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Analysis of intracellular amyloid‐β as a consistent feature of hippocampal neurons
Author(s) -
Blair Jeffrey Adam,
Siedlak Sandra L,
Zhu Xiongwei,
Lee Hyounggon,
Salomon Robert G,
Nunomura Akihiko,
Castellani Rudy J,
Smith Mark A
Publication year - 2011
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.25.1_supplement.965.1
Subject(s) - senile plaques , amyloid (mycology) , pathological , disease , hippocampal formation , extracellular , biology , neuroscience , intracellular , pathology , population , etiology , alzheimer's disease , medicine , microbiology and biotechnology , environmental health
Amyloid‐β, a 39–43 amino acid long peptide, accumulates both intraneuronally (iAβ) and in extracellular senile plaques, the major pathological hallmark in Alzheimer disease (AD). While hypotheses on the role of iAβ are most often derived from etiological approaches regarding AD, iAβ is also commonly reported in the brains of non‐diseased individuals. In this investigation of iAβ, we designed experiments to consider a variety of biological circumstances and relate iAβ to parameters including circumstances of death, use of opiates, gender, postmortem interval, ApoE genotype, disease state, tissue handling and staining methodologies. Ongoing analyses on this large population (n=67) will determine whether iAβ shows a pattern of natural occurrence and whether iAβ plays a role in the risk of or development of AD.