| Literature DB >> 27726110 |
Agata Mata1,2,3,4, Laura Urrea1,2,3,4, Silvia Vilches1,2,3,4, Franc Llorens5, Katrin Thüne5, Juan-Carlos Espinosa6, Olivier Andréoletti7, Alejandro M Sevillano8,9, Juan María Torres6, Jesús Rodríguez Requena8,9, Inga Zerr5, Isidro Ferrer10,11,4, Rosalina Gavín1,2,3,4, José Antonio Del Río12,13,14,15.
Abstract
Reelin is an extracellular glycoprotein involved in key cellular processes in developing and adult nervous system, including regulation of neuronal migration, synapse formation, and plasticity. Most of these roles are mediated by the intracellular phosphorylation of disabled-1 (Dab1), an intracellular adaptor molecule, in turn mediated by binding Reelin to its receptors. Altered expression and glycosylation patterns of Reelin in cerebrospinal and cortical extracts have been reported in Alzheimer's disease. However, putative changes in Reelin are not described in natural prionopathies or experimental models of prion infection or toxicity. With this is mind, in the present study, we determined that Reelin protein and mRNA levels increased in CJD human samples and in mouse models of human prion disease in contrast to murine models of prion infection. However, changes in Reelin expression appeared only at late terminal stages of the disease, which prevent their use as an efficient diagnostic biomarker. In addition, increased Reelin in CJD and in in vitro models does not correlate with Dab1 phosphorylation, indicating failure in its intracellular signaling. Overall, these findings widen our understanding of the putative changes of Reelin in neurodegeneration.Entities:
Keywords: Cellular prion protein; Creutzfeldt-Jakob disease; Dab-1; Reelin
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Year: 2016 PMID: 27726110 DOI: 10.1007/s12035-016-0177-8
Source DB: PubMed Journal: Mol Neurobiol ISSN: 0893-7648 Impact factor: 5.590