neurons.

Src kinase is involved in intracellular signaling pathways triggered by low-power IR radiation in sensory neurons, acting through the Na,K-ATPase/Src complex to modulate NaV1.8 channel voltage sensitivity and inhibit neurite growth. This provides a novel mechanism for signal transduction distinct from G proteins, with potential applications in pain relief.

The study is limited to sensory neurons and may not generalize to other cell types. The patch-clamp method has inherent errors such as series resistance and run-down effect. The specific molecular interactions within the Na,K-ATPase/Src complex require further elucidation.

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