Cited by 262Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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Role of the β‐amyloid protein in Alzheimer's disease

Sisodia, Sangram S., Price, Donald L.·1995·The FASEB Journal

DOI 10.1096/fasebj.9.5.7896005

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Abstract

A major histopathological hallmark of Alzheimer's disease (AD) is the presence of amyloid deposits in the parenchyma of the amygdala, hippocampus, and neocortex. The principal component of amyloid is the beta-amyloid protein (A beta), a 39-43 amino acid peptide composed of a portion of the transmembrane domain and the extracellular domain of the amyloid precursor protein (APP). APP occurs as several A beta-containing isoforms of 695, 751, and 770 amino acids, with the latter two APP containing a domain that shares structural and functional homologies with Kunitz serine protease inhibitors. In cultured cells, APP mature through the constitutive secretory pathway, and some cell surface-bound APP are cleaved by an enzyme, designated as alpha-secretase, within the A beta domain, an event that precludes A beta amyloidogenesis. Several studies have delineated two additional pathways of APP processing: first, an endosomal/lysosomal pathway generates a complex set of APP-related membrane-bound fragments, some of which contain the entire A beta sequence; and, second, by mechanisms which are not fully understood, A beta 1-40 is secreted into the conditioned medium in vitro and is present in cerebrospinal fluid in vivo. The intracellular sites of enzymes responsible for proteolytic cleavage at the NH2 and COOH termini of A beta, termed gamma- and beta-secretase, respectively, have not been identified. Finally, recent molecular genetic investigations have identified a variety of mutation…

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Authors: Sisodia, S. S., & Price, D. L.
Affiliations: Johns Hopkins University (US)
Corresponding author: Sisodia, Sangram S.
ORCID: Sisodia, Sangram S.
Venue: The FASEB Journal
Publisher: Wiley
Published: 1995-03
Volume: 9
Issue: 5
Pages: 366-370
ISSN: 0892-6638 (ISSN-L)
1530-6860
DOI: 10.1096/fasebj.9.5.7896005
OpenAlex: W1955730586
Cited by: 262
References: 0
Citations by year: 2026: 3 · 2025: 3 · 2024: 7 · 2023: 8 · 2022: 5 · 2021: 4 · 2020: 6 · 2019: 4 · 2018: 8 · 2017: 2 · 2016: 9 · 2015: 5 · 2014: 4 · 2013: 15 · 2012: 13
FWCI: 9.72
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: The FASEB Journal (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r35ag007914-03)
National Institute on Aging (AG07914, P50AG005146, AG 05146)
National Institute of Neurological Disorders and Stroke (NS-20471)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: Alzheimer's disease, amyloid-beta, amyloid precursor protein, APP processing, alpha-secretase, gamma-secretase, beta-secretase, APP mutations, familial Alzheimer's disease, cerebrospinal fluid, amyloid plaques
MeSH terms: Prion Proteins, Alzheimer Disease, Amyloid, Humans, Prions, Protein Precursors, Amyloid beta-Peptides

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Role of the β‐amyloid protein in Alzheimer's disease

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