ArticleThe Journal of biological chemistry2010
Inherent anti-amyloidogenic activity of human immunoglobulin gamma heavy chains.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Heavy Chains, Heavy Consequences: A Case of Concomitant Heavy Chain Amyloidosis and Heavy Chain Deposition Disease.Kidney medicine · 2025Article
- Amyloid-β predominant Alzheimer's disease neuropathologic change.Brain : a journal of neurology · 2025Article
- Genomics and Functional Genomics of Alzheimer's Disease.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2022Review
- Interactive Effects of HLA and GM Alleles on the Development of Alzheimer Disease.Neurology. Genetics · 2021Article
- Whole exome sequencing study identifies novel rare and common Alzheimer's-Associated variants involved in immune response and transcriptional regulation.Molecular psychiatry · 2020Article
- A human monoclonal IgG that binds aβ assemblies and diverse amyloids exhibits anti-amyloid activities in vitro and in vivo.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- Intravenous immunoglobulin for the treatment of Alzheimer's disease: current evidence and considerations.Degenerative neurological and neuromuscular disease · 2014Review
- Rational design of potent domain antibody inhibitors of amyloid fibril assembly.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Hippocampus in health and disease: An overview.Annals of Indian Academy of Neurology · 2012Article
- New pharmacological strategies for treatment of Alzheimer's disease: focus on disease modifying drugs.British journal of clinical pharmacology · 2012Review
- A monoclonal antibody against synthetic Aβ dimer assemblies neutralizes brain-derived synaptic plasticity-disrupting Aβ.Journal of neurochemistry · 2011Article
- Immunological origin and functional properties of catalytic autoantibodies to amyloid beta peptide.Journal of clinical immunology · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously shown that a subpopulation of naturally occurring human IgGs were cross-reactive against conformational epitopes on pathologic aggregates of Abeta, a peptide that forms amyloid fibrils in the brains of patients with Alzheimer disease, inhibited amyloid fibril growth, and dissociated amyloid in vivo. Here, we describe similar anti-amyloidogenic activity that is a general property of free human Ig gamma heavy chains. A gamma(1) heavy chain, F1, had nanomolar binding to an amyloid fibril-related conformational epitope on synthetic oligomers and fibrils as well as on amyloid-laden tissue sections. F1 did not bind to native Abeta monomers, further indicating the conformational nature of its binding site. The inherent anti-amyloidogenic activity of Ig gamma heavy chains was demonstrated by nanomolar amyloid fibril and oligomer binding by polyclonal and monoclonal human heavy chains that were isolated from inert or weakly reactive antibodies. Most importantly, the F1 heavy chain prevented in vitro fibril growth and reduced in vivo soluble Abeta oligomer-induced impairment of rodent hippocampal long term potentiation, a cellular mechanism of learning and memory. These findings demonstrate that free human Ig gamma heavy chains comprise a novel class of molecules for developing potential therapeutics for Alzheimer disease and other amyloid disorders. Moreover, establishing the molecular basis for heavy chain-amyloidogenic conformer interactions should advance understanding on the types of interactions that these pathologic assemblies have with biological molecules.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.