Reference : Monomeric calgranulins measured by SELDI-TOF mass spectrometry and calprotectin measu...
Scientific journals : Article
Human health sciences : Rheumatology
Human health sciences : Gastroenterology & hepatology
http://hdl.handle.net/2268/4957
Monomeric calgranulins measured by SELDI-TOF mass spectrometry and calprotectin measured by ELISA as biomarkers in arthritis
English
De Seny, Dominique mailto [Centre Hospitalier Universitaire de Liège - CHU > > Rhumatologie >]
Fillet, Marianne mailto [Université de Liège - ULg > Département de pharmacie > Analyse des médicaments >]
Ribbens, Clio mailto [Centre Hospitalier Universitaire de Liège - CHU > > Rhumatologie >]
Marée, Raphaël mailto [Université de Liège - ULg > > GIGA-Management : Plateforme bioinformatique >]
Meuwis, Marie-Alice mailto [Université de Liège - ULg > > GIGA-Management : Plate-forme protéomique >]
Lutteri, Laurence mailto [Centre Hospitalier Universitaire de Liège - CHU > > Chimie médicale >]
Chapelle, Jean-Paul mailto [Centre Hospitalier Universitaire de Liège - CHU > > Chimie médicale >]
Wehenkel, Louis mailto [Université de Liège - ULg > Dép. d'électric., électron. et informat. (Inst.Montefiore) > Systèmes et modélisation >]
Louis, Edouard mailto [Université de Liège - ULg > Département des sciences cliniques > Hépato-gastroentérologie - Relations académiques et scientifiques (Médecine) >]
Merville, Marie-Paule [Université de Liège - ULg > Département de pharmacie > Chimie médicale >]
Malaise, Michel mailto [Centre Hospitalier Universitaire de Liège - CHU > > Rhumatologie >]
2008
Clinical Chemistry
American Association for Clinical Chemistry
54
1066-1075
Yes (verified by ORBi)
International
0009-9147
1530-8561
Washington
DC
[en] Biological Markers ; Calgranulin A ; Calgranulin B ; Leukocyte L1 Antigen Complex ; S100 Proteins ; Serum Amyloid A Protein ; Arthritis, Rheumatoid ; Enzyme-Linked Immunosorbent Assay ; Psoriasis
[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.
Researchers ; Professionals
http://hdl.handle.net/2268/94555

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