About: TRPV5 is a research topic. Over the lifetime, 159 publications have been published within this topic receiving 10646 citations. The topic is also known as: CAT2 & ECAC1.
TL;DR: It is reported here that TRPV5 is stimulated by the mammalian hormone klotho, which activates a cell surface channel by hydrolysis of its extracellular N-linked oligosaccharides and maintains durable calcium channel activity and membrane calcium permeability in kidney.
Abstract: Blood calcium concentration is maintained within a narrow range despite large variations in dietary input and body demand. The Transient Receptor Potential ion channel TRPV5 has been implicated in this process. We report here that TRPV5 is stimulated by the mammalian hormone klotho. Klotho, a beta-glucuronidase, hydrolyzes extracellular sugar residues on TRPV5, entrapping the channel in the plasma membrane. This maintains durable calcium channel activity and membrane calcium permeability in kidney. Thus, klotho activates a cell surface channel by hydrolysis of its extracellular N-linked oligosaccharides.
TL;DR: This novel epithelial Ca2+ channel (ECaC) of 730 amino acids contains six putative membrane-spanning domains with an additional hydrophobic stretch predicted to be the pore region and has the expected properties for being the gatekeeper of 1,25-dihydroxyvitamin D3-dependent active transepithelial Ca 2+ transport.
TL;DR: The data suggest the existence of a common activation mechanism for TRPV1,TRPV2, and TRPv3 that may serve as a therapeutic target for pain management and treatment for diseases caused by hypersensitivity and temperature misregulation.
TL;DR: Following cloning of the vanilloid receptor 1 (VR1), at least four other related proteins have been identified and these form a distinct subgroup of the transient receptor potential (TRP) family of ion channels, which have potential for the development of many future disease treatments.
TL;DR: The cloning of a novel transient receptor potential cation channel gene is reported and it is shown that this gene is mutated in patients with the disorder.
Abstract: Mucolipidosis type IV (MLIV) is a developmental neurodegenerative disorder characterized by severe neurologic and ophthalmologic abnormalities. The MLIV gene, ML4 (MCOLN1), has recently been localized to chromosome 19p13.2-13.3 by genetic linkage. Here we report the cloning of a novel transient receptor potential cation channel gene and show that this gene is mutated in patients with the disorder. ML4 encodes a protein, which we propose to call mucolipin, which has six predicted transmembrane domains and is a member of the polycystin II subfamily of the Drosophila transient receptor potential gene family. The role of a potential receptor-stimulated cation channel defect in the pathogenesis of mucolipidosis IV is discussed.