TRPV2 _ Vanilloid receptor_like protein 1
- Known as:
- TRPV2 _ Vanilloid receptor_like protein 1
- Catalog number:
- VRL11-S
- Product Quantity:
- 0.1 ml
- Category:
- -
- Supplier:
- ACR
- Gene target:
- TRPV2 _ Vanilloid receptor_like protein 1
Related genes to: TRPV2 _ Vanilloid receptor_like protein 1
- Gene:
- TRPV2 NIH gene
- Name:
- transient receptor potential cation channel subfamily V member 2
- Previous symbol:
- -
- Synonyms:
- VRL, VRL-1, VRL1
- Chromosome:
- 17p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-01-29
- Date modifiied:
- 2016-01-28
Related products to: TRPV2 _ Vanilloid receptor_like protein 1
Related articles to: TRPV2 _ Vanilloid receptor_like protein 1
- Connexin hemichannels are critical mediators of cellular signaling in both physiological and pathological states, yet their selective pharmacological modulation has remained elusive because of the close structural similarity between hemichannels and gap junction channels formed by the same connexins. - Source: PubMed
Publication date: 2026/06/25
Lagos Carlos FVargas AnibalGarcía AnibalDuarte YorleyYi ChenjuSáez Juan C - Transient receptor potential vanilloid 2 (TRPV2) is highly expressed in immune cells, including mast cells, yet its functional role in mast cell physiology remains incompletely understood. Given the increasing global prevalence of immune disorders, elucidating TRPV2-mediated mechanisms may uncover novel therapeutic approaches. Using fluorometric Ca influx assays and electrophysiological patch-clamp recordings, this study analyzes synergistic effects of the TRPV2 activators AV2-1, cannabidiol and probenecid. Superadditive TRPV2 activation was observed upon co-application of probenecid and cannabidiol, as well as by the combination of AV2-1 and cannabidiol. The effects of the activators were validated in primary mouse bone marrow-derived mast cells (mBMMCs) and the human mast cell-like cell line HMC-1.2. Activation of TRPV2 by the cannabidiol/probenecid combination or by AV2-1 alone induced mBMMC degranulation, as assessed by β-hexosaminidase release, histamine secretion, and increased CD63 surface expression measured by flow cytometry, without evidence of long-term cytotoxicity. TRPV2-dependent degranulation was additive to FcεRI-mediated responses induced by anti-DNP-IgE/DNP-HSA stimulation, indicating mechanistically distinct signaling pathways. In addition, TRPV2 activation enhanced mBMMC migration. All observed effects were abolished by the TRPV2 inhibitor IV2-1 or genetic deletion of TRPV2 in transwell migration assays. These findings demonstrate that pharmacological activation of TRPV2 modulates mast cell effector functions and migration, supporting a role for TRPV2 as an immunomodulatory ion channel and a potential therapeutic target in immune system-related pathologies. - Source: PubMed
Publication date: 2026/07/09
Leipe AndreaRaudszus RickUrban NicoleSchaefer MichaelHill Kerstin - TRPA1 and TRPV1 are nociceptive ion channels that integrate noxious chemical stimuli and are attractive targets for non-opioid analgesics. The phytocannabinoids cannabidiol (CBD) and cannabigerol (CBG) modulate both channels, but their pharmacological profiles and underlying structural determinants remain poorly defined. Here, we used rational ligand design to convert CBD and CBG into potent dual TRPA1/TRPV1 agonists and to probe a conserved lipid-sensing architecture in both channels. Guided by the structural features of the TRPV1 vanilloid-binding site and our previously developed TRPA1 cannabinoid-binding site model, we incorporated an aryl carbamate anchor into the CBD and CBG scaffolds. We compared their activity with that of the parent phytocannabinoids in heterologous expression systems using calcium imaging and whole-cell patch-clamp recordings. Whereas CBD and CBG preferentially activated TRPA1 and were weak TRPV1 agonists at physiologically relevant concentrations, carbamate functionalization markedly increased potency and efficacy at TRPV1 while preserving robust TRPA1 activation. In contrast to the parent phytocannabinoids, carbamate derivatives did not potentiate TRPV2 responses, demonstrating channel selectivity. Site-directed mutagenesis and molecular docking localized carbamate-based ligand binding to the canonical vanilloid binding site in TRPV1 and the non-electrophilic cannabinoid-binding site in TRPA1, consistent with engagement of a shared lipid-sensing pocket. Carbamate derivatives also activated nociceptive neurons in primary rat trigeminal ganglion cultures in a TRPV1-dependent manner, as confirmed by pharmacological block with the selective TRPV1 antagonist BCTC. These findings define a conserved structural framework for lipid ligand recognition in TRPA1 and TRPV1 and provide a rational starting point for developing dual-target modulators of peripheral nociceptors. - Source: PubMed
Publication date: 2026/06/24
Amawi TalaKolesnykova YuliyaGhantous MarianaNmarneh AlaaKonovalov YanaGhantous NayefTsvelikhovsky DmitryPriel Avi - - Source: PubMed
Poole Alastair W - The homotetrameric thermosensitive transient receptor potential vanilloid 2 (TRPV2) channel is a biological macromolecule with unique high temperature threshold and sensitivity. However, the underlying thermodynamic basis has not been well understood. In this computational study, the 3D cryo-EM structures of rat TRPV2 in response to various chemical perturbations at different sites at low temperatures were quantified at the tertiary and quaternary levels using a highly sensitive thermoring model. The results indicated that a putative stable pre-open closed state without a lipid at the well-known active vanilloid site exhibited at least three weakest tertiary noncovalent bridges on the protein surface as primary thermal sensors with matched thresholds for initial heat activation. Any chemical perturbation away from these sensors activated the channel but with lower cold sensitivity. In contrast, when the sensors were simultaneously exposed to a mild detergent, together with hydrolysis of nearby charged residues at the membrane surface, the channel could be opened with the unique high cold sensitivity similarly to mirror the initial heat sensation. Further, disrupting intersubunit interactions near the heat sensors was required for full channel opening at both upper and lower gates. Therefore, the heat capacity mechanism, once cross-examined, could be applied to elucidate the unique thermoring basis for the sharp heat response of thermosensitive TRPV2 above body temperature. - Source: PubMed
Publication date: 2026/06/10
Wang Guangyu