{"id":98436,"date":"2018-03-11T10:19:12","date_gmt":"2018-03-11T10:19:12","guid":{"rendered":"https:\/\/www.deberes.net\/tesis\/sin-categoria\/caracterizacion-de-los-transportadores-mitocondriales-de-atp-mg-pi-y-su-implicacion-en-la-senalizacion-por-calcio-a-la-mitocondria\/"},"modified":"2018-03-11T10:19:12","modified_gmt":"2018-03-11T10:19:12","slug":"caracterizacion-de-los-transportadores-mitocondriales-de-atp-mg-pi-y-su-implicacion-en-la-senalizacion-por-calcio-a-la-mitocondria","status":"publish","type":"post","link":"https:\/\/www.deberes.net\/tesis\/biologia-molecular\/caracterizacion-de-los-transportadores-mitocondriales-de-atp-mg-pi-y-su-implicacion-en-la-senalizacion-por-calcio-a-la-mitocondria\/","title":{"rendered":"Caracterizacion de los transportadores mitocondriales de atp-mg\/pi y su implicacion en la se\u00f1alizacion por calcio a la mitocondria"},"content":{"rendered":"<h2>Tesis doctoral de <strong> Javier Traba Dominguez <\/strong><\/h2>\n<p>The transport of metabolites across the inner mitocondrial membrane is carried out by a  familiy of proteins called mitocondrial carriers (mc). Studies in our laboratory led to the  identification of a novel subfamily of mitochondrial carriers, the scamcs (short calciumbinding mitochondrial carriers), with at least four paralogues in mammals (scamc- 1\/slc25a24, scamc-2\/slc25a25, scamc-3\/slc25a23 and scamc-3like\/slc25a41) and  only one in the yeast saccharomyces cerevisiae (sal1). Most scamcs are characterized by, in  addition to the mc domain, an n-terminal domain which harbours calcium binding motifs that  face the intermembrane space. Thus, the activity of these proteins could be regulated by  extramitochondrial calcium.  scamcs correspond to isoforms of the atp-mg\/pi carrier, whose transport activity was  functionally identified 20 years ago, and catalyze the net transport of adenine nucleotides across  the inner mitochondrial membrane. They mediate a reversible electroneutral exchange between  atp-mg2- and hp042-. The atp-mg\/pi carrier regulates the matrix adenine nucleotide content,  contributing to the regulation of mitochondrial activities dependent on adenine nucleotides such  as gluconeogesis, urea synthesis, mitochondrial biogenesis or permeability transition pore  opening.   we have studied the transport activity, calcium regulation and function of the scamcs in  three different models: yeast mitochondria, where sal1p is the only scamc present; mouse  liver and brain mitochondria, where scamc-3 is the main paralogue; and cell lines  mitochondria, where scamc-1 is the main paralogue.   the yeast atp-mg\/pi carrier is activated by calcium with a s0.5 of 15.0 \u00c2\u00bfm, and is recruited  as a ca2+-dependent mechanism to import atp-mg from the citosol upon glucose addition to  nutrient starved yeast, and is also involved in atp-mg uptake from the cytosol in yeast growing  exponentially in glucose, a condition in which yeast mitochondria are atp consumers.  scamc-1 and scamc-3 in mammals are activated by calcium with a s0.5 of 12.7 and 3.4  \u00c2\u00bfm, respectively. They are involved in the regulation of the calcium retention capacity, by  regulating the matrix free calcium concentration, and thus they regulate the permeability  transition pore (ptp), a non-specific pore that is formed in the inner mitochondrial membrane  under conditions of calcium overload and\/or oxidative stress, which has been implicated in cell  death by necrosis, for example in situations of ischemia-reperfusion. These findings have led us  to propose a new model for the regulation of the calcium retention capacity and ptp opening in  mitochondria.<\/p>\n<p>&nbsp;<\/p>\n<h3>Datos acad\u00e9micos de la tesis doctoral \u00ab<strong>Caracterizacion de los transportadores mitocondriales de atp-mg\/pi y su implicacion en la se\u00f1alizacion por calcio a la mitocondria<\/strong>\u00ab<\/h3>\n<ul>\n<li><strong>T\u00edtulo de la tesis:<\/strong>\u00a0 Caracterizacion de los transportadores mitocondriales de atp-mg\/pi y su implicacion en la se\u00f1alizacion por calcio a la mitocondria <\/li>\n<li><strong>Autor:<\/strong>\u00a0 Javier Traba Dominguez <\/li>\n<li><strong>Universidad:<\/strong>\u00a0 Aut\u00f3noma de Madrid<\/li>\n<li><strong>Fecha de lectura de la tesis:<\/strong>\u00a0 21\/12\/2009<\/li>\n<\/ul>\n<p>&nbsp;<\/p>\n<h3>Direcci\u00f3n y tribunal<\/h3>\n<ul>\n<li><strong>Director de la tesis<\/strong>\n<ul>\n<li>Araceli Del Arco Martinez<\/li>\n<\/ul>\n<\/li>\n<li><strong>Tribunal<\/strong>\n<ul>\n<li>Presidente del tribunal: Jos\u00e9 manuel Cuezva marcos <\/li>\n<li>eduardo Rial zueco (vocal)<\/li>\n<li>Santiago Lamas pel\u00e1ez (vocal)<\/li>\n<li>Carlos Villalobos Jorge (vocal)<\/li>\n<\/ul>\n<\/li>\n<\/ul>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Tesis doctoral de Javier Traba Dominguez The transport of metabolites across the inner mitocondrial membrane is carried out by a [&hellip;]<\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"site-sidebar-layout":"default","site-content-layout":"","ast-site-content-layout":"","site-content-style":"default","site-sidebar-style":"default","ast-global-header-display":"","ast-banner-title-visibility":"","ast-main-header-display":"","ast-hfb-above-header-display":"","ast-hfb-below-header-display":"","ast-hfb-mobile-header-display":"","site-post-title":"","ast-breadcrumbs-content":"","ast-featured-img":"","footer-sml-layout":"","theme-transparent-header-meta":"","adv-header-id-meta":"","stick-header-meta":"","header-above-stick-meta":"","header-main-stick-meta":"","header-below-stick-meta":"","astra-migrate-meta-layouts":"default","ast-page-background-enabled":"default","ast-page-background-meta":{"desktop":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center 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