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Macromolecular complexes in Alzheimers disease pathogenesis : dottorato di ricerca in scienze farmacotossicologiche, farmacognostiche e biotecnologie farmacologiche : tesi di dottorato

Epis, Roberta <1980- >

Tesi o dissertazioni - 2008

Abstract
MACROMOLECULAR COMPLEXES IN ALZHEIMER’S DISEASE PATHOGENESIS APP can undergo two different metabolic pathways: the amyloidogenic one, which leads to the release of Aß and the non-amyloidogenic one, mediated by a-secretase, ADAM10, that destroys this amyloidogenic peptide. These processes are differentially segregated within the cells. a-secretase activity is localized in the Trans-Golgi Network or at the plasma membrane. SAP97, a protein involved in dynamic trafficking of proteins to the excitatory synapse, can drive ADAM10 to the post synapse by direct interaction. This interaction can be disrupted by a cell-permeable peptide, Tat-Pro ADAM10709-729, that mimics the proline-rich region of ADAM10, responsible for its association to SAP97. We administered this peptide in adult mice for 14 days, to reduce ADAM10 trafficking to the membrane. The disruption of SAP97/ADAM10 interaction prevents the ADAM10-mediated cleavage of APP shifting APP metabolism towards amyloidosis. Recent studies showed that Aß monomers or oligomers can affect synaptic function [...]
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