Ask about this productRelated genes to: TRPM5 Blocking Peptide
- Gene:
- TRPM5 NIH gene
- Name:
- transient receptor potential cation channel subfamily M member 5
- Previous symbol:
- -
- Synonyms:
- LTRPC5, MTR1
- Chromosome:
- 11p15.5
- Locus Type:
- gene with protein product
- Date approved:
- 2002-01-11
- Date modifiied:
- 2016-01-28
Related products to: TRPM5 Blocking Peptide
Related articles to: TRPM5 Blocking Peptide
- Tuft cells (TCs) act as crucial airway sentinels that detect bacterial metabolites and initiate immune responses, yet the underlying mechanisms remain poorly understood. Here, we identify tracheal TCs as the initial source of leukotrienes (LTs), released during bacterial infection. Tracheal TCs discriminate pathogenic from commensal bacteria by sensing extracellular ATP (eATP) released by pathogens, including Pseudomonas aeruginosa and Rodentibacter pneumotropicus, within 4 h of infection, through the transient receptor potential cation channel subfamily M member 5 (Trpm5). This induces the LT release, including LTB, and promotes rapid recruitment of neutrophils and macrophages to the trachea and alveolar spaces. Trpm5 mice failed to detect bacterial eATP, exhibited neutrophil sequestration in the spleen, and became colonized following R. pneumotropicus infection, while Trpm5 mice efficiently cleared the pathogen. These findings uncover a critical TC-dependent sensing mechanism in pneumonia, establishing TCs as both ATP sensors and triggers of acute innate immune responses. - Source: PubMed
Publication date: 2026/08/21
Elhawy Mohamed IbrahemWadood Noran AbdelGrammer MariaBetzold PaulaHerrmann EmelyLanzilli Giuseppina SoleBiradli FiratKlozenbücher CarolineKlein AndreasAlakkam NosaibahHollenhorst Monika IGaini-Rahimi KianaEvers Saskia BKusumakshi SoumyaWyatt AmandaKany Andreas MBecker Sören LBischoff MarkusFlockerzi VeitGudermann ThomasChubanov VladimirEmpting MartinHirsch Anna K HSchneider ChristophBoehm UlrichKrasteva-Christ Gabriela - Bitter taste receptors are distributed in various non-taste tissues and cells, where they exert crucial roles in neuroimmune regulation and inflammatory response. In this study, a mouse model of fine particle (FPs) exposure was established by nebulized ovalbumin (OVA) inhalation to investigate the effects of FPs on renal function and structure. The experiment results revealed that inhalation of OVA led to glomerular atrophy, and renal tubular epithelial cell swelling and vacuolization, accompanied by increased levels of blood urea nitrogen and creatinine in the bloodstream. OVA inhalation induced a significant elevation in the levels of HO and malondialdehyde (MDA), while significantly decreased the activity of total superoxide dismutase (T-SOD) and the content of glutathione (GSH) in renal tissues. Furthermore, OVA downregulated Th1 cytokine IFN-γ, upregulated Th2 cytokines IL-4, IL-5 and IL-13, and activated pro-inflammatory cytokines (TNF-α, IL-1β, IL-6) as well as genes involved in inflammatory pathways (TLR-2, TLR-4, MyD88, NF-κB, JAK-1, JAK-2, JAK-3, STAT-3, STAT-6). Notably, OVA-induced kidney injury was accompanied by the downregulation of bitter taste receptors and their downstream signaling molecules (α-gustducin, transient receptor potential melastatin 5 [Trpm5]). However, gavage administration of multi-strain probiotics significantly alleviated the toxic effects of OVA on the mouse kidneys, as evidenced by the reversal of the aforementioned abnormal changes in renal structure, biochemical indicators, oxidative stress markers, inflammatory factors, and bitter taste transduction-related molecules. Collectively, these findings indicate that OVA-induced distal organ injury, particularly renal injury, is associated with systemic inflammation and the inhibition of bitter taste transduction pathways. The protective effect of multi-strain probiotics on OVA-inhaled mice is correlated with the activation of bitter taste transduction, as well as the regulation of immune balance and inflammatory responses. - Source: PubMed
Publication date: 2026/07/22
Jiao SiweiZhang RuigangPei YaochenWang MuhuaMa JiePeng XiaoguangYi Huilan - Taste buds (TBs) are the fundamental units of taste perception and are distributed throughout the oral cavity, including the tongue, soft palate, epiglottis, pharynx, and retromolar pad. Despite their widespread presence, a complete and systematic understanding of TB distribution and functional organization remains incomplete. In this study, we focus on a small population of TBs located in the mandibular sublingual caruncle of mice, adjacent to the openings of the Wharton's ducts, a site previously noted in anatomical and physiological studies that has not been comprehensively characterized. TBs of the sublingual caruncle exhibit canonical morphology and cellular composition, comprising type I ( +), type II ( +), and type III ( +) cells, as confirmed by transgenic reporter lines and immunofluorescence staining. Molecular analysis revealed the expression of key taste transduction components, including , , and , as well as 26 of 35 bitter taste receptors. Immunofluorescence confirmed TB innervation by -positive nerve fibers, including -positive sensory afferents, -positive presynaptic terminals, and -positive peptidergic endings, indicating integration into the peripheral gustatory circuitry. Retrograde neuronal tracing (Dil/DiO) further demonstrated that nerve fibers associated with sublingual caruncle TBs project specifically to the geniculate but not the petrosal ganglion, supporting their attribution to the facial gustatory pathway. Functionally, localized sucrose stimulation of the sublingual caruncle elicited activation in the nucleus of the solitary tract, indicating central connectivity. Furthermore, tastants representing all 5 basic taste qualities (sweet, sour, bitter, umami, and salty) elicited measurable saliva secretion, with bitter-, sweet-, and umami-induced salivation reduced in transgenic mouse models with impaired gustatory function. Together, these findings establish the sublingual caruncle as a functional gustatory site involved in taste-evoked salivary reflexes, expanding current understanding of taste system organization and its coordination with salivary function. - Source: PubMed
Publication date: 2026/07/17
Liu JXi RHan MXu XTizzano M - Cetaceans and sirenians independently transitioned from land to water, evolving unique and convergent sensory adaptations shaped by aquatic environments. Among sensory receptors, the Transient Receptor Potential (TRP) channel superfamily is central to thermo-, chemo-, and mechanosensation, but its evolutionary history in fully aquatic mammals remains poorly characterized. Here, we investigated the molecular evolution of TRP channels in these lineages. Orthology and phylogenetic relationships were inferred using Maximum Likelihood and Bayesian approaches. Signals of positive selection and molecular convergence were evaluated with codon and amino acid models. Amino acid substitutions, protein structure, and stability were assessed using 3D protein modeling. Our analyses reveal accelerated evolutionary rates in aquatic mammals, including multiple positively selected sites, lineage-specific amino acid substitutions, and convergent evolution across cetaceans and sirenians. Protein-level assessments identified substitutions with potential functional consequences, and evidence of pseudogenization was detected in cetacean PKD1L3, PKD2L1, TRPA1, and TRPM5, in contrast to intact copies in sirenians. These patterns suggest lineage-specific sensory trajectories, including reduced chemosensory repertoires in cetaceans, conservation of taste-related genes in sirenians, and adaptations in somatosensory associated genes that reflect both convergent requirements of fully underwater living and distinct aquatic environments. Overall, our findings advance understanding of the molecular mechanisms underlying sensory evolution during the land-to-water transition in mammals. - Source: PubMed
Publication date: 2026/07/01
Lein-Borba Ana LuizaSelleghin-Veiga GiovannaDaros BeatrizMagpali LetíciaNery Mariana F - Proteins operate in dynamic environments where ions, lipids and temperature collectively define their properties, yet most studies rely on simplified conditions that overlook these intrinsic variables. Here we show two such factors-temperature and Ca-remodel the function and pharmacology of TRPM4, an ion channel implicated in cardiac conduction, immune regulation, cancer and intestinal-fluid homeostasis. At physiological temperature and Ca, TPPO-previously considered a selective TRPM5 inhibitor inactive toward TRPM4-potently activates TRPM4, revealing strong synergy among temperature, Ca and ligand binding. By contrast, Necrocide-1, a necroptotic activator targeting the same binding pocket, defies this logic: it opens TRPM4 without Ca but is antagonized by Ca. Meanwhile, the inhibitors NBA and CBA engage a nearby pocket, locking the channel in a non-conductive pre-open state. Our findings highlight that even rigid binding pockets can exhibit temperature-dependent ligand recognition, revealing hidden pharmacology and informing selective, environment-aware therapeutic strategies. - Source: PubMed
Publication date: 2026/06/09
Hu JinhongIevleva SofiaPark Sung JinLee JunukCheng JieO'Dea GarrettSheng JiangnanDu JuanLü Wei