ArticleCell stress & chaperones2013
Acute phase proteins are major clients for the chaperone action of α₂-macroglobulin in human plasma.
Article in Cell stress & chaperones, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Human α2-Macroglobulin: Architecture, Mechanisms, and Functional Implications.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Review
- Characterization of Plasma SDS-Protein Aggregation Profile of Patients with Heart Failure with Preserved Ejection Fraction.Journal of cardiovascular translational research · 2023Article
- The Influence of Clusterin Glycosylation Variability on Selected Pathophysiological Processes in the Human Body.Oxidative medicine and cellular longevity · 2022Review
- Article
- Potential Serum Biomarkers for Postoperative Neurocognitive Disorders Based on Proteomic Analysis of Cognitive-Related Brain Regions.Frontiers in aging neuroscience · 2021Article
- Human pregnancy zone protein stabilizes misfolded proteins including preeclampsia- and Alzheimer's-associated amyloid beta peptide.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Alpha-2-Macroglobulin, a Hypochlorite-Regulated Chaperone and Immune System Modulator.Oxidative medicine and cellular longevity · 2019Review
- Comparison of dextran and albumin on blood coagulation in patients undergoing major gynaecological surgery.Perioperative medicine (London, England) · 2018Article
- How schistosomes alter the human serum proteome.Molecular and biochemical parasitology · 2017Article
- Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
- Erratum issuedZammit, Nathan W [added]
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Extracellular protein misfolding is implicated in many age-related diseases including Alzheimer's disease, macular degeneration and arthritis. In this study, putative endogenous clients for the chaperone activity of α₂-macroglobulin (α₂M) were identified after human plasma was subjected to physiologically relevant sheer stress at 37 °C for 10 days. Western blot analysis showed that four major acute phase proteins: ceruloplasmin, fibrinogen, α₁-acid glycoprotein and complement component 3, preferentially co-purified with α₂M after plasma was stressed. Furthermore, the formation of complexes between α₂M and these putative chaperone clients, detected by sandwich ELISA, was shown to be enhanced in response to stress. These results support the hypothesis that α₂M plays an important role in extracellular proteostasis by sequestering misfolded proteins and targeting them for disposal, particularly during acute phase reactions.
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