TRPV5 belongs to the TRP superfamily, which consists of cation-selective ion channels with similar molecular structures. The TRPV5 gene consists of 15 exons, which translates into a protein of 729 amino acids in human. This protein contains six putative transmembrane domains and an intracellular N and C tail. Functional TRPV5 channels exist as tetramers forming together a single Ca²⁺-selective pore. The pore is formed by the hydrophobic region between TM5 and TM6. The pore-residue aspartate-542 appeared to be crucial for high-affinity Ca²⁺ binding and selectivity. Mutation of this aspartate into an alanine abolished Ca²⁺ permeation, whereas the current carried by monovalent cations remained intact. The channel is activated by low internal calcium level and the current exhibits an inward rectification. A Ca²⁺-dependent feedback regulation includes fast channel inactivation and slow current decay. TRPV5 is expressed in kidney, duodenum, jejunum, placenta and pancreas.
|Basic Information of TRPV5|
|Protein Name||Transient receptor potential cation channel subfamily V member 5|
|Gene Name||TRPV5, ECAC1|
|Aliases||Calcium transport protein 2 (CaT2), Epithelial calcium channel 1 (ECaC, ECaC1), Osm-9-like TRP channel (OTRPC3)|
|Organism||Homo sapiens (Human)|
As a Ca²⁺ channel, TRPV-5 contributes to maintaining the homeostasis of the human skeleton via a negative feedback loop in receptor activator of NF-κB ligand (RANKL)-induced bone resorption. Furthermore, analysis of femoral bone sections from TRPV5 knockout (TRPV5-/-) mice revealed increased osteoclast numbers and osteoclast area. Therefore, TRPV5 is essential for osteoclast differentiation and bone resorption. TRPV5 has also been confirmed to be involved in the estrogen-mediated Ca²⁺ influx in many cells. It has been demonstrated that TRPV5 protein expression is highly modulated by estrogen in the kidney. Furthermore, estrogen has the ability to regulate renal Ca²⁺ re-absorption through rapid effects on TRPV5 channel activity in kidney and intestine, which is required for normal Ca²⁺ reabsorption in the kidney distal convoluted tubules.
Fig.1 Models of the regulation of apical membrane TRPV5 in renal distal tubules by Klotho and FGF23. (Andrukhova, 2014)
This article finds that TRPV5 represents a potential therapeutic target for disorders with altered Ca(2+) homeostasis.
This article shows that a novel primary cell model with TRPV5-dependent Ca(2+) transport characteristics is successfully established, enabling comprehensive studies of transcellular Ca(2+) transport.
This article suggests that strong environmental cues may affect the intracellular calcium level in Jurkat T cells by influencing the traffic of TRPV5/V6 channels in lymphocytes.
This article reveals that the combined expression of TRPV5 and TRPV6 in tumor tissues presents promising prognostic value in NSCLC patients.
This article suggests that TRPV5 may contribute to the process of estrogen-inhibited osteoclastogenesis and bone resorption activity.
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