Activation of TRPM8 channel inhibits contraction of the isolated human ureter

2021 ◽  
Author(s):  
Jiaxin Liu ◽  
Lei Liu ◽  
Mengmeng Zhao ◽  
Ning Ding ◽  
Nan Ge ◽  
...  
Keyword(s):  
Trpm8 Channel ◽  
Human Ureter

Agonist of TRPM8 channel, menthol, facilitates the initiation of thermoregulatory responses to external cooling

2010 ◽  
Vol 35 (8) ◽  
pp. 428-434 ◽  
Author(s):  
T.V. Kozyreva ◽  
V.P. Kozaruk ◽  
E.Ya. Tkachenko ◽  
G.M. Khramova
Keyword(s):  
Trpm8 Channel ◽  
Thermoregulatory Responses ◽  
External Cooling

scholarly journals Regulation of Activity of Transient Receptor Potential Melastatin 8 (TRPM8) Channel by Its Short Isoforms

2011 ◽  
Vol 287 (5) ◽  
pp. 2948-2962 ◽  
Author(s):  
Gabriel Bidaux ◽  
Benjamin Beck ◽  
Alexander Zholos ◽  
Dmitri Gordienko ◽  
Loic Lemonnier ◽  
...  
Keyword(s):  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Trpm8 Channel ◽  
Short Isoforms ◽  
Transient Receptor Potential Melastatin ◽  
Regulation Of Activity ◽  
Transient Receptor

scholarly journals TRPM8 channel as a novel molecular target in androgen-regulated prostate cancer cells

Oncotarget ◽  
2015 ◽  
Vol 6 (19) ◽  
pp. 17221-17236 ◽  
Author(s):  
Swapna Asuthkar ◽  
Kiran Kumar Velpula ◽  
Pia A. Elustondo ◽  
Lusine Demirkhanyan ◽  
Eleonora Zakharian
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Molecular Target ◽  
Prostate Cancer Cells ◽  
Trpm8 Channel

scholarly journals Activation of the cold-sensing TRPM8 channel triggers UCP1-dependent thermogenesis and prevents obesity

2012 ◽  
Vol 4 (2) ◽  
pp. 88-96 ◽  
Author(s):  
Shuangtao Ma ◽  
Hao Yu ◽  
Zhigang Zhao ◽  
Zhidan Luo ◽  
Jing Chen ◽  
...  
Keyword(s):  
Trpm8 Channel ◽  
Cold Sensing

Evidence for the involvement of peripheral cold-sensitive TRPM8 channels in human cutaneous hygrosensation

2020 ◽  
Vol 318 (3) ◽  
pp. R579-R589 ◽  
Author(s):  
Oliver Typolt ◽  
Davide Filingeri
Keyword(s):  
Human Skin ◽  
Chemical Activation ◽  
The Body ◽  
Cold Sensitivity ◽  
Trpm8 Channel ◽  
Body Regions ◽  
Skin Cooling ◽  
Cold Sensitive ◽  
Skin Wetness

In contrast to other species, humans are believed to lack hygroreceptors for sensing skin wetness. Yet, the molecular basis of human hygrosensation is currently unknown, and it remains unclear whether we possess a receptor-mediated sensing mechanism for skin wetness. The aim of this study was to assess the role of the cutaneous cold-sensitive transient receptor potential melastatin-8 (TRPM8) channel as a molecular mediator of human hygrosensation. To this end, we exploited both the thermal and chemical activation of TRPM8-expressing cutaneous Aδ cold thermoreceptors, and we assessed wetness sensing in healthy young men in response to 1) dry skin cooling in the TRPM8 range of thermosensitivity and 2) application of the TRPM8 agonist menthol. Our results indicate that 1) independently of contact with moisture, a cold-dry stimulus in the TRPM8 range of activation induced wetness perceptions across 12 different body regions and those wetness perceptions varied across the body following regional differences in cold sensitivity; and 2) independently of skin cooling, menthol-induced stimulation of TRPM8 triggered wetness perceptions that were greater than those induced by physical dry cooling and by contact with an aqueous cream containing actual moisture. For the first time, we show that the cutaneous cold-sensing TRPM8 channel plays the dual role of cold and wetness sensor in human skin and that this ion channel is a peripheral mediator of human skin wetness perception.

scholarly journals Structural basis of cooling agent and lipid sensing by the cold-activated TRPM8 channel

Science ◽  
2019 ◽  
Vol 363 (6430) ◽  
pp. eaav9334 ◽  
Author(s):  
Ying Yin ◽  
Son C. Le ◽  
Allen L. Hsu ◽  
Mario J. Borgnia ◽  
Huanghe Yang ◽  
...  
Keyword(s):  
Transient Receptor Potential ◽  
Structural Information ◽  
Receptor Potential ◽  
Membrane Lipid ◽  
Structural Basis ◽  
Trpm8 Channel ◽  
Allosteric Coupling ◽  
Transient Receptor Potential Melastatin ◽  
Lipid Sensing ◽  
Transient Receptor

Transient receptor potential melastatin member 8 (TRPM8) is a calcium ion (Ca2+)–permeable cation channel that serves as the primary cold and menthol sensor in humans. Activation of TRPM8 by cooling compounds relies on allosteric actions of agonist and membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2), but lack of structural information has thus far precluded a mechanistic understanding of ligand and lipid sensing by TRPM8. Using cryo–electron microscopy, we determined the structures of TRPM8 in complex with the synthetic cooling compound icilin, PIP2, and Ca2+, as well as in complex with the menthol analog WS-12 and PIP2. Our structures reveal the binding sites for cooling agonists and PIP2in TRPM8. Notably, PIP2binds to TRPM8 in two different modes, which illustrate the mechanism of allosteric coupling between PIP2and agonists. This study provides a platform for understanding the molecular mechanism of TRPM8 activation by cooling agents.

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