Phosphorylation of APP in primary cortical neurons is p75NTR-dependent

Noralyn Manucat-Tan, Xin-Fu Zhou

Research output: Contribution to journalMeeting Abstractpeer-review


Endogeneous phosphorylarted form of APP (pAPP) was investigated in WT and p75KO neurons to elucidate whether APP phosphorylation is mediated by p75. In addition, APP (wild type) and mutant APP (T668A) will be co‐transfected with different forms of p75 to identify the interaction of p75 and pAPP in vitro.

Mouse primary cortical neuron cultures from wild type and p75KO mice were treated with amyloid beta 42 and the level of phosphorylated APP measured by Western Blotting. The cololalization of pAPP/p75, BACE1/p75 were also investigated by immunohistochemistry. In addition, phosphorylation of APP in AD models with wild type and knocked out p75 will be further investigated.

The phosphorylation of APP was increased when treated with 0.1, 0.3 and 1.0 uM amyloid beta 42 in WT primary neurons but not in p75KO neurons. In WT neurons, p75 colocalized with pAPP more at the soma and less at the dendrites while BACE1, one of the main secretases responsible for amyloidogenic processing of APP highly colocalized with p75 in the body and dendrites of neurons. This colocalization increase when treated with 0.1 uM amyloid beta.

p75NTR maybe required in APP phosphorylation and play a direct role in APP processing. Further investigation is required to show whether p75ECD can block APP phosphorylation in WT neurons and to determine the mechanism on how p75 mediate the process.
Original languageEnglish
Pages (from-to)P365-P365
Number of pages1
JournalAlzheimer's & Dementia
Issue number7S Part 8
Publication statusPublished - Jul 2015
Externally publishedYes
EventAlzheimer’s Association International Conference 2016 - Toronto, Canada
Duration: 22 Jul 201628 Jul 2016


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