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XB-ART-2190
Mol Biochem Parasitol. April 1, 2005; 140 (2): 197-203.

Molecular and electrophysiological characterization of nucleotide-sensitive chloride current-inducing protein of Fasciola hepatica.

Park JB , Son SJ , Lee GS , Cho PY , Song KS , Ryu PD , Kang SY , Hong SJ .


Abstract
Nucleotide-sensitive chloride current regulating proteins (ICln''s) of the chloride channels have been characterized from man and animals. An ICln of Fasciola hepatica (ICln-Fh) consisting of 231 amino acids revealed high similarities to both consensus domain of ICln''s and two acidic residue-abundant patches in its C-terminus. Native ICln-Fh protein was confirmed present in F. hepatica soluble extract by immunoblotting. The recombinant ICln-Fh protein expressed in collagenase-defolliculated Xenopus oocytes induced fast rising and outward rectifying Cl- currents (I(Cln-Fh)). The recombinant ICln-Fh protein, however, did not trigger cell swelling-induced Cl- currents (I(Cl-swell)). The I(Cln-Fh) currents were significantly reduced by substituting external Cl- with gluconic acid and by externally adding cAMP. Collectively, these results suggest that ICln-Fh protein is an inducer of Cl- currents in F. hepatica.

PubMed ID: 15760659
Article link: Mol Biochem Parasitol.

Genes referenced: clns1a
Antibodies referenced:
Morpholinos referenced:

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