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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Chloride channel 5

ClC-5, CLCN5
This gene encodes a member of the ClC family of chloride ion channels and ion transporters. The encoded protein is primarily localized to endosomal membranes and may function to facilitate albumin uptake by the renal proximal tubule. Mutations in this gene have been found in Dent disease and renal tubular disorders complicated by nephrolithiasis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.] (from NCBI)
Top mentioned proteins: HAD, ClC-3, CAN, ACID, ClC-4
Papers on ClC-5
Urine proteome analysis in Dent's disease shows high selective changes potentially involved in chronic renal damage.
Ghiggeri et al., Genova, Italy. In J Proteomics, Feb 2016
Results are presented here on a combined proteomic approach (LC-mass spectrometry, Western blot and zymograms for proteases and inhibitors) to characterise urine proteins in a large family (18 members, 6 hemizygous patients, 6 carrier females, and 6 normals) with Dent's diseases due to the 1070G>T mutation of the CLCN5.
[Clinical and genetic analysis of Dent disease in 4 Chinese children].
Sun et al., Beijing, China. In Zhongguo Dang Dai Er Ke Za Zhi, Dec 2015
Mutations of the CLCN5 gene were revealed in three patients (Cases 1, 2 and 4), including exon 6-7del, c.785_787de l(p.263del
The renoprotective effect of shichimotsukokato on hypertension-induced renal dysfunction in spontaneously hypertensive rats.
Shimada et al., Toyama, Japan. In J Nat Med, Dec 2015
A notable loss of chloride channel 5 (ClC-5), a chloride channel in the proximal renal tubules, occurred in the SHR control group.
Chloride-hydrogen antiporters ClC-3 and ClC-5 drive osteoblast mineralization and regulate fine-structure bone patterning in vitro.
Blair et al., Pittsburgh, United States. In Physiol Rep, Nov 2015
Gene screening in mineralizing osteoblasts showed dramatic expression of chloride-proton antiporters ClC-3 and ClC-5.
Chloride transporters and receptor-mediated endocytosis in the renal proximal tubule.
Luciani et al., Zürich, Switzerland. In J Physiol, Oct 2015
Dedifferentiation of proximal tubule cells and dysfunction of receptor-mediated endocytosis characterize Dent's disease, a rare disorder caused by inactivating mutations in the CLCN5 gene that encodes the endosomal chloride-proton exchanger, ClC-5.
A tale of two CLCs: biophysical insights toward understanding ClC-5 and ClC-7 function in endosomes and lysosomes.
Zifarelli, Oxford, United Kingdom. In J Physiol, Oct 2015
The endosomal ClC-5 and the lysosomal ClC-7 are the best characterized human CLC transporters.
Mutation Update of the CLCN5 Gene Responsible for Dent Disease 1.
Vargas-Poussou et al., Paris, France. In Hum Mutat, Aug 2015
Two genetic subtypes have been described to date: Dent disease 1 is caused by mutations of the CLCN5 gene, coding for the chloride/proton exchanger ClC-5; and Dent disease 2 by mutations of the OCRL gene, coding for the inositol polyphosphate 5-phosphatase OCRL-1.
ClC-5: Physiological role and biophysical mechanisms.
Zifarelli et al., Genova, Italy. In Cell Calcium, Jul 2015
This review will focus on a member of the CLC protein family, the endosomal Cl(-)/H(+) antiporter ClC-5.
Nephrolithiasis, kidney failure and bone disorders in Dent disease patients with and without CLCN5 mutations.
Dent Disease Italian Network et al., Padova, Italy. In Springerplus, 2014
CLCN5 encodes the electrogenic chloride/proton exchanger ClC-5 which is involved in the tubular reabsorption of albumin and LMW proteins, OCRL encodes the inositol polyphosphate 5-phosphatase, and was initially associated with Lowe syndrome.
Dent-Wrong disease and other rare causes of the Fanconi syndrome.
Ing et al., Washington, D.C., United States. In Clin Kidney J, 2014
Since then, extensive investigation identified two genetic mutations (CLCN5 and OCRL1) to be associated with Dent-Wrong disease.
Patterned expression of ion channel genes in mouse dorsal raphe nucleus determined with the Allen Mouse Brain Atlas.
Commons et al., Boston, United States. In Brain Res, 2012
This study demonistrated that Clcn5 gene expression in mouse dorsal raphe nucleus
Glutamate 268 regulates transport probability of the anion/proton exchanger ClC-5.
Alekov et al., Hannover, Germany. In J Biol Chem, 2012
protonation of the gating glutamate 211 at the central anion-binding site of ClC-5 is mediated by the proton glutamate 268.
Chloride channel (Clc)-5 is necessary for exocytic trafficking of Na+/H+ exchanger 3 (NHE3).
Guggino et al., Baltimore, United States. In J Biol Chem, 2011
ClC-5 plays an essential role in exocytosis of NHE3.
Heterogeneity in the processing of CLCN5 mutants related to Dent disease.
Lourdel et al., Paris, France. In Hum Mutat, 2011
Heterogeneity in the processing of CLCN5 mutants related to Dent disease.
Endosomal chloride-proton exchange rather than chloride conductance is crucial for renal endocytosis.
Jentsch et al., Berlin, Germany. In Science, 2010
findings show that endosomal chloride concentration, which is raised by ClC-5 in exchange for protons accumulated by H+-ATPase, may play a role in endocytosis
Role of CFTR and ClC-5 in modulating vacuolar H+-ATPase activity in kidney proximal tubule.
Malnic et al., São Paulo, Brazil. In Cell Physiol Biochem, 2009
ClC-5 chloride-proton exchangers by siRNA-mediated silencing are important modulators of H+-ATPase function in immortalized rat renal proximal tubule cells.
The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes.
Mindell et al., Bethesda, United States. In Nature, 2008
Several mammalian members of the CLC family have been characterized in detail; some (including ClC-0, ClC-1 and ClC-2) function as Cl--conducting ion channels, whereas others act as Cl-/H+antiporters (ClC-4 and ClC-5).
The nitrate/proton antiporter AtCLCa mediates nitrate accumulation in plant vacuoles.
Barbier-Brygoo et al., Gif-sur-Yvette, France. In Nature, 2006
Some members of the chloride channel (CLC) protein family, such as the torpedo-fish ClC-0 and mammalian ClC-1, are anion channels, whereas the bacterial ClC-ec1 and mammalian ClC-4 and ClC-5 have recently been characterized as Cl-/H+ exchangers with unknown cellular functions.
Chloride/proton antiporter activity of mammalian CLC proteins ClC-4 and ClC-5.
Pusch et al., Genova, Italy. In Nature, 2005
coupled Cl-/H+ transport of ClC-4 and ClC-5 is of significant magnitude in vivo
Voltage-dependent electrogenic chloride/proton exchange by endosomal CLC proteins.
Jentsch et al., Hamburg, Germany. In Nature, 2005
Loss-of-function mutations in the endosomal protein ClC-5 impair renal endocytosis and lead to kidney stones, whereas loss of function of the endosomal/lysosomal protein ClC-7 entails osteopetrosis and lysosomal storage disease.
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