scholarly journals Intracellular chloride channel protein CLIC1 regulates macrophage function through modulation of phagosomal acidification

2012 ◽  
Vol 125 (22) ◽  
pp. 5479-5488 ◽  
Author(s):  
Lele Jiang ◽  
Kanin Salao ◽  
Hui Li ◽  
Joanna M. Rybicka ◽  
Robin M. Yates ◽  
...  
Keyword(s):  
Chloride Channel ◽  
Macrophage Function ◽  
Channel Protein ◽  
Intracellular Chloride

Functional Expression of p64, an Intracellular Chloride Channel Protein

1998 ◽  
Vol 163 (2) ◽  
pp. 119-127 ◽  
Author(s):  
J.C. Edwards *, † , B. Tulk ◽  
P.H. Schlesinger
Keyword(s):  
Chloride Channel ◽  
Functional Expression ◽  
Channel Protein ◽  
Intracellular Chloride

Expression, Purification, Crystallization and Preliminary Crystallographic Analysis of the Human Intracellular Chloride Channel Protein CLIC4

2006 ◽  
Vol 13 (6) ◽  
pp. 641-643 ◽  
Author(s):  
De-Feng Li ◽  
Yun-Feng Li ◽  
Qiu-Hua Huang ◽  
Ying Zhang ◽  
Da-Cheng Wang
Keyword(s):  
Chloride Channel ◽  
Crystallographic Analysis ◽  
Channel Protein ◽  
Intracellular Chloride

scholarly journals mtCLIC/CLIC4, an Organellular Chloride Channel Protein, Is Increased by DNA Damage and Participates in the Apoptotic Response to p53

2002 ◽  
Vol 22 (11) ◽  
pp. 3610-3620 ◽  
Author(s):  
Ester Fernández-Salas ◽  
Kwang S. Suh ◽  
Vladislav V. Speransky ◽  
Wendy L. Bowers ◽  
Joshua M. Levy ◽  
...  
Keyword(s):  
Dna Damage ◽  
Chloride Channel ◽  
Chloride Channels ◽  
Mitochondrial Membrane ◽  
Cellular Response ◽  
Mitochondrial Protein ◽  
Inner Mitochondrial Membrane ◽  
Necrosis Factor Alpha ◽  
Channel Protein ◽  
Factor Alpha

ABSTRACT mtCLIC/CLIC4 (referred to here as mtCLIC) is a p53- and tumor necrosis factor alpha-regulated cytoplasmic and mitochondrial protein that belongs to the CLIC family of intracellular chloride channels. mtCLIC associates with the inner mitochondrial membrane. Dual regulation of mtCLIC by two stress response pathways suggested that this chloride channel protein might contribute to the cellular response to cytotoxic stimuli. DNA damage or overexpression of p53 upregulates mtCLIC and induces apoptosis. Overexpression of mtCLIC by transient transfection reduces mitochondrial membrane potential, releases cytochrome c into the cytoplasm, activates caspases, and induces apoptosis. mtCLIC is additive with Bax in inducing apoptosis without a physical association of the two proteins. Antisense mtCLIC prevents the increase in mtCLIC levels and reduces apoptosis induced by p53 but not apoptosis induced by Bax, suggesting that the two proapoptotic proteins function through independent pathways. Our studies indicate that mtCLIC, like Bax, Noxa, p53AIP1, and PUMA, participates in a stress-induced death pathway converging on mitochondria and should be considered a target for cancer therapy through genetic or pharmacologic approaches.

scholarly journals The Intracellular Chloride Ion Channel Protein CLIC1 Undergoes a Redox-controlled Structural Transition

2003 ◽  
Vol 279 (10) ◽  
pp. 9298-9305 ◽  
Author(s):  
Dene R. Littler ◽  
Stephen J. Harrop ◽  
W. Douglas Fairlie ◽  
Louise J. Brown ◽  
Greg J. Pankhurst ◽  
...  
Keyword(s):  
Ion Channel ◽  
Structural Transition ◽  
Chloride Ion ◽  
Channel Protein ◽  
Intracellular Chloride

Anion-induced dynamic behavior of apical water channels in vasopressin-sensitive epithelia exposed to mercury

1994 ◽  
Vol 266 (6) ◽  
pp. C1577-C1585 ◽  
Author(s):  
A. Grosso ◽  
P. Jaquet ◽  
P. Brawand ◽  
R. C. De Sousa
Keyword(s):  
Dynamic Behavior ◽  
Water Flow ◽  
Water Permeability ◽  
Water Channels ◽  
Bufo Marinus ◽  
Glutaraldehyde Fixation ◽  
Experimental Conditions ◽  
Anion Effect ◽  
Channel Protein ◽  
Intracellular Chloride

We showed recently that, in toad skins preexposed to Hg, water permeability is high in SO4-Ringer and low in Cl-Ringer. This anion effect was further investigated in Hg-treated skins and bladders of toads (Bufo marinus) in a variety of experimental conditions, including glutaraldehyde fixation and stimulation by vasopressin (VP) or isoproterenol (IP). In fixed bladders either unstimulated or stimulated with VP, net water flow (Jw) in SO4-Ringer [Jw (SO4)] was always significantly higher than Jw in Cl [Jw (Cl)]; the same applies to fixed toad skins, either unstimulated or stimulated with IP. In unfixed isolated toad epidermis challenged with IP before Hg exposure, Jw(SO4)/Jw(Cl) >> 1 approaching the ratio Jw (maximally stimulated)/Jw (basal). Therefore, anion-induced Jw changes were present whether Hg acted on epithelial water channels exocytosed by Hg itself or by hydrosomotic agents and suggest a switching between open and closed configurations of the channel protein. This anion effect was not abolished by glutaraldehyde and might be correlated with changes in intracellular chloride.

scholarly journals Abundance of ClC-1 chloride channel in human skeletal muscle: fiber type specific differences and effect of training

2018 ◽  
Vol 125 (2) ◽  
pp. 470-478 ◽  
Author(s):  
Martin Thomassen ◽  
Morten Hostrup ◽  
Robyn M. Murphy ◽  
Brett A. Cromer ◽  
Casper Skovgaard ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Exercise Performance ◽  
Chloride Channel ◽  
Human Skeletal Muscle ◽  
Fiber Type ◽  
Human Muscle ◽  
Type I ◽  
Maximal Heart Rate ◽  
Channel Protein ◽  
Slow Twitch

Cl− channel protein 1 (ClC-1) may be important for excitability and contractility in skeletal muscle, but ClC-1 abundance has not been examined in human muscle. The aim of the present study was to examine ClC-1 abundance in human skeletal muscle, including fiber type specific differences and the effect of exercise training. A commercially available antibody was tested with positive and negative control tissue, and it recognized specifically ClC-1 in the range from 100 to 150 kDa. Abundance of ClC-1 was 38% higher ( P < 0.01) in fast twitch Type IIa muscle fibers than in slow twitch Type I. Muscle ClC-1 abundance did not change with 4 wk of training consisting of 30 min cycling at 85% of maximal heart rate (HRmax) and 3 × 30-s all out sprints or during a 7-wk training period with 10–12 × 30 s uphill cycling and 4–5 × ~4 min cycling at 90%–95% of HRmax. ClC-1 abundance correlated negatively ( P < 0.01) with maximal oxygen consumption ( r = –0.552) and incremental exercise performance ( r = –0.546). In addition, trained cyclists had lower ( P < 0.01) ClC-1 abundance than lesser trained individuals. The present observations indicate that a low abundance of muscle ClC-1 may be beneficial for exercise performance, but the role of abundance and regulation of ClC-1 in skeletal muscle of humans with respect to exercise performance and trainability need to be elucidated. NEW & NOTEWORTHY Abundance of the Cl− channel protein 1 (ClC-1) chloride channel may be important for excitability and contractility in human skeletal muscle and may therefore have implications for fatigue development. In this study, we confirmed ClC-1 specificity for a commercially available antibody, and this study is first to our knowledge to determine ClC-1 protein abundance in human muscle by Western blotting. We observed that abundance of ClC-1 was higher in fast compared with slow twitch fibers and lower in trained individuals than in recreationally active.

scholarly journals Subcellular distribution and targeting of the intracellular chloride channel p64.

1997 ◽  
Vol 8 (4) ◽  
pp. 691-704 ◽  
Author(s):  
C Redhead ◽  
S K Sullivan ◽  
C Koseki ◽  
K Fujiwara ◽  
J C Edwards
Keyword(s):  
Chloride Channel ◽  
Subcellular Distribution ◽  
Cell Type ◽  
Electron Microscopic ◽  
Intracellular Chloride ◽  
Terminal Domain ◽  
Electron Microscopic Technique ◽  
Membrane Compartment ◽  
A Cell ◽  
Kidney Microsomes

p64 is an intracellular chloride channel originally identified in bovine kidney microsomes. Using a combination of immunofluorescent and electron microscopic technique, we demonstrate that p64 resides in the limiting membranes of perinuclear dense core vesicles which appear to be regulated secretory vesicles. Heterologous expression of p64 in PancI cells, a cell type which does not normally express p64, results in targeting to a similar compartment. Mutagenesis experiments demonstrate that both the N- and C-terminal domains of the protein independently contribute to subcellular distribution of the protein. The C-terminal domain functions to prevent expression of p64 on the plasma membrane and the N-terminal domain is necessary to deliver p64 to the appropriate membrane compartment.

scholarly journals Intracellular Chloride Ion Channel Protein-1 Expression in Clear Cell Renal Cell Carcinoma

2019 ◽  
Vol 16 (4) ◽  
pp. 299-307 ◽  
Author(s):  
ALEXANDRU NESIU ◽  
ANCA MARIA CIMPEAN ◽  
RALUCA AMALIA CEAUSU ◽  
AHMED ADILE ◽  
IOAN IOIART ◽  
...  
Keyword(s):  
Renal Cell Carcinoma ◽  
Ion Channel ◽  
Cell Carcinoma ◽  
Renal Cell ◽  
Clear Cell ◽  
Chloride Ion ◽  
Cell Renal Cell Carcinoma ◽  
Channel Protein ◽  
Intracellular Chloride
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