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Sequential proteolysis of APP by beta\u2010 and gamma\u2010secretases generates amyloid\u2010beta peptide (A\u03b2), the main component of senile plaques in Alzheimer Disease. Alternative APP cleavage by alpha\u2010secretase occurs within A\u03b2 domain, releasing soluble \u03b1\u2010APP (sAPP\u03b1), a neurotrophic fragment. Among other functions, sAPP\u03b1 is important to synaptogenesis, neural survival and axonal growth. APP and sAPP\u03b1 levels are increased in models of neuroplasticity, which suggests an important role for APP and its metabolites, especially sAPP\u03b1, in the rearranging brain. In this work we analyzed the effects of monocular enucleation (ME), a classical model of lesion\u2010induced plasticity, upon APP content, processing and also in secretases levels. Besides, we addressed whether \u03b1\u2010secretase activity is crucial for retinotectal remodeling after ME. Our results showed that ME induced a transient reduction in total APP content. We also detected an increase in \u03b1\u2010secretase expression and in sAPP production concomitant with a reduction in A\u03b2 and \u03b2\u2010secretase contents. These data suggest that ME facilitates APP processing by the non\u2010amyloidogenic pathway, increasing sAPP\u03b1 levels. Indeed, the pharmacological inhibition of \u03b1\u2010secretase activity reduced the axonal sprouting of ipsilateral retinocollicular projections from the intact eye after ME, suggesting that sAPP\u03b1 is necessary for synaptic structural rearrangement. Understanding how APP processing is regulated under lesion conditions may provide new insights into APP physiological role on neural plasticity.<\/jats:p>","DOI":"10.1016\/j.ijdevneu.2017.03.003","type":"journal-article","created":{"date-parts":[[2017,3,18]],"date-time":"2017-03-18T16:47:26Z","timestamp":1489855646000},"page":"16-25","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Monocular denervation of visual nuclei modulates APP processing and sAPP\u03b1 production: A possible role on neural plasticity"],"prefix":"10.1002","volume":"60","author":[{"given":"Juliana Ferreira","family":"Vasques","sequence":"first","affiliation":[{"name":"Programa nde Neuroci\u00eancias Departamento de Neurobiologia Instituto de Biologia, Universidade Federal Fluminense CEP 24001\u2010970 Niter\u00f3i 100180 RJ Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pedro Vin\u00edcius Bastos","family":"Heringer","sequence":"additional","affiliation":[{"name":"Programa nde Neuroci\u00eancias Departamento de Neurobiologia Instituto de Biologia, Universidade Federal Fluminense CEP 24001\u2010970 Niter\u00f3i 100180 RJ Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Renata Guedes","family":"de Jesus Gon\u00e7alves","sequence":"additional","affiliation":[{"name":"Programa nde Neuroci\u00eancias Departamento de Neurobiologia Instituto de Biologia, Universidade Federal Fluminense CEP 24001\u2010970 Niter\u00f3i 100180 RJ Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paula","family":"Campello\u2010Costa","sequence":"additional","affiliation":[{"name":"Programa nde Neuroci\u00eancias Departamento de Neurobiologia Instituto de Biologia, Universidade Federal Fluminense CEP 24001\u2010970 Niter\u00f3i 100180 RJ Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Claudio Alberto","family":"Serfaty","sequence":"additional","affiliation":[{"name":"Programa nde Neuroci\u00eancias Departamento de Neurobiologia Instituto de Biologia, Universidade Federal Fluminense CEP 24001\u2010970 Niter\u00f3i 100180 RJ Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adriana da Cunha","family":"Faria\u2010Melibeu","sequence":"additional","affiliation":[{"name":"Programa nde Neuroci\u00eancias Departamento de Neurobiologia Instituto de Biologia, Universidade Federal Fluminense CEP 24001\u2010970 Niter\u00f3i 100180 RJ Brazil"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2017,3,18]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/srep11708"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.neurobiolaging.2006.11.004"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(76)90527-3"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1038\/85064"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0016301"},{"key":"e_1_2_8_7_1","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1006\/exnr.2002.7920","article-title":"Phosphatidylinositol\u20103\u2010kinase\u2010Akt\u2010kinase and p42\/p44 mitogen\u2010activated protein kinases mediate neurotrophic and excitoprotective actions of a secreted form of amyloid precursor protein","volume":"175","author":"Cheng G.","year":"2002","journal-title":"Exp. 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