chloride channel

Members of the CLIC family are largely soluble proteins that possess the intriguing property of spontaneous insertion into phospholipid bilayers to form integral membrane ion channels. Chloride intracellular channel 1 (CLIC1), a newly discovered member of the chloride channel protein family, has been implicated in multiple human cancers. CLIC1 is a Chloride Intracellular Ion Channel protein that exists either in a soluble state in the cytoplasm or as a membrane bound protein. CLIC1 acts as a putative oncogene in pancreatic cancer and may represent a novel diagnostic and therapeutic target for pancreatic cancer. Intracellular chloride channel protein 1 (CLIC1) participates in inflammatory processes by regulating macrophage phagosomal functions such as pH and proteolysis. CLIC1 is a novel therapeutic target to help reduce the adaptive immune response in autoimmune diseases. The expression of CLIC1 might be closely related to the carcinogenesis, clinical biological behaviors, and prognosis of pancreatic ductal adenocarcinomas. Intracellular chloride channel 1 (CLIC1), a novel metamorphic protein, acts as a sensor of cell oxidation and is involved in inflammation.

Chloride Intracellular Channel Protein 2 (CLIC2) is a critical component of all living cells; it regulatescellular traffic of Chloride ion and it can be inserted into membranes anf form chloride ion channels. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions, channel activity depends on the pH. CLIC2 is involved in regulating membrane potential and organic solute transport. CLIC2 modulates the activity of RYR2 and inhibits Calcium influx. CLIC2 can be detected in the adult brain, liver, lung, heart, stomach, spleen and testis. It is expressed in fetal liver and adult skeletal muscle. CLIC2 is a potential candidate for one of many diseases linked to Xq28.

Chloride Intracellular Channel Protein 5 (CLIC5) is a single-pass membrane protein which belongs to the chloride channel CLIC family. It contains one GST C-terminal domain. Chloride intracellular channels are involved in chloride ion transport within various subcellular compartments. CLIC5 can insert into membranes and form selective ion channels regulated by actin that may transport chloride ions. It may play a role in the regulation of transepithelial ion absorption and secretion. CLIC5 specifically associates with the cytoskeleton of placenta microvilli. CLIC5 is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture.

Chloride intracellular channel protein 4, also known as Intracellular chloride ion channel protein p64H1 and CLIC4, is a member of the chloride channel CLIC family. It contains oneGST C-terminal domain. CLIC4 is a member of a family of intracellular chloride channels. It is regulated by p53, c-Myc, and tumor necrosis factor-alpha. CLIC4 is detected in epithelial cells from colon, esophagus and kidney (at protein level). CLIC4 has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. CLIC4 could promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis). Expression of CLIC4 is prominent in heart, kidney, placenta and skeletal muscle. Overexpression of CLIC4 in cancer cells inhibits tumor growth. Conversely, overexpression of CLIC4 in tumor stromal cells stimulates tumor growth. Thus, CLIC4 participates in normal and pathological processes and may serve as a useful target for therapies in disturbances of homeostasis and neoplastic transformation. Loss of CLIC4 in tumor cells and gain in tumor stroma is common to many human cancers and marks malignant progression. Up-regulation of CLIC4 in tumor stroma is coincident with myofibroblast conversion, generally a poor prognostic indicator. Reactivation and restoration of CLIC4 in tumor cells or the converse in tumor stromal cells could provide a novel approach to inhibit tumor growth.

Chloride intracellular channel protein 3 (CLIC3) is encoded by the CLIC3 gene. CLIC3 is a single-pass membrane protein which belongs to the chloride channel CLIC family. It contains one GST C-terminal domain and one GST N-terminal domain. Chloride intracellular channel protein 3 high expressed in the placental, lung and heart, low expressed in skeletal muscle, kidney and pancreas. Chloride intracellular channel protein 3 can insert into membranes and forms chloride ion channels, may participate in cellular growth control.

CLNS1A Protein, Rabbit, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 33.4 kDa and the accession number is Q28678.

GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. In the uterus, the function of the receptor appears to be related to tissue contractility. The binding of this pI subunit with other GABA(A) receptor subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone. GABRP Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 28.9 kDa and the accession number is O00591.

STX8, also known as syntaxin 8, directly interacts with HECTd3. STX8 forms the SNARE complex with syntaxin 7, vti1b and endobrevin. STX8 belongs to the syntaxin family. Members of this family are key molecules implicated in diverse vesicle docking and membrane fusion events. STX8 physically interacts with cystic fibrosis transmembrane conductance regulator (CFTR): recombinant syntaxin 8 binds CFTR in vitro and both proteins co-immunoprecipitate in HT29 cells. Syntaxin 8 regulates CFTR-mediated currents in chinese hamster ovary (CHO) cells stably expressing CFTR and syntaxin 8. STX8 contributes to the regulation of CFTR trafficking and chloride channel activity by the SNARE machinery.

Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Channel opening is also triggered by taurine and beta-alanine. Channel characteristics depend on the subunit composition; heteropentameric channels are activated by lower glycine levels and display faster desensitization. Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents. Channel activity is potentiated by ethanol. Potentiation of channel activity by intoxicating levels of ethanol contribute to the sedative effects of ethanol.