Aquaporin-11 containing a divergent NPA motif has normal water channel activity.
Biochim Biophys Acta
; 1768(3): 688-93, 2007 Mar.
Article
em En
| MEDLINE
| ID: mdl-17178102
ABSTRACT
Recently, two novel mammalian aquaporins (AQPs), AQPs 11 and 12, have been identified and classified as members of a new AQP subfamily, the "subcellular AQPs". In members of this subfamily one of the two asparagine-proline-alanine (NPA) motifs, which play a crucial role in selective water conduction, are not completely conserved. Mouse AQP11 (mAQP11) was expressed in Sf9 cells and purified using the detergent Fos-choline 10. The protein was reconstituted into liposomes, which were used for water conduction studies with a stopped-flow device. Single water permeability (pf) of AQP11 was measured to be 1.72+/-0.03x10(-13) cm(3)/s, suggesting that other members of the subfamily with incompletely conserved NPA motifs may also function as water channels.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Asparagina
/
Prolina
/
Água
/
Aquaporinas
/
Alanina
Limite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
2007
Tipo de documento:
Article