Annexin 6 modulates the maxi-chloride channel of the apical membrane of syncytiotrophoblast isolated from human placenta

RIQUELME, G; Llanos P.; Tischner, E; Neil, J; Campos, BA

Abstract

The syncytiotrophoblast separates the maternal and fetal blood and constitutes the primary barrier for maternal-fetal transport. The Maxi-chloride channel from the apical membrane of the syncytiotrophoblast plays a role in the chloride conductance. Annexins can play an important role in the regulation of membrane events. In this study we evaluate the role of annexin 6 in the Maxichloride channel properties. The results showed that annexin 6 is bound in the apical placenta membranes in a calcium-dependent phospholipid-binding manner but also in a calcium-independent fashion. The neutralization of annexin 6 decreased the total current by 39 ± 1.9% in the range of ± 80 mV, and the currents decrease with the time. The single-channel slope conductance was decreased from 253 ± 7.4 pS (control) to 105 ± 13 pS, and the amplitude decreased by 50%. The open probability was also affected when higher voltage steps were used, changes in either the positive or negative direction induced the channel to close, and the open probability (Po) did not decrease. In channels with neutralized annexin 6, it was maintained at 1 at ±40mV and at ±80 mV. These results suggest that endogenous annexin 6 could regulate the Maxi-chloride channel. The results obtained with normal placentae, in which annexin 6 was neutralized, are similar to those described for the Maxichloride channel isolated from pre-eclamptic placenta. Together these data suggest that annexin 6 could play an important role in ion transport of the placenta.

Más información

Título según WOS: Annexin 6 modulates the maxi-chloride channel of the apical membrane of syncytiotrophoblast isolated from human placenta
Título según SCOPUS: Annexin 6 modulates the maxi-chloride channel of the apical membrane of syncytiotrophoblast isolated from human placenta
Título de la Revista: JOURNAL OF BIOLOGICAL CHEMISTRY
Volumen: 279
Número: 48
Editorial: Elsevier
Fecha de publicación: 2004
Página de inicio: 50601
Página final: 50608
Idioma: English
URL: http://www.jbc.org/cgi/doi/10.1074/jbc.M407859200
DOI:

10.1074/jbc.M407859200

Notas: ISI, SCOPUS