| pubmed-article:17002286 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17002286 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:17002286 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:17002286 | lifeskim:mentions | umls-concept:C1621574 | lld:lifeskim |
| pubmed-article:17002286 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:17002286 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
| pubmed-article:17002286 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
| pubmed-article:17002286 | lifeskim:mentions | umls-concept:C2827421 | lld:lifeskim |
| pubmed-article:17002286 | pubmed:issue | 39 | lld:pubmed |
| pubmed-article:17002286 | pubmed:dateCreated | 2006-9-27 | lld:pubmed |
| pubmed-article:17002286 | pubmed:abstractText | Spliced isoforms of the Na+/Ca2+ exchanger, NCLX, truncated at the alpha-repeat region have been identified. The activity and functional organization of such proteins are, however, poorly understood. In the present work, we have studied Na+/Ca2+ exchange mediated by single alpha-repeat constructs (alpha1 and alpha2) of NCLX. Sodium-dependent calcium transport was fluorescently detected in both the reversal and forward modes; calcium-dependent outward currents were also recorded using a whole cell patch configuration in HEK293 cells heterologously expressing either the alpha1 or alpha2 single-domain proteins. In contrast, calcium transport and reversal currents were not detected when cells were transfected with a vector or with an alpha2 mutant (alpha2-S273T). Thus, our data indicate that the single alpha-domain constructs mediate electrogenic Na+/Ca2+ exchange. The alpha1 domain, but not the alpha2, exhibited partial sensitivity to the NCX inhibitor, KB-R7943, while Li+-dependent Ca2+ efflux was detected in cells expressing either the alpha1 or alpha2 construct. The functional organization of the single alpha-domain constructs was assessed using a dominant-negative approach. Coexpression of the alpha1 or alpha2 constructs with the nonfunctional alpha2-S273T mutant had a synergistic inhibitory effect on Na+/Ca2+ transport. Dose-dependence analysis of the inhibition of alpha2 construct activity by the alpha2-S273T mutant indicated that the functional unit is either a dimer or a trimer. Immunoprecipitation analysis indicated that the alpha2 construct indeed interacts with the alpha2-S273T mutant. Taken together, our data indicate that although single alpha1 or alpha2 domain constructs are independently capable of Na+/Ca2+ exchange, oligomerization is required for their activity. Such organization may give rise to transport activity with distinct kinetic parameters and physiological roles. | lld:pubmed |
| pubmed-article:17002286 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17002286 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17002286 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17002286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17002286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17002286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17002286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17002286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17002286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17002286 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17002286 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17002286 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17002286 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:17002286 | pubmed:author | pubmed-author:SaarDroritD | lld:pubmed |
| pubmed-article:17002286 | pubmed:author | pubmed-author:GrossmanYoram... | lld:pubmed |
| pubmed-article:17002286 | pubmed:author | pubmed-author:SeklerIsraelI | lld:pubmed |
| pubmed-article:17002286 | pubmed:author | pubmed-author:HershfinkelMi... | lld:pubmed |
| pubmed-article:17002286 | pubmed:author | pubmed-author:PeretzAsherA | lld:pubmed |
| pubmed-article:17002286 | pubmed:author | pubmed-author:KhananshviliD... | lld:pubmed |
| pubmed-article:17002286 | pubmed:author | pubmed-author:PaltyRazR | lld:pubmed |
| pubmed-article:17002286 | pubmed:author | pubmed-author:YagevOrenO | lld:pubmed |
| pubmed-article:17002286 | pubmed:author | pubmed-author:BarkalifaRoni... | lld:pubmed |
| pubmed-article:17002286 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17002286 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:17002286 | pubmed:volume | 45 | lld:pubmed |
| pubmed-article:17002286 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17002286 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17002286 | pubmed:pagination | 11856-66 | lld:pubmed |
| pubmed-article:17002286 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:17002286 | pubmed:meshHeading | pubmed-meshheading:17002286... | lld:pubmed |
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| pubmed-article:17002286 | pubmed:meshHeading | pubmed-meshheading:17002286... | lld:pubmed |
| pubmed-article:17002286 | pubmed:meshHeading | pubmed-meshheading:17002286... | lld:pubmed |
| pubmed-article:17002286 | pubmed:meshHeading | pubmed-meshheading:17002286... | lld:pubmed |
| pubmed-article:17002286 | pubmed:meshHeading | pubmed-meshheading:17002286... | lld:pubmed |
| pubmed-article:17002286 | pubmed:meshHeading | pubmed-meshheading:17002286... | lld:pubmed |
| pubmed-article:17002286 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17002286 | pubmed:articleTitle | Single alpha-domain constructs of the Na+/Ca2+ exchanger, NCLX, oligomerize to form a functional exchanger. | lld:pubmed |
| pubmed-article:17002286 | pubmed:affiliation | Department of Physiology, Zlotowski Center for Neuroscience, Faculty of Health Sciences, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel. | lld:pubmed |
| pubmed-article:17002286 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17002286 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17002286 | lld:pubmed |
