[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
Foell D, Wittkowski H, Vogl T, Roth J. S100 proteins expressed in phagocytes: a novel group of damage-associated molecular pattern molecules. J Leukoc Biol 2007;81:28-37.
De Rycke L, Baeten D, Foell D, Kruithof E, Veys EM, Roth J, et al. Differential expression and response to anti-TNFα treatment of infiltrating versus resident tissue macrophage subsets in autoimmune arthritis. J Pathol 2005;206:17-27.
Frosch M, Strey A, Vogl T, Wulffraat NM, Kuis W, Sunderkotter C, et al. Myeloid-related proteins 8 and 14 are specifically secreted during interaction of phagocytes and activated endothelium and are useful markers for monitoring disease activity in pauciarticular-onset juvenile rheumatoid arthritis. Arthritis Rheum 2000;43:628-37.
Sunahori K, Yamamura M, Yamana J, Takasugi K, Kawashima M, Yamamoto H, et al. The S100A8/A9 heterodimer amplifies proinflammatory cytokine production by macrophages via activation of nuclear factor kappa B and p38 mitogen-activated protein kinase in rheumatoid arthritis. Arthritis Res Ther 2006;8:R69.
Hunter MJ, Chazin WJ. High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14. J Biol Chem 1998;273:12427-35.
Propper C, Huang X, Roth J, Sorg C, Nacken W. Analysis of the MRP8-MRP14 protein-protein interaction by the two-hybrid system suggests a prominent role of the C-terminal domain of S100 proteins in dimer formation. J Biol Chem 1999;274:183-8.
Strupat K, Rogniaux H, Van Dorsselaer A, Roth J, Vogl T. Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 are confirmed by electrospray ionization-mass analysis. J Am Soc Mass Spectrom 2000;11:780-8.
Korndorfer IP, Brueckner F, Skerra A. The crystal structure of the human (S100A8/S100A9)2 heterotetramer, calprotectin, illustrates how conformational changes of interacting α-helices can determine specific association of two EF-hand proteins. J Mol Biol 2007;370:887-98.
Zwadlo G, Bruggen J, Gerhards G, Schlegel R, Sorg C. Two calcium-binding proteins associated with specific stages of myeloid cell differentiation are expressed by subsets of macrophages in inflammatory tissues. Clin Exp Immunol 1988;72:510-5.
Kane D, Roth J, Frosch M, Vogl T, Bresnihan B, FitzGerald O. Increased perivascular synovial membrane expression of myeloid-related proteins in psoriatic arthritis. Arthritis Rheum 2003;48:1676-85.
Liao H, Wu J, Kuhn E, Chin W, Chang B, Jones MD, et al. Use of mass spectrometry to identify protein biomarkers of disease severity in the synovial fluid and serum of patients with rheumatoid arthritis. Arthritis Rheum 2004;50:3792-803.
Sinz A, Bantscheff M, Mikkat S, Ringel B, Drynda S, Kekow J, et al. Mass spectrometric proteome analyses of synovial fluids and plasmas from patients suffering from rheumatoid arthritis and comparison to reactive arthritis or osteoarthritis. Electrophoresis 2002;23:3445-56.
Tilleman K, Van Beneden K, Dhondt A, Hoffman I, De Keyser F, Veys E, et al. Chronically inflamed synovium from spondyloarthropathy and rheumatoid arthritis investigated by protein expression profiling followed by tandem mass spectrometry. Proteomics 2005;5:2247-57.
Lugering N, Stoll R, Kucharzik T, Schmid KW, Rohlmann G, Burmeister G, et al. Immunohistochemical distribution and serum levels of the Ca 2+-binding proteins MRP8, MRP14 and their heterodimeric form MRP8/14 in Crohn's disease. Digestion 1995;56:406-14.
Brun JG, Jonsson R, Haga HJ. Measurement of plasma calprotectin as an indicator of arthritis and disease activity in patients with inflammatory rheumatic diseases. J Rheumatol 1994;21:733-8.
Hammer HB, Odegard S, Fagerhol MK, Landewe R, van der Heijde D, Uhlig T, et al. Calprotectin (a major leucocyte protein) is strongly and independently correlated with joint inflammation and damage in rheumatoid arthritis. Ann Rheum Dis 2007;66:1093-7.
Vogl T, Propper C, Hartmann M, Strey A, Strupat K, van den Bos C, et al. S100A12 is expressed exclusively by granulocytes and acts independently from MRP8 and MRP14. J Biol Chem 1999;274:25291-6.
Hofmann MA, Drury S, Fu C, Qu W, Taguchi A, Lu Y, et al. RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell 1999;97:889-901.
Foell D, Kane D, Bresnihan B, Vogl T, Nacken W, Sorg C, et al. Expression of the pro-inflammatory protein S100A12 (EN-RAGE) in rheumatoid and psoriatic arthritis. Rheumatology (Oxford) 2003;42:1383-9.
Foell D, Kucharzik T, Kraft M, Vogl T, Sorg C, Domschke W, et al. Neutrophil derived human S100A12 (EN-RAGE) is strongly expressed during chronic active inflammatory bowel disease. Gut 2003;52:847-53.
Cai H, Song C, Endoh I, Goyette J, Jessup W, Freedman SB, et al. Serum amyloid A induces monocyte tissue factor. J Immunol 2007;178:1852-60.
Buhimschi IA, Buhimschi CS, Weiner CP, Kimura T, Hamar BD, Sfakianaki AK, et al. Proteomic but not enzyme-linked immunosorbent assay technology detects amniotic fluid monomeric calgranulins from their complexed calprotectin form. Clin Diagn Lab Immunol 2005;12:837-44.
Tang N, Tornatore P, Weinberger SR. Current developments in SELDI affinity technology. Mass Spectrom Rev 2004;23:34-44.
de Seny D, Fillet M, Meuwis MA, Geurts P, Lutteri L, Ribbens C, et al. Discovery of new rheumatoid arthritis biomarkers using the surface-enhanced laser desorption/ionization time-of-flight mass spectrometry ProteinChip approach. Arthritis Rheum 2005;52:3801-12.
Meuwis MA, Fillet M, Geurts P, de Seny D, Lutteri L, Chapelle JP, et al. Biomarker discovery for inflammatory bowel disease, using proteomic serum profiling. Biochem Pharmacol 2007;73:1422-33.
Arnett FC, Edworthy SM, Bloch DA, MacShane DJ, Fries JF, Cooper N. The American Rheumatism Association 1987 revised criteria for the classification of rheumatoid arthritis. Arthritis Rheum 1988;31:315-24.
Dougados M, van der Linden S, Juhlin R, Huitfeldt B, Amor B, Calin A, et al. The European Spondylarthropathy Study Group preliminary criteria for the classification of spondylarthropathy. Arthritis Rheum 1991;34:1218-27.
Sands BE. From symptom to diagnosis: clinical distinctions among various forms of intestinal inflammation. Gastroenterology 2004;126:1518-32.
Geurts P, Fillet M, de Seny D, Meuwis MA, Malaise M, Merville MP, et al. Proteomic mass spectra classification using decision tree based ensemble methods. Bioinformatics 2005;21:3138-45.
Ribbens C, Martin y Porras M, Franchimont N, Kaiser MJ, Jaspar JM, Damas P, et al. Increased matrix metalloproteinase-3 serum levels in rheumatic diseases: relationship with synovitis and steroid treatment. Ann Rheum Dis 2002;61:161-6.
Vogl T, Roth J, Sorg C, Hillenkamp F, Strupat K. Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 detected by ultraviolet matrix-assisted laser desorption/ionization mass spectrometry. J Am Soc Mass Spectrom 1999;10:1124-30.
Foell D, Roth J. Proinflammatory S100 proteins in arthritis and autoimmune disease. Arthritis Rheum 2004;50:3762-71.
Roesch Ely M, Nees M, Karsai S, Mägele I, Bogumil R, Vorderwülbecke S, et al. Transcript and proteome analysis reveals reduced expression of calgranulins in head and neck squamous cell carcinoma. Eur J Cell Biol 2005;84:431-44.
McMorran BJ, Ouvry Patat SA, Carlin JB, Grimwood K, Jones A, Armstrong DS, et al. Novel neutrophil-derived proteins in bronchoalveolar lavage fluid indicate an exaggerated inflammatory response in pediatric cystic fibrosis patients. Clin Chem 2007;53:1782-91.
Syversen SW, Gaarder PI, Goll GL, Odegard S, Haavardsholm EA, Mowinckel P, et al. High anti-CCP levels and an algorithm of four variables predict radiographic progression in patients with rheumatoid arthritis: results from a 10-year longitudinal study. Ann Rheum 2008; 2008;67:212-7.
Louis E, Ribbens C, Godon A, Franchimont D, De Groote D, Hardy N, et al. Increased production of matrix metalloproteinase-3 and tissue inhibitor of metalloproteinase-1 by inflamed mucosa in inflammatory bowel disease. Clin Exp Immunol 2000;120:241-6.
Mullan RH, Bresnihan B, Golden-Mason L, Markham T, O'Hara R, FitzGerald O, et al. Acute-phase serum amyloid A stimulation of angiogenesis, leukocyte recruitment, and matrix degradation in rheumatoid arthritis through an NF-κB-dependent signal transduction pathway. Arthritis Rheum 2006;54:105-14.
Stix B, Kahne T, Sletten K, Raynes J, Roessner A, Rocken C. Proteolysis of AA amyloid fibril proteins by matrix metalloproteinases-1, -2, and -3. Am J Pathol 2001;159:561-70.