• Nanion Technologies: Smart Tools for Ion Channel Research

    Nanion Technologies: Smart Tools for Ion Channel Research

  • CardioExcyte 96 SOL: Pacing Cardiomyocytes with Light

    CardioExcyte 96 SOL: Pacing Cardiomyocytes with Light

  • SURFE²R 96SE: Label-free HTS Transporter Screening

    SURFE²R 96SE: Label-free HTS Transporter Screening

  • Bilayer recordings: Orbit product family

    Bilayer recordings: Orbit product family

Our Product Portfolio

SyncroPatch 384i

SyncroPatch 384i

Patchliner

Patchliner

Port-a-Patch

Port-a-Patch

Port-a-Patch mini

Port-a-Patch mini

CardioExcyte 96

CardioExcyte 96

FLEXcyte 96

FLEXcyte 96

SURFE²R 96SE

SURFE²R 96SE

SURFE²R N1

SURFE²R N1

Orbit 16

Orbit 16

Orbit Mini

Orbit Mini

Vesicle Prep Pro

Vesicle Prep Pro

2016 - Human TRPA1 is a heat sensor displaying intrinsic U-shaped thermosensitivity

icon pap  Port-a-Patch and   icon vpp   Vesicle Prep Pro publication in Scientific Reports (2016)

Authors: 
Moparthi L., Kichko T. I., Eberhardt M., Högestätt E. D., Kjellbom P., Johanson U., Reeh P., W., Leffler A., Filipovic M. R., Zygmunt P. M.

 

Journal: 
Scientific Reports (2016) 6:28763


Abstract: 

Thermosensitive Transient Receptor Potential (TRP) channels are believed to respond to either cold or heat. In the case of TRP subtype A1 (TRPA1), there seems to be a species-dependent divergence in temperature sensation as non-mammalian TRPA1 is heat-sensitive whereas mammalian TRPA1 is sensitive to cold. It has been speculated but never experimentally proven that TRPA1 and other temperature-sensitive ion channels have the inherent capability of responding to both cold and heat. Here we show that redox modification and ligands affect human TRPA1 (hTRPA1) cold and heat sensing properties in lipid bilayer and whole-cell patch-clamp recordings as well as heat-evoked TRPA1-dependent calcitonin gene-related peptide (CGRP) release from mouse trachea. Studies of purified hTRPA1 intrinsic tryptophan fluorescence, in the absence of lipid bilayer, consolidate hTRPA1 as an intrinsic bidirectional thermosensor that is modified by the redox state and ligands. Thus, the heat sensing property of TRPA1 is conserved in mammalians, in which TRPA1 may contribute to sensing warmth and uncomfortable heat in addition to noxious cold.


Download here

Back to Overview

Nanion Corporate Blog

Cookies make it easier for us to provide you with our services. With the usage of our services you permit us to use cookies.