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Blood, 15 September 2007, Vol. 110, No. 6, pp. 2158-2165. Prepublished online as a Blood First Edition Paper on June 6, 2007; DOI 10.1182/blood-2006-12-063420. This Article Full Text (PDF) Supplemental Figures All Versions of this Article: blood-2006-12-063420v1 110/6/2158    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Guizouarn, H. Articles by Borgese, F. Search for Related Content PubMed PubMed Citation Articles by Guizouarn, H. Articles by Borgese, F. Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted December 21, 2006 Accepted May 16, 2007 Point mutations involved in red cell stomatocytosis convert the electroneutral anion exchanger 1 to a non-selective cation conductance Helene Guizouarn*, Sonia Martial, Nicole Gabillat, and Franck Borgese Laboratoire de physiologie cellulaire et moleculaire, UMR6548, CNRS-Universite de Nice, Nice, France * Corresponding author; email: helene.guizouarn{at}unice.fr. The anion exchanger 1, AE1, is encoded by the SLC4A1 gene and catalyses the electroneutral anion exchange across cell plasma membrane. It is the most abundant transmembrane protein expressed in red cell where it is involved in CO2 transport. Recently, four new point mutations of SLC4A1 gene have been described leading to missense mutations in the protein sequence (L687P, D705Y, S731P or H734R). These point mutations were associated to hemolytic anemia and it was shown that they confer a cation transport feature to the human AE1. Facing this unexpected property for an electroneutral anion exchanger we have studied the transport features of mutated hAE1 by expression in xenopus oocytes. Our results show that the point mutations of hAE1 convert the electroneutral anion exchanger to a cation conductance : the exchangers are no longer able to exchange Cl- and HCO3- whereas they transport Na+ and K+ through a conductive mechanism. These data shed new light on transport mechanisms showing the tiny difference, in terms of primary sequence, between an electroneutral exchange and a conductive pathway. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. Iolascon, L. De Falco, F. Borgese, M. R. Esposito, R. A. Avvisati, P. Izzo, C. Piscopo, H. Guizouarn, A. Biondani, A. Pantaleo, et al. A novel erythroid anion exchange variant (Gly796Arg) of hereditary stomatocytosis associated with dyserythropoiesis Haematologica, August 1, 2009; 94(8): 1049 - 1059. [Abstract] [Full Text] [PDF] S. L. Alper Molecular physiology and genetics of Na+-independent SLC4 anion exchangers J. Exp. Biol., June 1, 2009; 212(11): 1672 - 1683. [Abstract] [Full Text] [PDF] J.C Ellory, H Guizouarn, F Borgese, L.J Bruce, R.J Wilkins, and G.W Stewart Leaky Cl--HCO3- exchangers: cation fluxes via modified AE1 Phil Trans R Soc B, January 27, 2009; 364(1514): 189 - 194. [Abstract] [Full Text] [PDF] S. Walsh, F. Borgese, N. Gabillat, R. Unwin, and H. Guizouarn Cation transport activity of anion exchanger 1 mutations found in inherited distal renal tubular acidosis Am J Physiol Renal Physiol, August 1, 2008; 295(2): F343 - F350. [Abstract] [Full Text] [PDF]

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