Molecular and electrophysiological characterization of nucleotide-sensitive chloride current-inducing protein of Fasciola hepatica
- Authors
- Park, JB; Son, SJ; Lee, GS; Cho, PY; Song, KS; Ryu, PD; Kang, SY; Hong, SJ
- Issue Date
- Apr-2005
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- Fasciola hepatica; chloride current-inducing protein; nucleotide-sensitive; outward rectifier
- Citation
- MOLECULAR AND BIOCHEMICAL PARASITOLOGY, v.140, no.2, pp 197 - 203
- Pages
- 7
- Journal Title
- MOLECULAR AND BIOCHEMICAL PARASITOLOGY
- Volume
- 140
- Number
- 2
- Start Page
- 197
- End Page
- 203
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/24633
- DOI
- 10.1016/j.molbiopara.2005.01.004
- ISSN
- 0166-6851
1872-9428
- 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 (ICln-Fh). The recombinant ICln-Fh protein, however, did not trigger cell swelling-induced Cl- currents (ICl-swell). The ICln-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. (c) 2005 Elsevier B.V. All rights reserved.
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