Journal
JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY
Volume 77, Issue 1, Pages 2-20Publisher
OXFORD UNIV PRESS INC
DOI: 10.1093/jnen/nlx099
Keywords
Amyloid; Entorhinal; Hippocampus; Neuropathology; Proteomics; SNAP; Subpial
Categories
Funding
- NIH [P30 AG028383, R01 AG042419, T32 AG000242]
- Institute of Academic Medicine at Houston Methodist
- NATIONAL INSTITUTE ON AGING [R01AG057187, R01AG042475, P30AG028383] Funding Source: NIH RePORTER
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Over the course of most common neurodegenerative diseases the amygdala accumulates pathologically misfolded proteins. Misfolding of 1 protein in aged brains often is accompanied by the misfolding of other proteins, suggesting synergistic mechanisms. The multiplicity of pathogenic processes in human amygdalae has potentially important implications for the pathogenesis of Alzheimer disease, Lewy body diseases, chronic traumatic encephalopathy, primary age-related tauopathy, and hippocampal sclerosis, and for the biomarkers used to diagnose those diseases. Converging data indicate that the amygdala may represent a preferential locus for a pivotal transition from a relatively benign clinical condition to a more aggressive disease wherein multiple protein species are misfolded. Thus, understanding of amygdalar pathobiology may yield insights relevant to diagnoses and therapies; it is, however, a complex and imperfectly defined brain region. Here, we review aspects of amygdalar anatomy, connectivity, vasculature, and pathologic involvement in neurodegenerative diseases with supporting data from the University of Kentucky Alzheimer's Disease Center autopsy cohort. Immunohistochemical staining of amygdalae for A beta, Tau, alpha-synuclein, and TDP-43 highlight the often-coexisting pathologies. We suggest that the amygdala may represent an incubator for misfolded proteins and that it is possible that misfolded amygdalar protein species are yet to be discovered.
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