TRPA1 Membrane Protein Introduction

Introduction of TRPA1

Transient receptor potential cation channel subfamily A member 1, encoded by the TRPA1 gene, is also known as transient receptor potential ankyrin 1 (TRPA1). It is one of the members of the TRP superfamily of structurally related, non-selective cation channels. As an ion channel, TRPA1 is mainly located on the plasma membrane of many human and animal cells. TRPA1 is best known as a sensor for environmental irritants. It has a biased expression in the urinary bladder, colon, appendix, duodenum, gall bladder, stomach, and small intestine. No alternatively spliced transcript variant of TRPA1 has been reported.

Function of TRPA1 Membrane Protein

Generally, TRPA1 functions as a sensor of chemical and mechanical stress, but the specific function of TRPA1 is still unclear. However, there are various studies have indicated that the function may be associated with growth control and signal transduction. Recent studies suggest that TRPA1 can be activated by many reactive (cinnamaldehyde, allyl isothiocyanate, formalin, farnesyl thiosalicylic acid, 4-hydroxynonenal, hydrogen peroxide, acrolein, and tear gases) and non-reactive compounds (nicotine, PF-4840154) and considered as a chemosensor in the body. Additionally, TRPA1 is also considered as a pain target on account of the fact that mice with TRPA1 knockout show near thorough attenuation of formalin-induced pain behaviors. It is reported that the antagonists of TRPA1 can block pain behaviors induced by inflammation. On the other side, several studies have demonstrated that cold sensation is regulated by TRPA1 in vitro, but there is no in vivo evidence. The structure of human TRPA1 has been solved by electron microscopy.

Fig.1 Structure of the TRPA1 ion channel determined by electron cryo-microscopy. (Paulsen, 2015)

Application of TRPA1 Membrane Protein in Literature

1. Han Q., et al. miRNA-711 Binds and Activates TRPA1 Extracellularly to Evoke Acute and Chronic Pruritus. Neuron. 2018, 99(3): 449-463.e6. PubMed ID: 30033153
   
   

   This article demonstrates a special physiological role of extracellular naked miRNAs as ion channel (TRPA1) modulators and itch mediators to evoke chronic and acute pruritus.

2. Chianese G., et al. TRPA1 Modulating C14 Polyacetylenes from the Iranian Endemic Plant Echinophora platyloba. Molecules. 2018, 23(7). pii: E1750. PubMed ID: 30018233
   
   

   This article firstly reports the activity of plant polyacetylenes on transient receptor potential (TRP) channels, and demonstrates that C14 polyacetylenes can be modulated by TRPA1.

3. Hiyama H., et al. TRPA1 sensitization during diabetic vascular impairment contributes to cold hypersensitivity in a mouse model of painful diabetic peripheral neuropathy. Mol Pain. 2018, 14: 1744806918789812. PubMed ID: 29968518
   
   

   This article suggests that cold hypersensitivity in the early painful phase of diabetic peripheral neuropathy may be caused by sensitization of TRPA1 during diabetic vascular impairment.

4. Wang S., et al. Roles of TRPV1 and TRPA1 in Spontaneous Pain from Inflamed Masseter Muscle. Neuroscience. 2018, 384: 290-299. PubMed ID: 29890293
   
   

   This article confirms that concurrent repression of TRPA1 and TRPV1 can lead to significant relief of spontaneous pain, but doesn’t relieve bite-evoked pain during masseter inflammation, suggesting that mechanisms of bite-evoked and spontaneous pain from inflamed masseter muscle are distinct.

5. Nielsen T.A., et al. Psychophysical and vasomotor evidence for interdependency of TRPA1 and TRPV1 nociceptive responses in human skin: an experimental study. Pain. 2018, 159(10): 1989-2001. PubMed ID: 29847470
   
   

   This article demonstrates that TRPA1 nociceptive responses in human skin rely heavily on intact capsaicin-sensitive, TPRV1 fibers.

TRPA1 Preparation Options

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Reference

1. Paulsen C E, et al. (2015). Structure of the TRPA1 ion channel suggests regulatory mechanisms. Nature. 520: 511-517.

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