Article (Scientific journals)
Monomeric calgranulins measured by SELDI-TOF mass spectrometry and calprotectin measured by ELISA as biomarkers in arthritis
De Seny, Dominique; Fillet, Marianne; Ribbens, Clio et al.
2008In Clinical Chemistry, 54, p. 1066-1075
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Keywords :
Biological Markers; Calgranulin A; Calgranulin B; Leukocyte L1 Antigen Complex; S100 Proteins; Serum Amyloid A Protein; Arthritis, Rheumatoid; Enzyme-Linked Immunosorbent Assay; Psoriasis
Abstract :
[en] BACKGROUND: SELDI-TOF mass spectrometry (MS) is a high-throughput proteomic approach with potential for identifying novel forms of serum biomarkers of arthritis. METHODS: We used SELDI-TOF MS to analyze serum samples from patients with various forms of inflammatory arthritis. Several protein profiles were collected on different Bio-Rad Laboratories ProteinChip arrays (CM10 and IMAC-Cu(2+)) and were evaluated statistically to select potential biomarkers. RESULTS: SELDI-TOF MS analyses identified several calgranulin proteins [S100A8 (calgranulin A), S100A9 (calgranulin B), S100A9*, and S100A12 (calgranulin C)], serum amyloid A (SAA), SAA des-Arg (SAA-R), and SAA des-Arg/des-Ser (SAA-RS) as biomarkers and confirmed the results with other techniques, such as western blotting, immunoprecipitation, and nano-LC-MS/MS. The S100 proteins were all able to significantly differentiate samples from patients with rheumatoid arthritis (RA), psoriatic arthritis (PsA), and ankylosing spondylitis (AS) from those of patients with inflammatory bowel diseases used as an inflammatory control (IC) group, whereas the SAA, SAA-R, and SAA-RS proteins were not, with the exception of AS. The 4 S100 proteins were coproduced in all of the pathologies and were significantly correlated with the plasma calprotectin concentration; however, these S100 proteins were correlated with the SAA peak intensities only in the RA and IC patient groups. In RA, these S100 proteins (except for S100A12) were significantly correlated with the serum concentrations of C-reactive protein, matrix metalloproteinase 3, and anti-cyclic citrullinated peptide and with the Disease Activity Score (DAS(28)). CONCLUSIONS: The SELDI-TOF MS technology is a powerful approach for analyzing the status of monomeric, truncated, or posttranslationally modified forms of arthritis biomarkers, such as the S100A8, S100A9, S100A12, and SAA proteins. The fact that the SELDI-TOF MS data were correlated with results obtained with the classic calprotectin ELISA test supports the reliability of this new proteomic technique.
Disciplines :
Gastroenterology & hepatology
Rheumatology
Author, co-author :
De Seny, Dominique ;  Centre Hospitalier Universitaire de Liège - CHU > Rhumatologie
Fillet, Marianne ;  Université de Liège - ULiège > Département de pharmacie > Analyse des médicaments
Ribbens, Clio ;  Centre Hospitalier Universitaire de Liège - CHU > Rhumatologie
Marée, Raphaël  ;  Université de Liège - ULiège > GIGA-Management : Plateforme bioinformatique
Meuwis, Marie-Alice  ;  Université de Liège - ULiège > GIGA-Management : Plate-forme protéomique
Lutteri, Laurence ;  Centre Hospitalier Universitaire de Liège - CHU > Chimie médicale
Chapelle, Jean-Paul ;  Centre Hospitalier Universitaire de Liège - CHU > Chimie médicale
Wehenkel, Louis  ;  Université de Liège - ULiège > Dép. d'électric., électron. et informat. (Inst.Montefiore) > Systèmes et modélisation
Louis, Edouard  ;  Université de Liège - ULiège > Département des sciences cliniques > Hépato-gastroentérologie - Relations académiques et scientifiques (Médecine)
Merville, Marie-Paule ;  Université de Liège - ULiège > Département de pharmacie > Chimie médicale
Malaise, Michel ;  Centre Hospitalier Universitaire de Liège - CHU > Rhumatologie
Language :
English
Title :
Monomeric calgranulins measured by SELDI-TOF mass spectrometry and calprotectin measured by ELISA as biomarkers in arthritis
Publication date :
2008
Journal title :
Clinical Chemistry
ISSN :
0009-9147
eISSN :
1530-8561
Publisher :
American Association for Clinical Chemistry, Washington, United States - District of Columbia
Volume :
54
Pages :
1066-1075
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 28 January 2009

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