TRPV1 Membrane Protein Introduction

Introduction of TRPV1

TRPV1, also known as the capsaicin receptor and the vanilloid receptor 1 (VR1), belongs to the transient receptor potential cation channel subfamily V. TRPV1 gene is located at chromosome 17p13.2 and four alternatively spliced transcript variants have been reported. TRPV1 contains 6 transmembrane segments (S1-S6) and exhibits four-fold symmetry around a central ion pathway formed by S5-S6 and the intervening pore loop, which is flanked by S1-S4 voltage-sensor-like domains. TRPV1 is widely expressed in the duodenum, ovary, small intestine, skin, kidney, endometrium, and multiple other tissues.

Function of TRPV1 Membrane Protein

As a non-selective ion channel, TRPV1 is involved in a wide range of processes including nociception, thermosensation, and energy homeostasis. The primary role of TRPV1 is to detect and subsequently regulate body temperature. TRPV1 can be activated by a wide number of endogenous and exogenous chemical and physical stimulus, including a temperature above 43°C (109°F), acidic conditions, allyl isothiocyanate, the pungent compound in wasabi and mustard, and capsaicin. The TRPV1 activation results in a painful, burning sensation. The reported endogenous activators include low pH, N-oleyl-dopamine, the endocannabinoid anandamide, and N-arachidonoyl-dopamine. TRPV1 receptors are presented primarily in the nociceptive neurons of the peripheral nervous system and the central nervous system. TRPV1 plays a crucial role in the modulation and transmission of pain sensation, and it is also responsible for the integration of diverse painful stimuli. This receptor is also activated by increases in temperature in the noxious range, suggesting that it functions as a transducer of painful thermal stimuli in vivo.

Fig.1 The simulated model of TRPV1 based on a homology model. (Brauchi, 2007)

Application of TRPV1 Membrane Protein in Literature

1. Tykocki N.R., et al. Development of stress-induced bladder insufficiency requires functional TRPV1 channels. Am J Physiol Renal Physiol. 2018, 315(6): F1583-F1591. PubMed ID: 30089031
   
   

   This article suggests that TRPV1 ion channels are key components in the development of stress-induced bladder dysfunction, both with regard to bladder wall decompensation that results in the underactive bladder, and increased sensory outflow that results in overactive bladder.

2. Bashiri H., et al. Activation of TRPV1 receptors affects memory function and hippocampal TRPV1 and CREB mRNA expression in a rat model of biliary cirrhosis. Neurol Res. 2018, 6:1-10. PubMed ID: 30079821
   
   

   This article reveals that TRPV1 receptor may be associated with the modulation of memory and learning functions, and suggests that activated TRPV1 channels may be potential therapeutic targets for treatment of learning and memory impairments following biliary cirrhosis.

3. Yu S.Q., et al. Activation of TRPV1 Prevents Salt-Induced Kidney Damage and Hypertension After Renal Ischemia-Reperfusion Injury in Rats. Kidney Blood Press Res. 2018, 43(4):1285-1296. PubMed ID: 30078015
   
   

   This article confirms that activated TRPV1 ion channel plays anti-oxidative stress and anti-inflammatory role in preventing renal tissue damage and salt-induced hypertension after ischemia-reperfusion injury, and indicates that TRPV1 conveys preconditioning protection that may have a therapeutic implication.

4. Barbero R., et al. Expression of functional TRPV1 receptor in primary culture of canine keratinocytes. J Vet Pharmacol Ther. 2018, 41(6):795-804. PubMed ID: 30043987
   
   

   This article confirms the characterization and the identification of TRPV1 receptor in primary canine keratinocytes cultures.

5. Zhang X., et al. The contribution of TRPV1 channel to 20-HETE-Aggravated ischemic neuronal injury. Prostaglandins Other Lipid Mediat. 2018, 137:63-68. PubMed ID: 30041768
   
   

   This article concludes that TRPV1 ion channels are involved in neurotoxicity after ischemia and 20-HETE's reactive oxygen species generation.

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Reference

1. Brauchi S, et al. (2007). Dissection of the components for PIP2 activation and thermosensation in TRP channels. Proc Natl Acad Sci U S A. 104(24):10246-51.

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