Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9140050 | Molecular and Biochemical Parasitology | 2005 | 7 Pages |
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 Clâ currents (ICln-Fh). The recombinant ICln-Fh protein, however, did not trigger cell swelling-induced Clâ currents (ICl-swell). The ICln-Fh currents were significantly reduced by substituting external Clâ with gluconic acid and by externally adding cAMP. Collectively, these results suggest that ICln-Fh protein is an inducer of Clâ currents in F. hepatica.
Keywords
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Molecular Biology
Authors
Jin Bong Park, Sook Jin Son, Gyu Seung Lee, Pyo Yun Cho, Ky Sun Song, Pan Dong Ryu, Shin-Yong Kang, Sung-Jong Hong,