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The amyloid precursor protein of Alzheimer’s disease localizes to a domain adjacent to synaptic vesicles of the presynaptic terminal (596.9)
Author(s) -
Protsenko Ekaterina,
DeGiorgis Joseph
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.596.9
Subject(s) - synaptic vesicle , amyloid precursor protein , vesicle , alzheimer's disease , biology , microbiology and biotechnology , neuroscience , chemistry , biochemistry , disease , pathology , medicine , membrane
Alzheimer’s disease (AD) afflicts an estimated 26 million individuals worldwide and its incidence is predicted to reach 100 million by 2050. While abnormal aggregation of the A‐beta component of the amyloid precursor protein (APP) has been causally linked to AD, APP’s endogenous function remains elusive. While a number of reports claim that APP associates with synaptic vesicles, our recent experiments by confocal microscopy suggest that APP localizes to a region near the synaptic vesicles but does not directly overlap with the vesicular domain. Synaptic vesicles were identified by antibodies against the synaptic vesicle protein SV2, while APP was identified by an antibody against the C‐terminus of human APP. Similar experiments using antibodies against APP and the post‐synaptic marks PSD‐93 and PSD‐95 show that APP also does not overlap with the post‐synaptic density (PSD). We are currently immune‐localizing APP at the EM level in goldfish spinal cord using nano‐gold conjugated secondary antibodies and silver enhancement. All microscopy work was performed using goldfish and lamprey tissues. Sequencing of the species’ respective APP genes shows that these sequences share high sequence homology with the human APP responsible for the disease. Grant Funding Source : Supported by the Rhode Island INBRE Program NIMGS grant 5 P20 GM103430‐13