Am J Physiol Cell Physiol AJP: Gastrointestinal and Liver Physiology
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Am J Physiol Cell Physiol 277: C948-C954, 1999;
0363-6143/99 $5.00
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Vol. 277, Issue 5, C948-C954, November 1999

Identification of an acid-activated Clminus channel from human skeletal muscles

Masanobu Kawasaki, Toshiko Fukuma, Kazushi Yamauchi, Hisato Sakamoto, Fumiaki Marumo, and Sei Sasaki

Second Department of Internal Medicine, Tokyo Medical and Dental University, Tokyo 113-8519, Japan

ClC-4 gene was isolated as a putative Cl- channel. Due to a lack of functional expression of ClC-4, its physiological role remains unknown. We isolated a human ClC-4 clone (hClC-4sk) from human skeletal muscles and stably transfected it to Chinese hamster ovary cells. Whole cell patch-clamp studies showed that the hClC-4sk channel was activated by external acidic pH and inhibited by DIDS. It passed a strong outward Cl- current with a permeability sequence of I- > Cl- > F-. The hClC-4sk has consensus sites for phosphorylation by protein kinase A (PKA); however, stimulation of PKA had no effect on the currents. hClC-4sk mRNA was expressed in excitable tissues, such as heart, brain, and skeletal muscle. These functional characteristics of hClC-4sk provide a clue to its physiological role in excitable cells.

human ClC-4sk; ClCN4; outwardly rectifying chloride channel; acidification


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