To the top

Page Manager: Webmaster
Last update: 9/11/2012 3:13 PM

Tell a friend about this page
Print version

The proinflammatory activ… - University of Gothenburg, Sweden Till startsida
Sitemap
To content Read more about how we use cookies on gu.se

The proinflammatory activity of recombinant serum amyloid A is not shared by the endogenous protein in the circulation.

Journal article
Authors Lena Björkman
John G Raynes
Chandrabala Shah
Anna Karlsson
Claes Dahlgren
Johan Bylund
Published in Arthritis and rheumatism
Volume 62
Issue 6
Pages 1660-5
ISSN 1529-0131
Publication year 2010
Published at Institute of Medicine, Department of Rheumatology and Inflammation Research
Pages 1660-5
Language en
Links dx.doi.org/10.1002/art.27440
Keywords Acute-Phase Reaction, immunology, metabolism, Arthritis, Rheumatoid, blood, immunology, Enzyme-Linked Immunosorbent Assay, Flow Cytometry, Humans, L-Selectin, metabolism, Leukocytes, Mononuclear, immunology, metabolism, Neutrophil Activation, immunology, Recombinant Proteins, immunology, metabolism, pharmacology, Serum Amyloid A Protein, immunology, metabolism, pharmacology
Subject categories Microbiology in the medical area, Dermatology and Venereal Diseases

Abstract

OBJECTIVE: Elevated serum levels of the acute-phase protein serum amyloid A (SAA) are a marker for active rheumatoid arthritis (RA), and SAA can also be found in the tissues of patients with active RA. Based on a number of studies with recombinant SAA (rSAA), the protein has been suggested to be a potent proinflammatory mediator that activates human neutrophils, but whether endogenous SAA shares these proinflammatory activities has not been directly addressed. The present study was undertaken to investigate whether SAA in the plasma of patients with RA possesses proinflammatory properties and activates neutrophils in a manner similar to that of the recombinant protein. METHODS: Neutrophil activation was monitored by flow cytometry, based on L-selectin shedding from cell surfaces. Whole blood samples from healthy subjects and from RA patients with highly elevated SAA levels were studied before and after stimulation with rSAA as well as purified endogenous SAA. RESULTS: Recombinant SAA potently induced cleavage of L-selectin from neutrophils and in whole blood samples. Despite highly elevated SAA levels, L-selectin was not down-regulated on RA patient neutrophils as compared with neutrophils from healthy controls. Spiking SAA-rich whole blood samples from RA patients with rSAA, however, resulted in L-selectin shedding. In addition, SAA purified from human plasma was completely devoid of neutrophil- or macrophage-activating capacity. CONCLUSION: The present findings show that rSAA is proinflammatory but that this activity is not shared by endogenous SAA, either when present in the circulation of RA patients or when purified from plasma during an acute-phase response.

Page Manager: Webmaster|Last update: 9/11/2012
Share:

The University of Gothenburg uses cookies to provide you with the best possible user experience. By continuing on this website, you approve of our use of cookies.  What are cookies?