{"id":108707,"date":"2018-03-11T10:33:41","date_gmt":"2018-03-11T10:33:41","guid":{"rendered":"https:\/\/www.deberes.net\/tesis\/sin-categoria\/estudio-de-la-funcion-de-la-protea%c2%adna-mediadora-de-respuesta-a-colapsinas-2-crmp-2-en-cancer-de-pulmon-no-microca%c2%adtico\/"},"modified":"2018-03-11T10:33:41","modified_gmt":"2018-03-11T10:33:41","slug":"estudio-de-la-funcion-de-la-protea%c2%adna-mediadora-de-respuesta-a-colapsinas-2-crmp-2-en-cancer-de-pulmon-no-microca%c2%adtico","status":"publish","type":"post","link":"https:\/\/www.deberes.net\/tesis\/citologia\/estudio-de-la-funcion-de-la-protea%c2%adna-mediadora-de-respuesta-a-colapsinas-2-crmp-2-en-cancer-de-pulmon-no-microca%c2%adtico\/","title":{"rendered":"Estudio de la funci\u00f3n de la prote\u00edna mediadora de respuesta a colapsinas 2 (crmp-2) en c\u00e1ncer de pulm\u00f3n no microc\u00edtico"},"content":{"rendered":"<h2>Tesis doctoral de <strong> Erik Wolfgang Oliemuller Garc\u00eda <\/strong><\/h2>\n<p>Collapsin response mediator protein 2 (crmp-2) is a tubulin adaptor protein firstly described in neurons. This protein participates in tubulin polymerization by adding tubulin dimers to the growing tip of microtubules. Crmp-2 function as tubulin adaptor and is regulated by its phosphorylation in such a way that it decreases its affinity for tubulin and abrogates microtubule polymerization. microtubules are involved in a wide variety of cellular functions being most relevant its participation in cell division and migration; both processes being deregulated in cancer. There is scarce data on crmp-2 expression and phosphorylation in cancer. In this work we have described that crmp-2 is over-expressed in immortalized and transformed lung epithelial cells when compared to normal epithelium. Crmp-2 phosphorylation in ser 518 seems to be exclusive of transformed nsclc cells. in vitro experiments were performed by over-expressing crmp-2 and its phosphomimetic and phosphodefective mutants in a549 nsclc cells. After performing cell adhesion, migration and clonogenecity assays, crmp-2 phosphomimetic clones offered a more agressive behaviour. In vivo experiments performed in xenographt models in nude mice rendered contradictory results: cells expressing the phosphomimetic form of crmp-2 produced the smallest tumors while those expressing crmp-2 phosohodefective mutants resulted in the greatest but more apoptotic-prone ones. the study of the participation of crmp-2 in mitosis revealed its interaction with tubulin spindle during mitosis in a phosphorylation dependent way. Changes in crmp-2 phosphorylation status lead to alterations in the duration of several mitotic phases and aberrant cytocinesis, in the case of cells expressing crmp-2 phosphomimetic mutants.  crmp-2\tphosphorylation\tgsk-3&#946;\tmitosis \tnsclc \tmicrotubules<\/p>\n<p>&nbsp;<\/p>\n<h3>Datos acad\u00e9micos de la tesis doctoral \u00ab<strong>Estudio de la funci\u00f3n de la prote\u00edna mediadora de respuesta a colapsinas 2 (crmp-2) en c\u00e1ncer de pulm\u00f3n no microc\u00edtico<\/strong>\u00ab<\/h3>\n<ul>\n<li><strong>T\u00edtulo de la tesis:<\/strong>\u00a0 Estudio de la funci\u00f3n de la prote\u00edna mediadora de respuesta a colapsinas 2 (crmp-2) en c\u00e1ncer de pulm\u00f3n no microc\u00edtico <\/li>\n<li><strong>Autor:<\/strong>\u00a0 Erik Wolfgang Oliemuller Garc\u00eda <\/li>\n<li><strong>Universidad:<\/strong>\u00a0 Navarra<\/li>\n<li><strong>Fecha de lectura de la tesis:<\/strong>\u00a0 27\/05\/2011<\/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>Ana Rouzaut Subira<\/li>\n<\/ul>\n<\/li>\n<li><strong>Tribunal<\/strong>\n<ul>\n<li>Presidente del tribunal: Mar\u00eda pilar Sesma egozcue <\/li>\n<li>susana Llanos gir\u00f3n (vocal)<\/li>\n<li>ricardo Madrid gonzalez (vocal)<\/li>\n<li>Carlos gabriel de Miguel vazquez (vocal)<\/li>\n<\/ul>\n<\/li>\n<\/ul>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Tesis doctoral de Erik Wolfgang Oliemuller Garc\u00eda Collapsin response mediator protein 2 (crmp-2) is a tubulin adaptor protein firstly described [&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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