http://www.cnr.it/ontology/cnr/individuo/prodotto/ID286795
I-J loop involvement in the pharmacological profile of CLC-K channels expressed in Xenopus oocytes (Articolo in rivista)
- Type
- Label
- I-J loop involvement in the pharmacological profile of CLC-K channels expressed in Xenopus oocytes (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bbamem.2014.07.021 (literal)
- Alternative label
Gradogna, Antonella; Imbrici, Paola; Zifarelli, Giovanni; Liantonio, Antpnella; Camerino, Diana Conte; Pusch, Michael (2014)
I-J loop involvement in the pharmacological profile of CLC-K channels expressed in Xenopus oocytes
in Biochimica et biophysica acta. Biomembranes
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Gradogna, Antonella; Imbrici, Paola; Zifarelli, Giovanni; Liantonio, Antpnella; Camerino, Diana Conte; Pusch, Michael (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Consiglio Nazionale delle Ricerche (CNR); University of Bari (literal)
- Titolo
- I-J loop involvement in the pharmacological profile of CLC-K channels expressed in Xenopus oocytes (literal)
- Abstract
- CLC-K chloride channels and their subunit, barttin, are crucial for renal NaCl reabsorption and for inner ear endolymph production. Mutations in CLC-Kb and barttin cause Bartter syndrome. Here, we identified two adjacent residues, F256 and N257, that when mutated hugely alter in Xenopus oocytes CLC-Ka's biphasic response to niflumic acid, a drug belonging to the fenamate class, with F256A being potentiated 37-fold and N257A being potently blocked with a KD similar to 1 mu M. These residues are localized in the same extracellular I-J loop which harbors a regulatory Ca2+ binding site. This loop thus can represent an ideal and CLC-K specific target for extracellular ligands able to modulate channel activity. Furthermore, we demonstrated the involvement of the barttin subunit in the NFA potentiation. Indeed the F256A mutation confers onto CLC-K1 a transient potentiation induced by NFA which is found only when CLC-K1/F256A is co-expressed with barttin. Thus, in addition to the role of barttin in targeting and gating, the subunit participates in the pharmacological modulation of CLC-K channels and thus represents a further target for potential drugs. (C) 2014 The Authors. Published by Elsevier B.V. (literal)
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