ArticleThe Journal of biological chemistry2012
Heparan sulfate dissociates serum amyloid A (SAA) from acute-phase high-density lipoprotein, promoting SAA aggregation.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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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.
The trial behind it
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Who cites it
24 citing papers in PubMed, 52 citations in OpenAlex.
- Structural Basis for the Pro-amyloidogenic Action and Ligand Binding of a Novel W72R Variant of Human Apolipoprotein A-I.Journal of molecular biology · 2026Article
- Beyond Biomimetics: Pathology-Informed Engineering Rescues Reconstituted HDL From Inflammatory Dysfunction for Sepsis Immunotherapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Serum amyloid A: multifaceted roles in inflammation and cellular interactions.Immunologic research · 2025Review
- Serum Amyloid A Binding to Glycosaminoglycans is Synergistic with Amyloid Formation: Therapeutic Targeting in the Inflammation-linked Amyloidosis.Journal of molecular biology · 2025Article
- Elucidating the Mechanism of Recognition and Binding of Heparin to Amyloid Fibrils of Serum Amyloid A.Biochemistry · 2025Article
- Haptoglobin is dispensable for haemoglobin uptake byFrontiers in immunology · 2024Article
- The potential role of glycosaminoglycans in serum amyloid A fibril formation byMatrix biology plus · 2021Article
- Review
- Heparin-binding Peptides as Novel Therapies to Stop SARS-CoV-2 Cellular Entry and Infection.Molecular pharmacology · 2020Review
- Structural Basis for Vital Function and Malfunction of Serum Amyloid A: an Acute-Phase Protein that Wears Hydrophobicity on Its Sleeve.Current atherosclerosis reports · 2020Review
- Binding to heparin triggers deleterious structural and biochemical changes in human low-density lipoprotein, which are amplified in hyperglycemia.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Article
- Serum amyloid A exhibits pH dependent antibacterial action and contributes to host defense againstThe Journal of biological chemistry · 2020Article
- Serum amyloid A - a review.Molecular medicine (Cambridge, Mass.) · 2018Review
- Serum Amyloid A Is an Exchangeable Apolipoprotein.Arteriosclerosis, thrombosis, and vascular biology · 2018Article
- Serum amyloid A3 is a high density lipoprotein-associated acute-phase protein.Journal of lipid research · 2018Article
- Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission.Cold Spring Harbor perspectives in medicine · 2018Review
- Targeting heparin and heparan sulfate protein interactions.Organic & biomolecular chemistry · 2017Review
- Structure of serum amyloid A suggests a mechanism for selective lipoprotein binding and functions: SAA as a hub in macromolecular interaction networks.FEBS letters · 2016Article
- Historical and Current Concepts of Fibrillogenesis and In vivo Amyloidogenesis: Implications of Amyloid Tissue Targeting.Frontiers in molecular biosciences · 2016Review
- Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A.Biochimie · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inflammation-related (AA) amyloidosis is a severe clinical disorder characterized by the systemic deposition of the acute-phase reactant serum amyloid A (SAA). SAA is normally associated with the high-density lipoprotein (HDL) fraction in plasma, but under yet unclear circumstances, the apolipoprotein is converted into amyloid fibrils. AA amyloid and heparan sulfate (HS) display an intimate relationship in situ, suggesting a role for HS in the pathogenic process. This study reports that HS dissociates SAA from HDLs isolated from inflamed mouse plasma. Application of surface plasmon resonance spectroscopy and molecular modeling suggests that HS simultaneously binds to two apolipoproteins of HDL, SAA and ApoA-I, and thereby induce SAA dissociation. The activity requires a minimum chain length of 12-14 sugar units, proposing an explanation to previous findings that short HS fragments preclude AA amyloidosis. The results address the initial events in the pathogenesis of AA amyloidosis.
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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.