TRPV1 Channel: A Noxious Signal Transducer That Affects Mitochondrial Function

Juárez-Contreras, Rebeca; Méndez-Reséndiz, Karina Angélica; Rosenbaum, Tamara; González‐Ramírez, Ricardo; Morales‐Lázaro, Sara L.

doi:10.3390/ijms21238882

Cited by 26 publications

(20 citation statements)

References 80 publications

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“…Although the TRPV1 protein has been mainly visualized in neuronal cells, there are studies that show its presence in the heart of the mouse. Furthermore, TRPV1 has been detected in mitochondrial fractions [ 16 , 18 ].…”

Section: Discussionmentioning

confidence: 99%

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TRPV1 Contributes to Modulate the Nitric Oxide Pathway and Oxidative Stress in the Isolated and Perfused Rat Heart during Ischemia and Reperfusion

et al. 2022

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The transient vanilloid receptor potential type 1 (TRPV1) regulates neuronal and vascular functions mediated by nitric oxide (NO) and by the calcitonin gene-related peptide (CGRP). Here, we study the participation of TRPV1 in the regulation of myocardial injury caused by ischemia-reperfusion and in the control of NO, tetrahydrobiopterin (BH4), the cGMP pathway, CGRP, total antioxidant capacity (TAC), malondialdehyde (MDA) and phosphodiesterase-3 (PDE-3). Isolated hearts of Wistar rats perfused according to the Langendorff technique were used to study the effects of an agonist of TRPV1, capsaicin (CS), an antagonist, capsazepine (CZ), and their combination CZ+CS. The hearts were subjected to three conditions: (1) control, (2) ischemia and (3) ischemia-reperfusion. We determined cardiac mechanical activity and the levels of NO, cGMP, BH4, CGRP, TAC, MDA and PDE-3 in ventricular tissue after administration of CS, CZ and CZ+CS. Western blots were used to study the expressions of eNOS, iNOS and phosphorylated NOS (pNOS). Structural changes were determined by histological evaluation. CS prevented damage caused by ischemia-reperfusion by improving cardiac mechanical activity and elevating the levels of NO, cGMP, BH4, TAC and CGRP. TRPV1 and iNOS expression were increased under ischemic conditions, while eNOS and pNOS were not modified. We conclude that the activation of TRPV1 constitutes a therapeutic possibility to counteract the damage caused by ischemia and reperfusion by regulating the NO pathway through CGRP.

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Section: Discussionmentioning

confidence: 99%

“…In the last two decades, TRPV1 has been proposed as a therapeutic possibility to reduce the effects of pain-related diseases such as migraine and other diseases including rheumatoid arthritis [ 15 , 16 , 17 ]. Moreover, CS and neuronal depletion of TRPV1 have been used as strategies in pain sensation studies.…”

Section: Introductionmentioning

confidence: 99%

TRPV1 Contributes to Modulate the Nitric Oxide Pathway and Oxidative Stress in the Isolated and Perfused Rat Heart during Ischemia and Reperfusion

et al. 2022

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“…TRPV1 is one of the TRP cation channels that can be activated by heat ( Zheng, 2013 ). The TPRV1 structure can be divided into three parts: the N- and C-termini in cells, and the six transmembrane segments with pore loop region formed between S5 and S6 ( Juárez-Contreras et al, 2020 ). The N-terminus of TRPV1 contains calmodulin and ATP binding sites, which modulate the activation of the channel ( Cao et al, 2013 ; Lee and Zheng, 2015 ).…”

Section: Overview On Trpv1mentioning

confidence: 99%

“…The intracellular localization of TRPV1 is different between tissues. For example, TRPV1 is present in both the SR and mitochondrial outer membrane in cardiomyocytes ( Randhawa and Jaggi, 2015 ; Juárez-Contreras et al, 2020 ), whereas TRPV1 in skeletal muscle cells is localized on the SR ( Xin et al, 2005 ). TRPV1 is enriched in longitudinal SR but not in the mixture of longitudinal SR and terminal cisternae, which is drawn from Western blot results from protein samples prepared by sucrose step gradient centrifuge ( Lotteau et al, 2013 ).…”

Section: Overview On Trpv1mentioning

confidence: 99%

Role of TRPV1 in High Temperature-Induced Mitochondrial Biogenesis in Skeletal Muscle: A Mini Review

Zhao

Gao

2022

Front. Cell Dev. Biol.

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Transient receptor potential vanilloid 1 (TRPV1) is a protein that is susceptible to cell environment temperature. High temperatures of 40–45°C can activate the TRPV1 channel. TRPV1 is highly expressed in skeletal muscle and located on the sarcoplasmic reticulum (SR). Therefore, TRPV1 activated by high-temperature stress releases Ca2+ from the SR to the cytoplasm. Cellular Ca2+ accumulation is a key event that enhances TRPV1 activity by directly binding to the N-terminus and C-terminus. Moreover, Ca2+ is the key messenger involved in regulating mitochondrial biogenesis in skeletal muscle. Long-term activation of TRPV1 may promote mitochondrial biogenesis in skeletal muscle through the Ca2+-CaMKII-p38 MAPK-PGC-1α signaling axis. The discovery of the TRPV1 channel highlights the potential mechanism for high-temperature stress improving muscle mitochondrial biogenesis. The appropriate hot stimulus in thermal environments might be beneficial to the muscular mitochondrial adaptation for aerobic capacity. However, the investigation of TRPV1 on mitochondrial biogenesis is at an early stage. Further investigations need to examine the role of TRPV1 in response to mitochondrial biogenesis in skeletal muscle induced by different thermal environments.

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“…The pharmacological activity of capsaicin is explained by its specific action on TRPV1 ion channels [ 4 , 5 ]. After exposure to a high or repeated dose of capsaicin, TRPV1 is desensitized with the subsequent inhibition resulting in analgesia.…”

Section: Introductionmentioning

confidence: 99%

Membrane Interactivity of Capsaicin Antagonized by Capsazepine

Mizogami

Tsuchiya

2022

IJMS

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Although the pharmacological activity of capsaicin has been explained by its specific binding to transient receptor potential vanilloid type 1, the amphiphilic structure of capsaicin may enable it to act on lipid bilayers. From a mechanistic point of view, we investigated whether capsaicin and its antagonist capsazepine interact with biomimetic membranes, and how capsazepine influences the membrane effect of capsaicin. Liposomal phospholipid membranes and neuro-mimetic membranes were prepared with 1,2-dipalmitoylphosphatidylcholine and with 1-palmitoyl-2-oleoylphosphatidylcholine and sphingomyelin plus cholesterol, respectively. These membrane preparations were subjected to reactions with capsaicin and capsazepine at 0.5–250 μM, followed by measuring fluorescence polarization to determine the membrane interactivity to modify the fluidity of membranes. Both compounds acted on 1,2-dipalmitoylphosphatidylcholine bilayers and changed membrane fluidity. Capsaicin concentration-dependently interacted with neuro-mimetic membranes to increase their fluidity at low micromolar concentrations, whereas capsazepine inversely decreased the membrane fluidity. When used in combination, capsazepine inhibited the effect of capsaicin on neuro-mimetic membranes. In addition to the direct action on transmembrane ion channels, capsaicin and capsazepine share membrane interactivity, but capsazepine is likely to competitively antagonize capsaicin’s interaction with neuro-mimetic membranes at pharmacokinetically-relevant concentrations. The structure-specific membrane interactivity may be partly responsible for the analgesic effect of capsaicin.

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TRPV1 Channel: A Noxious Signal Transducer That Affects Mitochondrial Function

Cited by 26 publications

References 80 publications

TRPV1 Contributes to Modulate the Nitric Oxide Pathway and Oxidative Stress in the Isolated and Perfused Rat Heart during Ischemia and Reperfusion

TRPV1 Contributes to Modulate the Nitric Oxide Pathway and Oxidative Stress in the Isolated and Perfused Rat Heart during Ischemia and Reperfusion

Role of TRPV1 in High Temperature-Induced Mitochondrial Biogenesis in Skeletal Muscle: A Mini Review

Membrane Interactivity of Capsaicin Antagonized by Capsazepine

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