Cited by 373Alzheimer's disease research and treatmentsCellular transport and secretionDementia and Cognitive Impairment Research

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Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative

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Gabuzda, D., Busciglio, J., Chen, L.B., Matsudaira, P., Yankner, B.A.·1994·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(17)36875-8

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Abstract

The cellular mechanisms which lead to the generation and pathological deposition of beta amyloid in Alzheimer's disease are unknown. In this report we describe the proteolytic processing of the amyloid precursor protein (APP) to an 11.5-kDa COOH-terminal derivative which contains the full-length beta amyloid sequence. This processing step normally occurs at low levels in parallel with APP maturation in the secretory pathway. Inhibition of oxidative energy metabolism by sodium azide or the mitochondrial uncoupler carbonyl cyanide m-chlorophenylhydrazone increased the proteolysis of APP to the 11.5-kDa derivative by about 80-fold with accumulation of this APP derivative in the Golgi complex. Agents which inhibit protein transport in the secretory pathway, including monensin and brefeldin A, also increased the production of the 11.5-kDa derivative. Inhibition of APP maturation demonstrated that the 11.5-kDa derivative could be produced by proteolysis of immature APP. These results demonstrate that APP processing to potentially amyloidogenic COOH-terminal derivatives occurs in either the endoplasmic reticulum or Golgi complex and can be modulated by the state of cellular energy metabolism. Deficits in oxidative energy metabolism have recently been found in the cerebral cortex of patients with Alzheimer's disease. These findings raise the possibility that energy-related metabolic stress may lead to altered metabolism of APP and contribute to amyloidosis in Alzheimer's disease.

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Authors: Gabuzda, D., Busciglio, J., Chen, L. B., Matsudaira, P., & Yankner, B. A.
Affiliations: Boston Children's Hospital (US)
ORCID: Gabuzda, D.
Busciglio, J.
Matsudaira, P.
Yankner, B.A.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1994-05
Volume: 269
Issue: 18
Pages: 13623-13628
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(17)36875-8
OpenAlex: W1580327310
Cited by: 373
References: 45
Citations by year: 2026: 3 · 2025: 3 · 2024: 7 · 2023: 9 · 2022: 5 · 2021: 14 · 2020: 13 · 2019: 16 · 2018: 14 · 2017: 6 · 2016: 9 · 2015: 9 · 2014: 6 · 2013: 7 · 2012: 11
FWCI: 13.25
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 9674 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r29ag009229-05)
National Institute on Aging (AG09229)
National Institute of Neurological Disorders and Stroke (R01NS030352, NS30352)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: amyloid precursor protein, APP processing, amyloid-beta, Alzheimer's disease, oxidative metabolism, mitochondrial uncoupling, sodium azide, CCCP, Golgi apparatus, secretory pathway, protein trafficking, endoplasmic reticulum, proteolysis, metabolic stress, amyloidosis
MeSH terms: Adenosine Triphosphate, Amyloid, Biological Transport, Cells, Cultured, Energy Metabolism, Humans, Hydrolysis, Protein Processing, Post-Translational, Amyloid beta-Protein Precursor

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Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative

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