{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTRPV5 is a highly Ca²⁺‐selective epithelial channel that serves as the gatekeeper for active Ca²⁺ reabsorption in the distal renal tubules, thereby playing a critical role in whole‐body calcium homeostasis (11765215."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In bone, its expression in osteoclasts is essential for normal bone remodeling, as impaired TRPV5 function disrupts Ca²⁺ resorption and alters osteoclast activity (16291808"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": "; 19295174."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " In the kidney, TRPV5 activity is acutely regulated by calciotropic signals. For example, parathyroid hormone rapidly stimulates the channel via a cAMP–protein kinase A cascade, thereby increasing its open probability (19423690"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": ", while activation of protein kinase C and the extracellular Ca²⁺‐sensing receptor further enhance Ca²⁺ influx (18305097"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "; 19157541."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": " Moreover, intracellular pathways involving kinases such as WNK4 together with scaffolding proteins like NHERF2 boost TRPV5 delivery to the plasma membrane (21187068"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": ", whereas extracellular modifiers—including tissue transglutaminase that alters glycosylation and plasmin acting via protease‐activated receptor‐1—act to inhibit its function (21952826"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": "; 23024298."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": " In addition, the anti‐aging protein Klotho promotes both forward trafficking and plasma membrane stability of TRPV5 (25378396"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": ", and interactions with phosphatidylinositol 4,5‐bisphosphate further fine‐tune channel kinetics (27291418."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAt the molecular and structural levels, genetic variations and high‐resolution imaging have provided crucial insights into TRPV5 function. Its expression is not confined to renal epithelia; TRPV5 is also detectable in the retinal pigment epithelium (20405023"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "and in blood cells where channel activity appears to correlate with proliferative status (23968883"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": "; 23970553."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": " Furthermore, targeted upregulation strategies using small activating RNAs have emerged as a means to enhance TRPV5 expression in kidney‐derived cells (25139832"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": ", and its expression in parathyroid tissue further underscores the channel’s broader physiological relevance (25164318."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": " At the level of amino acid sequence, site‐directed mutagenesis has revealed that substitution at methionine 490 (M490P) diminishes Ca²⁺‐dependent inactivation, thereby reducing Ca²⁺ permeability (21035851"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": ", whereas replacement of alanine 563 with threonine (A563T) stabilizes the pore and enhances Ca²⁺ influx (26837804."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": " In contrast, the L530R mutation disrupts hydrophobic interactions critical for proper folding and plasma membrane trafficking, effectively abolishing channel function (28847730."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": " Cryo‐electron microscopy has further delineated TRPV5’s closed pore conformation upon binding of inhibitory ligands (29323279"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}]}, {"type": "t", "text": ", while heteromeric assembly with TRPML3 points to potential diversification of its function in tissues such as the inner ear (23469151."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": " Comprehensive reviews have also emphasized the cooperative roles of TRPV5 and its close homolog TRPV6 in mediating epithelial Ca²⁺ absorption (26089600."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinical investigations have further linked TRPV5 to disorders of calcium homeostasis. Genetic aberrations and polymorphisms in TRPV5 are associated with renal hypercalciuria and an increased risk of nephrolithiasis across different populations (19131347"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": "; 31428848"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "; 31471161"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": "; 36088585."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "26"}]}, {"type": "t", "text": " In addition, modulation of TRPV5 activity may influence calcium signaling in neoplastic cells exposed to ionizing radiation, thereby affecting cell cycle progression and survival (21063097."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "27"}]}, {"type": "t", "text": " Collectively, these findings position TRPV5 as a pivotal determinant of epithelial Ca²⁺ transport and underscore its potential as a therapeutic target in conditions ranging from kidney stone disease to radiation‐induced cellular stress.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "R Vennekens, G Droogmans, B Nilius "}, {"type": "b", "children": [{"type": "t", "text": "Functional properties of the epithelial Ca2+ channel, ECaC."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gen Physiol Biophys (2001)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11765215"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11765215"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Bram C J van der Eerden, Joost G J Hoenderop, Teun J de Vries, et al. 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