ArticleThe Journal of biological chemistry2009
The Caenorhabditis elegans A beta 1-42 model of Alzheimer disease predominantly expresses A beta 3-42.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.
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Who cites it
74 citing papers in PubMed, 122 citations in OpenAlex.
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- A C. elegans model of familial Alzheimer's disease shows age-dependent synaptic degeneration independent of amyloid β-peptide.Neurobiology of disease · 2026Article
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- Label-Free Proteomic Profiling of the dvls2 (CL2006) Caenorhabditis elegans Alzheimer's Disease (AD) Model Reveals Conserved Molecular Signatures Shared With the Human AD Brain.Journal of neurochemistry · 2025Article
- Experimental modeling of Alzheimer's disease: Translational lessons from cross-taxon analyses.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025Review
- A Brief Review on Caenorhabditis elegans Role in Modelling Neurodegenerative Disease.Central nervous system agents in medicinal chemistry · 2025Review
- Cathepsin B promotes Aβ proteotoxicity by modulating aging regulating mechanisms.Nature communications · 2024Article
- Chemical Genetics inACS chemical biology · 2024Article
- Towards Understanding Neurodegenerative Diseases: Insights fromInternational journal of molecular sciences · 2023Review
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- Activation of autophagy attenuates motor deficits and extends lifespan in a C. elegans model of ALS.Free radical biology & medicine · 2022Article
- Modeling Alzheimer's Disease inBiomedicines · 2022Review
- Suppression of a core metabolic enzyme dihydrolipoamide dehydrogenase (Genes & diseases · 2021Article
- Beneficial Effects of Cyclic Ether 2-Butoxytetrahydrofuran from Sea CucumberMolecules (Basel, Switzerland) · 2021Article
14 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transgenic expression of human amyloid beta (A beta) peptide in body wall muscle cells of Caenorhabditis elegans has been used to better understand aspects of Alzheimer disease (AD). In human aging and AD, A beta undergoes post-translational changes including covalent modifications, truncations, and oligomerization. Amino truncated A beta is increasingly recognized as potentially contributing to AD pathogenesis. Here we describe surface-enhanced laser desorption ionization-time of flight mass spectrometry mass spectrometry of A beta peptide in established transgenic C. elegans lines. Surprisingly, the A beta being expressed is not full-length 1-42 (amino acids) as expected but rather a 3-42 truncation product. In vitro analysis demonstrates that A beta(3-42) self-aggregates like A beta(1-42), but more rapidly, and forms fibrillar structures. Similarly, A beta(3-42) is also the more potent initiator of A beta(1-40) aggregation. Seeded aggregation via A beta(3-42) is further enhanced via co-incubation with the transition metal Cu(II). Although unexpected, the C. elegans model of A beta expression can now be co-opted to study the proteotoxic effects and processing of A beta(3-42).
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