Proteoliposomes reconstituted with human aquaporin-1 reveal novel single-ion-channel properties.
Journal
Biophysical reports
ISSN: 2667-0747
Titre abrégé: Biophys Rep (N Y)
Pays: United States
ID NLM: 9918266001106676
Informations de publication
Date de publication:
08 Mar 2023
08 Mar 2023
Historique:
received:
04
09
2022
accepted:
11
01
2023
entrez:
23
3
2023
pubmed:
24
3
2023
medline:
24
3
2023
Statut:
epublish
Résumé
Human aquaporin 1 (hAQP1) forms homotetrameric channels that facilitate fluxes of water and small solutes across cell membranes. In addition to water channel activity, hAQP1 displays non-selective monovalent cation-channel activity gated by intracellular cyclic GMP. Dual water and ion-channel activity of hAQP1, thought to regulate cell shape and volume, could offer a target for novel therapeutics relevant to controlling cancer cell invasiveness. This study probed properties of hAQP1 ion channels using proteoliposomes, which, unlike conventional cell-based systems such as
Identifiants
pubmed: 36949749
doi: 10.1016/j.bpr.2023.100100
pii: S2667-0747(23)00001-0
pmc: PMC10025285
doi:
Types de publication
Journal Article
Langues
eng
Pagination
100100Informations de copyright
© 2023 The Author(s).
Déclaration de conflit d'intérêts
The authors declare no competing interests.
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