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Ion Channels in Immune Cells
Published in Shyam S. Bansal, Immune Cells, Inflammation, and Cardiovascular Diseases, 2022
Devasena Ponnalagu, Shridhar Sanghvi, Shyam S. Bansal, Harpreet Singh
Even intracellular ion channels localized to mitochondria and other organelles have been established to contribute to immune cell activation by regulating key cellular signaling pathways, including mitochondrial pathways, as summarized in a recent review1. A family of anion channel proteins called chloride intracellular channel (CLIC) proteins has been identified in the mitochondria of cardiomyocytes, in which these proteins were shown to be important in maintaining cardiac mitochondrial physiology117. Their function is also implicated in macrophage activation and the formation of inflammasome complex118–120. CLICs contain glutathione S-transferase (GST) omega fold and are therefore classified under the GST super-family of proteins121–124. CLICs are an evolutionarily conserved unique class of ion channel proteins that can exist in both soluble and integral membrane forms123–126. There are six main paralogs of CLIC proteins that are identified in mammals. They are referred to as CLIC1–CLIC6127–135. Some of the CLICs, such as CLIC5 and CLIC6, also seem to exhibit splice variation126. Other than mammals, CLIC orthologs are also observed in plants136, invertebrates137,138, and prokaryotes139, in which they have been shown to exhibit channel-like activity139,140. Similar to GST, some of the CLIC members, CLIC1, CLIC2, and CLIC4, exhibit glutaredoxin-like activity122. CLICs, through either their channel activity or other regulatory mechanisms, have been demonstrated to play a role in many of the physiological and pathophysiological processes125,141.
Chloride intracellular channel protein 2 in cancer and non-cancer human tissues: relationship with tight junctions
Published in Tissue Barriers, 2019
Yoshitomo Ueno, Saya Ozaki, Akihiro Umakoshi, Hajime Yano, Mohammed E. Choudhury, Naoki Abe, Yutaro Sumida, Jun Kuwabara, Rina Uchida, Afsana Islam, Kohei Ogawa, Kei Ishimaru, Toshihiro Yorozuya, Takeharu Kunieda, Yuji Watanabe, Yasutsugu Takada, Junya Tanaka
CLIC2 is the least investigated subtype among the CLIC family members. Its known physiological function may be the modulation of ryanodine receptor activities to regulate Ca2+-mediated intracellular signaling in skeletal and cardiac muscles18,19 CLIC2 may form chloride ion channels in vitro when it is inserted into an artificial lipid bilayer7 Compared with the localization of CD31 or PECAM, a transmembrane protein belonging to the immunoglobulin superfamily,20 CLIC2 was distributed in the cytoplasm and not as a transmembrane protein as described previously,21 suggesting that CLIC2 does not function as a chloride channel in the plasma membrane.