dc.creator | Cano Rodríguez, María Mercedes | es |
dc.creator | Calonge Castrillo, María Luisa | es |
dc.creator | Ilundáin Larrañeta, María Anunciación Ana | es |
dc.date.accessioned | 2020-04-24T15:13:27Z | |
dc.date.available | 2020-04-24T15:13:27Z | |
dc.date.issued | 2015 | |
dc.identifier.citation | Cano Rodríguez, M.M., Calonge Castrillo, M.L. y Ilundáin Larrañeta, M.A.A. (2015). Na+-dependent and Na+-independent betaine transport across the apical membrane of rat renal epithelium. Biochimica et Biophysica Acta - Biomembranes, 1848 (10), 2172-2179. | |
dc.identifier.issn | 0005-2736 | es |
dc.identifier.issn | 1879-2642 | es |
dc.identifier.uri | https://hdl.handle.net/11441/95722 | |
dc.description.abstract | The low renal excretion of betaine indicates that the kidney efficiently reabsorbs the betaine filtered by the glomeruli but the mechanisms involved in such a process have been scarcely investigated. We have detected concentrative and non-concentrative betaine transport activity in brush-border membrane vesicles (BBMV) from rat renal cortex and medulla. The concentrative system is the Sodium/Imino-acid Transporter 1 (SIT1) because it is Na+- and Cl--dependent, electrogenic and is inhibited by an anti-SIT1 antibody. Its apparent affinity constant for betaine, Kt, is 1.1 ± 0.5 mM and its maximal transport velocity, Vmax, 0.5 ± 0.1 nmol betaine/mg protein/s. Inhibitors of the Na+/Cl-/betaine uptake are l-proline (75%) and cold betaine, l-carnitine and choline (40-60%). Neither creatine, TEA, taurine, β-alanine, GABA nor glycine significantly inhibited Na+/Cl-/betaine uptake. The non-concentrative betaine transport system is Na+- and H+-independent, electroneutral, with a Kt for betaine of 47 ± 7 μM and a Vmax of 7.8 ± 1 pmol betaine/mg protein/s. Its transport activity is nearly abolished by betaine, followed by L-carnitine (70-80%) and proline (40-50%), but a difference from the Na+/Cl-/betaine transport is that it is inhibited by TEA (approx. 50%) and unaffected by choline. The underlying carrier functions as an antiporter linking betaine entry into the BBMV with the efflux of either l-carnitine or betaine, an exchange unaffected by the anti-SIT1 antibody. As far as we know this is the first work reporting that betaine crosses the apical membrane of rat renal epithelium by SIT1 and by a Na+- and H+-independent transport system. | es |
dc.description.sponsorship | Ministerio de Ciencia y Tecnología BFI2003-00222 | es |
dc.description.sponsorship | Junta de Andalucía 2010/BIO-144 | es |
dc.format | application/pdf | es |
dc.format.extent | 8 p. | es |
dc.language.iso | eng | es |
dc.publisher | Elsevier | es |
dc.relation.ispartof | Biochimica et Biophysica Acta - Biomembranes, 1848 (10), 2172-2179. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Betaine | es |
dc.subject | Brush-border membrane vesicles | es |
dc.subject | Kidney | es |
dc.subject | Transport | es |
dc.title | Na+-dependent and Na+-independent betaine transport across the apical membrane of rat renal epithelium | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Fisiología | es |
dc.relation.projectID | BFI2003-00222 | es |
dc.relation.projectID | 2010/BIO-144 | es |
dc.relation.publisherversion | http://dx.doi.org/10.1016/j.bbamem.2015.05.020 | es |
dc.identifier.doi | 10.1016/j.bbamem.2015.05.020 | es |
dc.journaltitle | Biochimica et Biophysica Acta - Biomembranes | es |
dc.publication.volumen | 1848 | es |
dc.publication.issue | 10 | es |
dc.publication.initialPage | 2172 | es |
dc.publication.endPage | 2179 | es |