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[P4–450]: HIPPOCAMPAL SLICES FROM CALHM1‐KO MOUSE, UPON OXYGEN‐GLUCOSE‐DEPRIVATION, ALTERS HIF‐1ALPHA AND AMYLOID β PRODUCTION
Author(s) -
Garrosa Javier,
Paredes Iñigo,
Lopez Manuela G.,
CanoAbad Maria
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.2017.07.611
Subject(s) - excitotoxicity , hippocampal formation , western blot , amyloid beta , knockout mouse , amyloid precursor protein , brain ischemia , endocrinology , ischemia , medicine , glutamate receptor , chemistry , biology , biochemistry , alzheimer's disease , receptor , peptide , disease , gene
Figure 1. Receptormediated internalizationofAb1-42.SH-EP1cells stablyexpressinga7-nAChRs ora7b2-nAChRs, andwild type cells were incubatedwith oligomeric Ab1-42, or scrambled peptide followed by incubation with AmyloGlo dye (Biosensis). Fluorescence intensity was used to compare relative amounts of Ab1-42 internalization. (A) SH-EP1 cells expressing a7-nAChRs had markedly high levels of internalized Ab1 -42 compared to the (B) same type of cells incubated with a scrambled peptide sequence Ab1-42 (scrambled), which did not appear to have internalized the peptide. Cells expressing the a7-nAChRs (A) had a higher fluorescence intensity than cells expressing a7b2-nAChRs (C) when incubated with amyloid beta oligomers. These results suggest that a7-nAChRs have a higher internalization rate than a7b2-nAChRs. (Original grayscale images were pseudocolored to show details.).