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XB-ART-19023
FEBS Lett 1995 Nov 13;3751-2:56-62.
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Molecular cloning and characterization of a novel truncated from (ClC-2 beta) of ClC-2 alpha (ClC-2G) in rabbit heart.

Furukawa T , Horikawa S , Terai T , Ogura T , Katayama Y , Hiraoka M .


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Two cDNAs encoding rabbit heart Cl- channels (rabClC-2 beta and rabClC-2 alpha) were isolated by a PCR cloning strategy. RabClC-2 beta is a novel cDNA consisting of 2998 bp and encoding the 822-amino acid protein, while rabClC-2 alpha is identical to previously reported ClC-2G. RabClC-2 beta is 68 amino acids truncated from NH2-terminus of rabClC-2 alpha, but all 13 putative hydrophobic domains are conserved in rabClC-2 beta. Although rabClC-2 alpha was suggested to be activated by extracellular hypotonicity, expression of rabClC-2 beta in Xenopus oocytes induced large Cl- currents even in the absence of extracellular hypotonicity. Induction of external hypotonicity did not further increase the amplitude of membrane currents. On the other hand, as similar to rabClC-2 alpha, rabClC-2 beta current was augmented by PKA activation. Thus, different RNA processing of the same gene appears to provide two highly homologous PKA-activated Cl- channels with or without responsiveness to cell swelling in rabbit heart.

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Species referenced: Xenopus laevis
Genes referenced: clcn2