The pore properties of human nociceptor channel TRPA1 evaluated in single channel recordings.

@article{Bobkov2011ThePP,
  title={The pore properties of human nociceptor channel TRPA1 evaluated in single channel recordings.},
  author={Y. Bobkov and E. Corey and B. Ache},
  journal={Biochimica et biophysica acta},
  year={2011},
  volume={1808 4},
  pages={
          1120-8
        }
}
TRPA channels detect stimuli of different sensory modalities, including a broad spectrum of chemosensory stimuli, noxious stimuli associated with tissue damage and inflammation, mechanical stimuli, and thermal stimuli. Despite a growing understanding of potential modulators, agonists, and antagonists for these channels, the exact mechanisms of channel regulation and activation remain mostly unknown or controversial and widely debated. Relatively little is also known about the basic biophysical… Expand
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References

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Pore dilation occurs in TRPA1 but not in TRPM8 channels
TLDR
It is shown that TRPV1 activation by reactive or non-reactive agonists induces Yo-Pro uptake, which can be blocked by TRPA1 antagonists, and pore dilation occurs in TRP1, but not in TRPM8 channels. Expand
NPPB structure-specifically activates TRPA1 channels.
TLDR
NPPB, a classic Cl(-) channel blocker, potently activated human TRPA1 channels overexpressed in mammalian HEK-293 cells, and it was demonstrated that NPPB activation was tightly associated with chemical structure. Expand
Agonist-induced changes in Ca(2+) permeation through the nociceptor cation channel TRPA1.
TLDR
The pore of TRPA1 is dynamic and supports a surprisingly large Ca(2+) influx, suggesting that binding of Ca( 2+) in the pore hinders monovalent cation permeation. Expand
TRPV1 shows dynamic ionic selectivity during agonist stimulation
TLDR
The qualitative signaling properties of TRpV1 are dynamically modulated during channel activation, a process that probably shapes TRPV1 participation in pain, cytotoxicity and neurotransmitter release. Expand
Intracellular alkalization causes pain sensation through activation of TRPA1 in mice.
TLDR
It is shown that alkaline pH activated transient receptor potential cation channel, subfamily A, member 1 (TRPA1) and that activation of this ion channel was involved in nociception and may provide a molecular explanation for some of the human alkalin pH-related sensory disorders. Expand
Dynamic changes in the TRPA1 selectivity filter lead to progressive but reversible pore dilation.
TLDR
It is found that agonist stimulation of TRPA1, along with other members of the TRP family, can induce the appearance of a large pore permeable to large organic cations such as Yo-Pro and N-methyl-d-glucamine, in an agonist and divalent cation-dependent manner. Expand
The Nociceptor Ion Channel TRPA1 Is Potentiated and Inactivated by Permeating Calcium Ions*
TLDR
Evidence is provided that the effect of extracellular Ca2+ on these processes is indirect and can be entirely attributed to entry through TRPA1 and subsequent elevation of intracellular calcium, and that potentiation and inactivation are independent processes. Expand
Nicotine activates the chemosensory cation channel TRPA1
TLDR
The identification of TRPA1 as a nicotine target suggests that existing models of nicotine-induced irritation should be revised and may facilitate the development of smoking cessation therapies with less adverse effects. Expand
Noxious Cold Ion Channel TRPA1 Is Activated by Pungent Compounds and Bradykinin
TLDR
It is demonstrated that TRPA1 activation elicits a painful sensation and provide a potential molecular model for why noxious cold can paradoxically be perceived as burning pain. Expand
ANKTM1, a TRP-like Channel Expressed in Nociceptive Neurons, Is Activated by Cold Temperatures
TLDR
The characterization of ANKTM1 is described, a cold-activated channel with a lower activation temperature compared to the cold and menthol receptor, TRPM8, which is found in a subset of nociceptive sensory neurons where it is coexpressed with TRPV1/VR1 (the capsaicin/heat receptor) but not TRPM 8. Expand
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