Ca2+-dependent PKC activation mediates menthol-induced desensitization of transient receptor potential M8

@article{Abe2006Ca2dependentPA,
  title={Ca2+-dependent PKC activation mediates menthol-induced desensitization of transient receptor potential M8},
  author={Junji Abe and Hiroshi Hosokawa and Yosuke Sawada and Kiyoshi Matsumura and Shigeo Kobayashi},
  journal={Neuroscience Letters},
  year={2006},
  volume={397},
  pages={140-144}
}
In 1950, Hensel and Zotterman reported cooling-induced desensitization of cold receptors by extracellular discharge recordings of cold fibers. Since then, however, its intracellular mechanism has remained unresolved. We studied menthol-induced desensitization of cold/menthol receptors (TRPM8, transient receptor potential M8) expressed in HEK cells. TRPM8 desensitization depended on extracellular Ca2+ ions, indicating that Ca2+ influx-induced [Ca2+]i elevation caused the desensitization. We… 
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  • Chemistry, Medicine
    Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques
  • 2009
TLDR
The finding on agonist-induced desensitization of TRPV3 by some monoterpenoids displays a novel mechanism through which TRP channels could be functionally modulated.
Desensitization of cold- and menthol-sensitive rat dorsal root ganglion neurones by inflammatory mediators
TLDR
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Ethanol inhibits cold‐menthol receptor TRPM8 by modulating its interaction with membrane phosphatidylinositol 4,5‐bisphosphate
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The findings suggest that ethanol inhibits TRPM8 by weakening the PIP2–TRPM8 channel interaction; a similar mechanism may contribute to the ethanol‐mediated modulation of some other PIP 2‐sensitive TRP channels.
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References

SHOWING 1-10 OF 18 REFERENCES
Desensitization of canonical transient receptor potential channel 5 by protein kinase C.
  • M. Zhu, M. Chae, +6 authors K. Kim
  • Chemistry, Medicine
    American journal of physiology. Cell physiology
  • 2005
TLDR
It is concluded that the desensitization of TRPC5 occurs via PKC phosphorylation and it is suggested that threonine at residue 972 of mouse TR PC5 might be required for its phosphorylated by PKC.
Functional Control of Cold- and Menthol-Sensitive TRPM8 Ion Channels by Phosphatidylinositol 4,5-Bisphosphate
TLDR
It is reported that phosphatidylinositol 4,5-bisphosphate (PIP2) is an essential regulator of the channel function and implies that the membrane lipid may have dual actions as a bimodal switch to selectively control the heat- and cold-induced responses in nociceptors expressing both channels.
Regulation of Canonical Transient Receptor Potential (TRPC) Channel Function by Diacylglycerol and Protein Kinase C*
TLDR
The results reveal that each TRPC subtype is strongly inhibited by D AG-induced PKC activation, reflecting a likely universal feedback control on TRPCs, and that DAG-mediated PKC-independent activation of TRPC channels is highly subtype-specific.
PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels through the TRP domain
The subjective feeling of cold is mediated by the activation of TRPM8 channels in thermoreceptive neurons by cold or by cooling agents such as menthol. Here, we demonstrate a central role for
Direct Phosphorylation of Capsaicin Receptor VR1 by Protein Kinase Cε and Identification of Two Target Serine Residues*
TLDR
Direct phosphorylation of VR1 upon application of phorbol 12-myristate 13-acetate (PMA) was proven biochemically in cells expressing VR1 and would be promising targets for the development of substance modulating VR1 function, thereby reducing pain.
Ionic Basis of Cold Receptors Acting as Thermostats
TLDR
It is proposed that cold receptors at distal ends of cold fibers are thermostats to regulate skin T against cold, and it is concluded that the same cold receptors exist at nerve endings and generate afferent impulses for cold sensation and heat-gain behaviors in response to cold.
An introduction to TRP channels.
The aim of this review is to provide a basic framework for understanding the function of mammalian transient receptor potential (TRP) channels, particularly as they have been elucidated in
Identification of a cold receptor reveals a general role for TRP channels in thermosensation
TLDR
These findings, together with the previous identification of the heat-sensitive channels VR1 and VRL-1, demonstrate that TRP channels detect temperatures over a wide range and are the principal sensors of thermal stimuli in the mammalian peripheral nervous system.
A TRP Channel that Senses Cold Stimuli and Menthol
TLDR
This work describes the cloning and characterization of TRPM8, a distant relative of VR1 that is specifically expressed in a subset of pain- and temperature-sensing neurons and implicates an expanded role for this family of ion channels in somatic sensory detection.
Phorbol myristate acetate stimulates formation of phosphatidyl inositol 4-phosphate and phosphatidyl inositol 4,5-bisphosphate in human platelets.
TLDR
The tumor-promoting phorbol ester PMA may directly affect inositol lipid kinases and/or phosphatases, or that PMA stimulation of protein kinase C provides feedback regulation of the enzymes that determine the levels of polyphosphoinositides involved in transmembrane stimulus-response coupling.
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1
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