ArticleAnnals of the rheumatic diseases2005
Proteolysis of serum amyloid A and AA amyloid proteins by cysteine proteases: cathepsin B generates AA amyloid proteins and cathepsin L may prevent their formation.
Article in Annals of the rheumatic diseases, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 66 citations in OpenAlex.
- Functional Interactions Between Recombinant Serum Amyloid A1 (SAA1) and Chemokines in Leukocyte Recruitment.International journal of molecular sciences · 2025Review
- HGA Triggers SAA Aggregation and Accelerates Fibril Formation in the C20/A4 Alkaptonuria Cell Model.Cells · 2024Article
- New Regulatory roles for Human Serum Amyloid A.International journal of research in oncology · 2024Article
- Acute-serum amyloid A and A-SAA-derived peptides as formyl peptide receptor (FPR) 2 ligands.Frontiers in endocrinology · 2023Review
- N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study.PloS one · 2022Article
- Mass spectrometry characterization of light chain fragmentation sites in cardiac AL amyloidosis: insights into the timing of proteolysis.The Journal of biological chemistry · 2020Article
- 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
- Cathepsin B Dependent Cleavage Product of Serum Amyloid A1 Identifies Patients with Chemotherapy-Related Cardiotoxicity.ACS pharmacology & translational science · 2019Article
- Serum amyloid A promotes LPS clearance and suppresses LPS-induced inflammation and tissue injury.EMBO reports · 2018Article
- Serum amyloid A - a review.Molecular medicine (Cambridge, Mass.) · 2018Review
- High-density lipoprotein inhibits serum amyloid A-mediated reactive oxygen species generation and NLRP3 inflammasome activation.The Journal of biological chemistry · 2018Article
- Variation of amino acid sequences of serum amyloid a (SAA) and immunohistochemical analysis of amyloid a (AA) in Japanese domestic cats.The Journal of veterinary medical science · 2018Article
- Matrix Metalloproteinase-9-Generated COOH-, but Not NHFrontiers in immunology · 2018Article
- Cellular mechanism of fibril formation from serum amyloid A1 protein.EMBO reports · 2017Article
- Clinical, Epidemiological, and Histopathological Features of Respiratory Involvement in Rheumatoid Arthritis.BioMed research international · 2017Review
- Paradoxical effects of SAA on lipoprotein oxidation suggest a new antioxidant function for SAA.Journal of lipid research · 2016Article
- A multiplexed analysis approach identifies new association of inflammatory proteins in patients with overactive bladder.American journal of physiology. Renal physiology · 2016Article
- Article
- Thermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL.Journal of lipid research · 2015Article
- Human serum amyloid A3 (SAA3) protein, expressed as a fusion protein with SAA2, binds the oxidized low density lipoprotein receptor.PloS one · 2015Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAA amyloidosis develops in patients with chronic inflammatory diseases. The AA amyloid proteins are proteolytic fragments obtained from serum amyloid A (SAA). Previous studies have provided evidence that endosomes or lysosomes might be involved in the processing of SAA, and contribute to the pathology of AA amyloidosis.
objectiveTo investigate the anatomical distribution of cathepsin (Cath) B and CathL in AA amyloidosis and their ability to process SAA and AA amyloid proteins.
methodsand results: CathB and CathL were found immunohistochemically in every patient with AA amyloidosis and displayed a spatial relationship with amyloid in all the cases studied. Both degraded SAA and AA amyloid proteins in vitro. With the help of mass spectrometry 27 fragments were identified after incubation of SAA with CathB, nine of which resembled AA amyloid proteins, and seven fragments after incubation with CathL. CathL did not generate AA amyloid-like peptides. When native human AA amyloid proteins were used as a substrate 26 fragments were identified after incubation with CathB and 18 after incubation with CathL.
conclusionThe two most abundant and ubiquitously expressed lysosomal proteases can cleave SAA and AA amyloid proteins. CathB generates nine AA amyloid-like proteins by its carboxypeptidase activity, whereas CathL may prevent the formation of AA amyloid proteins by endoproteolytic activity within the N-terminal region of SAA. This is particularly interesting, because AA amyloidosis is a systemic disease affecting many organs and tissue types, almost all of which express CathB and CathL.
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