Ask about this productRelated genes to: TRPV5 antibody
- Gene:
- TRPV5 NIH gene
- Name:
- transient receptor potential cation channel subfamily V member 5
- Previous symbol:
- ECAC1
- Synonyms:
- CaT2
- Chromosome:
- 7q34
- Locus Type:
- gene with protein product
- Date approved:
- 2000-05-05
- Date modifiied:
- 2016-01-28
Related products to: TRPV5 antibody
Related articles to: TRPV5 antibody
- TRPV5 is a calcium-selective epithelial ion channel that is essential for renal Ca reabsorption and systemic calcium homeostasis. Despite recent structural advances, the energetic basis and coordinated contributions of the three selectivity-filter residues (D542, T539, and N572/I575) to Ca selectivity remain unresolved. Here, we combine absolute and relative binding free-energy calculations (ABFE/RBFE), pore radius, and electrostatic analyses, and adaptive steered molecular dynamics (ASMD) to quantify how Ca and Na interact with and traverse these key sites in both wild-type and mutant channels. Free-energy analyses show that all three sites favor Ca over Na, with the outer D542 site making the dominant contribution to Ca selectivity, whereas T539 and N572/I575 provide weaker secondary contributions. ASMD-derived free-energy profiles further reveal a pronounced energetic preference for the Ca-driven displacement of Na. Mutation of any one of the three selectivity-filter residues induced perturbations of pore radius and electrostatic landscapes attenuated the energetic preference, revealing the cooperative contribution of these three sites to Ca selectivity in wild-type TRPV5. Based on the above results, we provide a hierarchical mechanism involving high-affinity Ca capture at D542 and subsequent downstream modulation of the free-energy landscape by T539 and N572, forming an integrated structure-energy framework for selective Ca permeation, offering testable hypotheses for disease variants and targeted modulation of TRPV5 in calcium-handling disorders. - Source: PubMed
Publication date: 2026/04/23
Meng YuxinLin YuhongShen Yong - Calcium (Ca²⁺) homeostasis is tightly regulated by the coordinated actions of the intestine, kidneys and bone. Ca²⁺ transport occurs via either a paracellular pathway, which depends on the expression of select claudins, including claudin-12 (CLDN12) in the tight junction, or a transcellular pathway, involving apical influx through TRPV6. While disruption of paracellular or transcellular pathways impairs transepithelial Ca²⁺ flux, Cldn12-deficient mice and Trpv6 mutant (Trpv6) mice do not display alterations in Ca²⁺ balance as reported previously, perhaps because one pathway compensates for the other. To test this hypothesis, we generated a double knockout mouse (DKO, Cldn12/ Trpv6) to assess Ca²⁺ homeostasis using metabolic cage balance studies, quantitative real-time PCR, and micro-computed tomography (Micro-CT). Despite lacking these key Ca²⁺ transport mechanisms, DKO mice maintained normal blood Ca²⁺. However, PTH and calcitriol were significantly elevated, as were renal Cyp27b1 and Cyp24a1 expression, consistent with hormonal compensation. The proximal colon and cecum exhibited significant compensatory changes in Ca²⁺-regulatory gene expression, including upregulation of the Ca²⁺ buffer S100g and basolateral extrusion mechanism Atp2b1. Notably, the Ca²⁺ channel Trpv5, which is absent from the intestine, became detectable in the proximal colon and cecum, but not in the distal colon or small intestine of DKO mice. Micro-CT of bone revealed reduced trabecular bone volume and thickness, indicating increased bone resorption as a secondary compensatory mechanism. This study highlights the adaptive plasticity of Ca²⁺-regulatory mechanisms and suggests a role for TRPV5 in reabsorbing Ca²⁺ from the proximal colon and cecum when upstream mechanisms of Ca²⁺ absorption are impaired. - Source: PubMed
Publication date: 2026/04/09
Deluque Amanda LimaPan WanlingO'Neill DeborahBogdanovic MilosDimke HenrikDoschak Michael RAlexander R Todd - TRPV5 channels play a critical role in calcium homeostasis and are implicated in various pathophysiological conditions. Here, we demonstrate that the monoterpene menthol, commonly used for pain and inflammation management, is an inhibitor of TRPV5. Electrophysiology experiments reveal that menthol blocks ion conduction through a slow blocker mechanism. Using single-particle cryo-EM, we determine the structure of menthol-bound TRPV5, which shows menthol interacting with W583, a residue previously implicated in channel permeation, gating and binding of endogenous modulators. These findings expand the repertoire of TRPV5 modulators and suggest that menthol could serve as a scaffold for developing channel-targeting modulators. - Source: PubMed
Publication date: 2026/03/18
Méndez-Reséndiz AngélicaDe Jesús-Pérez José JRangel-Yescas Gisela ERosenbaum TamaraMoiseenkova-Bell VeraIslas León D - Optimizing calcium metabolism is crucial for skeletal development and overall productivity in growing ruminants. Twenty-four Sunite lambs were randomly assigned to four groups and fed 0, 0.6, 1.2, or 2.4 g/(d·head) of γ-PGA for 60 days. Growth performance, serum parameters, duodenal morphology and calcium transporter expression, bone microarchitecture, and duodenal microbiota were analyzed. Supplementation with 1.2 g/(d·head) of γ-PGA (the M group) yielded optimal results, significantly improving final body weight and size. It enhanced duodenal health, evidenced by increased villus height, crypt depth, and microvilli density. Crucially, this dose significantly upregulated the expression of key duodenal calcium transporters (TRPV5/6, CaBPD9k, PMCA, VDR, claudin-12) and altered systemic calcium-regulating hormones (elevated calcitriol, PTH, FGF23). Bone micro-CT analysis revealed changes in trabecular architecture indicative of active remodeling. 16S rRNA sequencing and weighted OTU co-expression network analysis (WOCNA) revealed that γ-PGA reshaped the duodenal microbiota and identified core microbial modules strongly associated with host phenotypes. Genera such as [Eubacterium]_ruminantium_group, Fusicatenibacter, and Prevotella emerged as central hubs. In conclusion, dietary γ-PGA at 1.2 g/(d·head) enhances calcium absorption and bone metabolism in lambs through a coordinated modulation of intestinal integrity and calcium transport, systemic endocrine responses, and the duodenal microbial community, with specific microbiota identified as potential key mediators associated with these effects. - Source: PubMed
Publication date: 2026/03/04
Zhang XingfuGuo LiliZhao YaboWei WurilegeZhang JingDai LingliYang BinLiu ZaixiaWang XuBai ChenDu RuipingTong ManmanLi ShuyiWang JianmengSun YanyongSong Liwen - This study aimed to investigate the effectiveness of intraepididymal platelet-rich plasma (PRP) administration in preventing cryopreservation-induced sperm damage in rams. Twelve adult rams were randomly assigned into two groups ( = 6) in the non-breeding season. Rams in the PRP group received 0.2 ml/per epididymis (150–200 × 10⁶ platelets) of PRP every 15 days for a total of six injections, while control group received the same volume of saline. Semen samples were collected biweekly and pooled within each group before undergoing standard cryopreservation procedures. Post-thaw analyses included morphological, functional, biochemical, and molecular assessments. Compared to the control, intraepididimal PRP significantly increased hypo-osmotic swelling (HOS) response, total and progressive motility, rapid sperm percentage, and kinetic parameters (VCL- curvilinear velocity, VSL- straight-line velocity, VAP- average path velocity), while reducing static and acrosome-damaged sperm in thawed semen. Intraepididimal PRP also enhanced catalase activity, cholesterol and myristic acid (C14:0) concentrations and the levels of steroidogenic acute regulatory protein (StAR), 3β-hydroxysteroid dehydrogenase type 1 (HSD3β1), cation channel of sperm (CatSper1), platelet-derived growth factor (PDGF), platelet-derived growth factor receptor (PDGFR), and reduced malondialdehyde level in thawed semen. Intraepididimal PRP significantly increased the mRNA presence of CatSper2, CatSper3, CatSper4, transient receptor potential melastatin 3 (TRPM3) and transient receptor potential vanilloid 5 (TRPV5) ion channels, oar-miR-3958-3p and oar-miR-125b, and decreased bta-miR-22-3p and rno-miR-494 in thawed semen. Additionally, intraepididimal PRP significantly upregulated the protein expressions of CatSper3, HSD3β2 and PDGFA, and decreased protein expressions of vascular endothelial growth factor A (VEGFA) and transforming growth factor beta 1 (TGFβ1) in thawed semen. In conclusion, intraepididymal PRP administration improved cryoresistance in ram spermatozoa, likely due to its growth factors, lipids, and antioxidants. These effects enhanced post-thaw sperm quality by modulating oxidative stress, cholesterol, ion channels, microRNAs, and steroidogenic proteins, indicating PRP as a promising tool for improving semen cryotolerance in rams. - Source: PubMed
Publication date: 2026/02/28
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