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[P4–383]: FYN KINASE CONTROLS AMYLOID PRECURSOR PROTEIN TYROSINE PHOSPHORYLATION AND TRAFFICKING IN NEURAL STEM CELLS OF ALZHEIMER's DISEASE PATIENTS
Author(s) -
Iannuzzi Filomena
Publication year - 2017
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2017.06.2254
Subject(s) - fyn , amyloid precursor protein , phosphorylation , microbiology and biotechnology , p3 peptide , amyloid precursor protein secretase , tyrosine kinase , kinase , signal transducing adaptor protein , neural stem cell , biochemistry of alzheimer's disease , proto oncogene tyrosine protein kinase src , biology , chemistry , alzheimer's disease , stem cell , medicine , signal transduction , disease
elements” (DRE) in regulatory area of viral genes. Here, within five HSV-1 genes, including critical immediate-early (IE) ones, SITECON detected 7 to 8 potentially active DREs in the regulatory regions. Alongside, we conducted pilot studies demonstrating multi-fold elevated replication of HSV-1 caused by 1.0 ppt dioxin in all infected astrocyte cell lines studied. We chose astrocyte models because amyloid plaques appear early during AD, and their development is intimately linked to activated astrocytes and microglia. Also, the results obtained stick to the recent report that the dioxinspecific AhR, a key member of the transcriptional complex activating HSV-1 replication, is found in brain tissue, and may be associated with glial cells rather than neurons. Conclusions: Here we present data on newly molecular mechanism of how host cell dioxin receptor (AhR-Arnt) complex trans-activate neurotropic HSV-1 linked to AD.