Fibulin 3 peptides Fib3-1 and Fib3-2 are potential biomarkers of osteoarthritis
Objective This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and quantify them. Methods Proteomics analysis was performed in urine samples from 10 women (mean ± SD age 76.0 ± 5.0 years) undergoing knee rep...
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| Published in | Arthritis & rheumatology (Hoboken, N.J.) Vol. 64; no. 7; pp. 2260 - 2267 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article Web Resource |
| Language | English |
| Published |
Hoboken
Wiley Subscription Services, Inc., A Wiley Company
01.07.2012
Wiley Wiley Subscription Services, Inc John Wiley & Sons |
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| Abstract | Objective
This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and quantify them.
Methods
Proteomics analysis was performed in urine samples from 10 women (mean ± SD age 76.0 ± 5.0 years) undergoing knee replacement surgery due to severe OA and 5 healthy women (mean ± SD age 25.6 ± 2.6 years). Protein content was analyzed by 2‐dimensional differential gel electrophoresis. Protein spots that exhibited an OA:control abundance ratio of ≥1.5 were identified by mass spectrometry. Specific enzyme‐linked immunosorbent assays were developed and validated in serum obtained from 236 healthy subjects ages 20–64 years and from 76 patients with severe radiologic knee OA (mean ± SD age 68.8 ± 11.9 years). Immunohistochemical analysis was performed on articular cartilage from tibial plateaus.
Results
Thirteen proteins within spots that were significantly modified between groups were identified. Two peptides of fibulin 3, named Fib3‐1 and Fib3‐2, were of particular interest. Two antisera directed against these peptides were used to develop immunoassays. Compared with age‐matched healthy subjects, median levels of serum Fib3‐1 and Fib3‐2 were elevated in OA patients (54.6 pM versus 85.1 pM [P < 0.0001] and 144.4 pM versus 191.4 pM [P < 0.0001], respectively). Using area under the receiver operating characteristic curve analysis, we demonstrated that Fib3‐1 and Fib3‐2 levels discriminate between OA and normal populations. Immunostaining revealed the presence of Fib3‐1 and Fib3‐2 in chondrocytes and in the extracellular matrix of the superficial layer of the fibrillated cartilage.
Conclusion
Our findings indicate that Fib3‐1 and Fib3‐2 are potential biochemical markers for the diagnosis of OA. |
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| AbstractList | This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and quantify them.OBJECTIVEThis study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and quantify them.Proteomics analysis was performed in urine samples from 10 women (mean±SD age 76.0±5.0 years) undergoing knee replacement surgery due to severe OA and 5 healthy women (mean±SD age 25.6±2.6 years). Protein content was analyzed by 2-dimensional differential gel electrophoresis. Protein spots that exhibited an OA:control abundance ratio of ≥1.5 were identified by mass spectrometry. Specific enzyme-linked immunosorbent assays were developed and validated in serum obtained from 236 healthy subjects ages 20-64 years and from 76 patients with severe radiologic knee OA (mean±SD age 68.8±11.9 years). Immunohistochemical analysis was performed on articular cartilage from tibial plateaus.METHODSProteomics analysis was performed in urine samples from 10 women (mean±SD age 76.0±5.0 years) undergoing knee replacement surgery due to severe OA and 5 healthy women (mean±SD age 25.6±2.6 years). Protein content was analyzed by 2-dimensional differential gel electrophoresis. Protein spots that exhibited an OA:control abundance ratio of ≥1.5 were identified by mass spectrometry. Specific enzyme-linked immunosorbent assays were developed and validated in serum obtained from 236 healthy subjects ages 20-64 years and from 76 patients with severe radiologic knee OA (mean±SD age 68.8±11.9 years). Immunohistochemical analysis was performed on articular cartilage from tibial plateaus.Thirteen proteins within spots that were significantly modified between groups were identified. Two peptides of fibulin 3, named Fib3-1 and Fib3-2, were of particular interest. Two antisera directed against these peptides were used to develop immunoassays. Compared with age-matched healthy subjects, median levels of serum Fib3-1 and Fib3-2 were elevated in OA patients (54.6 pM versus 85.1 pM [P<0.0001] and 144.4 pM versus 191.4 pM [P<0.0001], respectively). Using area under the receiver operating characteristic curve analysis, we demonstrated that Fib3-1 and Fib3-2 levels discriminate between OA and normal populations. Immunostaining revealed the presence of Fib3-1 and Fib3-2 in chondrocytes and in the extracellular matrix of the superficial layer of the fibrillated cartilage.RESULTSThirteen proteins within spots that were significantly modified between groups were identified. Two peptides of fibulin 3, named Fib3-1 and Fib3-2, were of particular interest. Two antisera directed against these peptides were used to develop immunoassays. Compared with age-matched healthy subjects, median levels of serum Fib3-1 and Fib3-2 were elevated in OA patients (54.6 pM versus 85.1 pM [P<0.0001] and 144.4 pM versus 191.4 pM [P<0.0001], respectively). Using area under the receiver operating characteristic curve analysis, we demonstrated that Fib3-1 and Fib3-2 levels discriminate between OA and normal populations. Immunostaining revealed the presence of Fib3-1 and Fib3-2 in chondrocytes and in the extracellular matrix of the superficial layer of the fibrillated cartilage.Our findings indicate that Fib3-1 and Fib3-2 are potential biochemical markers for the diagnosis of OA.CONCLUSIONOur findings indicate that Fib3-1 and Fib3-2 are potential biochemical markers for the diagnosis of OA. OBJECTIVE: This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and quantify them. METHODS: Proteomics analysis was performed in urine samples from 10 women (mean+/-SD age 76.0+/-5.0 years) undergoing knee replacement surgery due to severe OA and 5 healthy women (mean+/-SD age 25.6+/-2.6 years). Protein content was analyzed by 2-dimensional differential gel electrophoresis. Protein spots that exhibited an OA:control abundance ratio of >/=1.5 were identified by mass spectrometry. Specific enzyme-linked immunosorbent assays were developed and validated in serum obtained from 236 healthy subjects ages 20-64 years and from 76 patients with severe radiologic knee OA (mean+/-SD age 68.8+/-11.9 years). Immunohistochemical analysis was performed on articular cartilage from tibial plateaus. RESULTS: Thirteen proteins within spots that were significantly modified between groups were identified. Two peptides of fibulin 3, named Fib3-1 and Fib3-2, were of particular interest. Two antisera directed against these peptides were used to develop immunoassays. Compared with age-matched healthy subjects, median levels of serum Fib3-1 and Fib3-2 were elevated in OA patients (54.6 pM versus 85.1 pM [P<0.0001] and 144.4 pM versus 191.4 pM [P<0.0001], respectively). Using area under the receiver operating characteristic curve analysis, we demonstrated that Fib3-1 and Fib3-2 levels discriminate between OA and normal populations. Immunostaining revealed the presence of Fib3-1 and Fib3-2 in chondrocytes and in the extracellular matrix of the superficial layer of the fibrillated cartilage. CONCLUSION: Our findings indicate that Fib3-1 and Fib3-2 are potential biochemical markers for the diagnosis of OA. This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and quantify them. Proteomics analysis was performed in urine samples from 10 women (mean±SD age 76.0±5.0 years) undergoing knee replacement surgery due to severe OA and 5 healthy women (mean±SD age 25.6±2.6 years). Protein content was analyzed by 2-dimensional differential gel electrophoresis. Protein spots that exhibited an OA:control abundance ratio of ≥1.5 were identified by mass spectrometry. Specific enzyme-linked immunosorbent assays were developed and validated in serum obtained from 236 healthy subjects ages 20-64 years and from 76 patients with severe radiologic knee OA (mean±SD age 68.8±11.9 years). Immunohistochemical analysis was performed on articular cartilage from tibial plateaus. Thirteen proteins within spots that were significantly modified between groups were identified. Two peptides of fibulin 3, named Fib3-1 and Fib3-2, were of particular interest. Two antisera directed against these peptides were used to develop immunoassays. Compared with age-matched healthy subjects, median levels of serum Fib3-1 and Fib3-2 were elevated in OA patients (54.6 pM versus 85.1 pM [P<0.0001] and 144.4 pM versus 191.4 pM [P<0.0001], respectively). Using area under the receiver operating characteristic curve analysis, we demonstrated that Fib3-1 and Fib3-2 levels discriminate between OA and normal populations. Immunostaining revealed the presence of Fib3-1 and Fib3-2 in chondrocytes and in the extracellular matrix of the superficial layer of the fibrillated cartilage. Our findings indicate that Fib3-1 and Fib3-2 are potential biochemical markers for the diagnosis of OA. Objective This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and quantify them. Methods Proteomics analysis was performed in urine samples from 10 women (mean plus or minus SD age 76.0 plus or minus 5.0 years) undergoing knee replacement surgery due to severe OA and 5 healthy women (mean plus or minus SD age 25.6 plus or minus 2.6 years). Protein content was analyzed by 2-dimensional differential gel electrophoresis. Protein spots that exhibited an OA:control abundance ratio of greater than or equal to 1.5 were identified by mass spectrometry. Specific enzyme-linked immunosorbent assays were developed and validated in serum obtained from 236 healthy subjects ages 20-64 years and from 76 patients with severe radiologic knee OA (mean plus or minus SD age 68.8 plus or minus 11.9 years). Immunohistochemical analysis was performed on articular cartilage from tibial plateaus. Results Thirteen proteins within spots that were significantly modified between groups were identified. Two peptides of fibulin 3, named Fib3-1 and Fib3-2, were of particular interest. Two antisera directed against these peptides were used to develop immunoassays. Compared with age-matched healthy subjects, median levels of serum Fib3-1 and Fib3-2 were elevated in OA patients (54.6 pM versus 85.1 pM [P < 0.0001] and 144.4 pM versus 191.4 pM [P < 0.0001], respectively). Using area under the receiver operating characteristic curve analysis, we demonstrated that Fib3-1 and Fib3-2 levels discriminate between OA and normal populations. Immunostaining revealed the presence of Fib3-1 and Fib3-2 in chondrocytes and in the extracellular matrix of the superficial layer of the fibrillated cartilage. Conclusion Our findings indicate that Fib3-1 and Fib3-2 are potential biochemical markers for the diagnosis of OA. Objective This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and quantify them. Methods Proteomics analysis was performed in urine samples from 10 women (mean ± SD age 76.0 ± 5.0 years) undergoing knee replacement surgery due to severe OA and 5 healthy women (mean ± SD age 25.6 ± 2.6 years). Protein content was analyzed by 2-dimensional differential gel electrophoresis. Protein spots that exhibited an OA:control abundance ratio of ≥1.5 were identified by mass spectrometry. Specific enzyme-linked immunosorbent assays were developed and validated in serum obtained from 236 healthy subjects ages 20-64 years and from 76 patients with severe radiologic knee OA (mean ± SD age 68.8 ± 11.9 years). Immunohistochemical analysis was performed on articular cartilage from tibial plateaus. Results Thirteen proteins within spots that were significantly modified between groups were identified. Two peptides of fibulin 3, named Fib3-1 and Fib3-2, were of particular interest. Two antisera directed against these peptides were used to develop immunoassays. Compared with age-matched healthy subjects, median levels of serum Fib3-1 and Fib3-2 were elevated in OA patients (54.6 pM versus 85.1 pM [P < 0.0001] and 144.4 pM versus 191.4 pM [P < 0.0001], respectively). Using area under the receiver operating characteristic curve analysis, we demonstrated that Fib3-1 and Fib3-2 levels discriminate between OA and normal populations. Immunostaining revealed the presence of Fib3-1 and Fib3-2 in chondrocytes and in the extracellular matrix of the superficial layer of the fibrillated cartilage. Conclusion Our findings indicate that Fib3-1 and Fib3-2 are potential biochemical markers for the diagnosis of OA. [PUBLICATION ABSTRACT] Objective This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and quantify them. Methods Proteomics analysis was performed in urine samples from 10 women (mean ± SD age 76.0 ± 5.0 years) undergoing knee replacement surgery due to severe OA and 5 healthy women (mean ± SD age 25.6 ± 2.6 years). Protein content was analyzed by 2‐dimensional differential gel electrophoresis. Protein spots that exhibited an OA:control abundance ratio of ≥1.5 were identified by mass spectrometry. Specific enzyme‐linked immunosorbent assays were developed and validated in serum obtained from 236 healthy subjects ages 20–64 years and from 76 patients with severe radiologic knee OA (mean ± SD age 68.8 ± 11.9 years). Immunohistochemical analysis was performed on articular cartilage from tibial plateaus. Results Thirteen proteins within spots that were significantly modified between groups were identified. Two peptides of fibulin 3, named Fib3‐1 and Fib3‐2, were of particular interest. Two antisera directed against these peptides were used to develop immunoassays. Compared with age‐matched healthy subjects, median levels of serum Fib3‐1 and Fib3‐2 were elevated in OA patients (54.6 pM versus 85.1 pM [P < 0.0001] and 144.4 pM versus 191.4 pM [P < 0.0001], respectively). Using area under the receiver operating characteristic curve analysis, we demonstrated that Fib3‐1 and Fib3‐2 levels discriminate between OA and normal populations. Immunostaining revealed the presence of Fib3‐1 and Fib3‐2 in chondrocytes and in the extracellular matrix of the superficial layer of the fibrillated cartilage. Conclusion Our findings indicate that Fib3‐1 and Fib3‐2 are potential biochemical markers for the diagnosis of OA. |
| Author | De Pauw, Edwin Deberg, Michelle Mazzucchelli, Gabriel Dubuc, Jean-Emile Henrotin, Yves Gharbi, Myriam |
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| Keywords | Peptides Diseases of the osteoarticular system Rheumatology Arthropathy Biological marker Degenerative disease Osteoarthritis |
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| Notes | ark:/67375/WNG-Q34K2WB9-N ArticleID:ART34392 istex:D12A14E6E8C5E1AC6DAAB681EEF1712BD34C2E57 Government of the Walloon Region of Belgium Drs. Henrotin and Gharbi contributed equally to this work. Drs. Henrotin, Gharbi, De Pauw, and Deberg hold patents for biomarkers of osteoarthritis and/or other aging‐related diseases and for the use of these biomarkers (EP 08157521.9, US 121737,051, EP 097557339.8, WO 2009/146956 A1, and 2009/146957.A1). Dr. Henrotin owns stock or stock options in Artialis. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 scopus-id:2-s2.0-84861961870 |
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| References | Nemirovskiy OV, Dufield DR, Sunyer T, Aggarwal P, Welsch DJ, Mathews WR. Discovery and development of a type II collagen neoepitope (TIINE) biomarker for matrix metalloproteinase activity: from in vitro to in vivo. Anal Biochem 2007; 361: 93-101. Deberg M, Labasse A, Christgau S, Cloos P, Bang Henriksen D, Chapelle JP, et al. New serum biochemical markers (Coll 2-1 and Coll 2-1 NO2) for studying oxidative-related type II collagen network degradation in patients with osteoarthritis and rheumatoid arthritis. Osteoarthritis Cartilage 2005; 13: 258-65. Klenotic PA, Munier FL, Marmorstein LY, Anand-Apte B. Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a binding partner of epithelial growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1): implications for macular degenerations. J Biol Chem 2004; 279: 30469-73. Wakabayashi T, Matsumine A, Nakazora S, Hasegawa M, Iino T, Ota H, et al. Fibulin-3 negatively regulates chondrocyte differentiation. Biochem Biophys Res Commun 2010; 391: 1116-21. Vincourt JB, Lionneton F, Kratassiouk G, Guillemin F, Netter P, Mainard D, et al. Establishment of a reliable method for direct proteome characterization of human articular cartilage. Mol Cell Proteomics 2006; 5: 1984-95. Blackburn J, Tarttelin EE, Gregory-Evans CY, Moosajee M, Gregory-Evans K. Transcriptional regulation and expression of the dominant drusen gene FBLN3 (EFEMP1) in mammalian retina. Invest Ophthalmol Vis Sci 2003; 44: 4613-21. Golightly YM, Marshall SW, Kraus VB, Renner JB, Villaveces A, Casteel C, et al. Serum cartilage oligomeric matrix protein, hyaluronan, high-sensitivity C-reactive protein, and keratan sulfate as predictors of incident radiographic knee osteoarthritis: differences by chronic knee symptoms [abstract]. Osteoarthritis Cartilage 2010; 18 Suppl 2: 62-3. Mobasheri A, Henrotin Y. Biomarkers of osteoarthritis: a review of recent research progress on soluble biochemical markers, published patents and areas for future development. Recent Pat Biomark 2011; 1: 25-43. Altman R, Asch E, Bloch D, Bole G, Borenstein D, Brandt K, et al. Development of criteria for the classification and reporting of osteoarthritis: classification of osteoarthritis of the knee. Arthritis Rheum 1986; 29: 1039-49. Ruiz-Romero C, Blanco FJ. Proteomics role in the search for improved diagnosis, prognosis and treatment of osteoarthritis. Osteoarthritis Cartilage 2010; 18: 500-9. Takei S, Hoshino T, Matsunaga K, Sakazaki Y, Sawada M, Oda H, et al. Soluble interleukin-18 receptor complex is a novel biomarker in rheumatoid arthritis. Arthritis Res Ther 2011; 13: R52. Zweig MH, Broste SK, Reinhart RA. ROC curve analysis: an example showing the relationships among serum lipid and apolipoprotein concentrations in identifying patients with coronary artery disease. Clin Chem 1992; 38: 1425-8. Felson DT. Identifying different osteoarthritis phenotypes through epidemiology. Osteoarthritis Cartilage 2010; 18: 601-4. Henrotin Y, Addison S, Kraus V, Deberg M. Type II collagen markers in osteoarthritis: what do they indicate? Curr Opin Rheumatol 2007; 19: 444-50. Bauer DC, Hunter DJ, Abramson SB, Attur M, Corr M, Felson D, et al. Classification of osteoarthritis biomarkers: a proposed approach. Osteoarthritis Cartilage 2006; 14: 723-7. Kamphorst JJ, van der Heijden R, DeGroot J, Lafeber FP, Reijmers TH, van El B, et al. Profiling of endogenous peptides in human synovial fluid by NanoLC-MS: method validation and peptide identification. J Proteome Res 2007; 6: 4388-96. Van Spil WE, DeGroot J, Lems WF, Oostveen JC, Lafeber FP. Serum and urinary biochemical markers for knee and hip-osteoarthritis: a systematic review applying the consensus BIPED criteria. Osteoarthritis Cartilage 2010; 18: 605-12. Wu J, Liu W, Bemis A, Wang E, Qiu Y, Morris EA, et al. Comparative proteomic characterization of articular cartilage tissue from normal donors and patients with osteoarthritis. Arthritis Rheum 2007; 56: 3675-84. Gobezie R, Kho A, Krastins B, Sarracino DA, Thornhill TS, Chase M, et al. High abundance synovial fluid proteome: distinct profiles in health and osteoarthritis. Arthritis Res Ther 2007; 9: R36. Ehlermann J, Weber S, Pfisterer P, Schorle H. Cloning, expression and characterization of the murine Efemp1, a gene mutated in Doyne-Honeycomb retinal dystrophy. Gene Expr Patterns 2003; 3: 441-7. Pappin DJ, Hojrup P, Bleasby AJ. Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol 1993; 3: 327-32. Sahebjam S, Khokha R, Mort JS. Increased collagen and aggrecan degradation with age in the joints of Timp3−/− mice. Arthritis Rheum 2007; 56: 905-9. 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. Kraus VB, Burnett B, Coindreau J, Cottrell S, Eyre D, Gendreau M, et al, the OARSI FDA Osteoarthritis Biomarkers Working Group. Application of biomarkers in the development of drugs intended for the treatment of osteoarthritis. Osteoarthritis Cartilage 2011; 19: 515-42. Kevorkian L, Young DA, Darrah C, Donell ST, Shepstone L, Porter S, et al. Expression profiling of metalloproteinases and their inhibitors in cartilage. Arthritis Rheum 2004; 50: 131-41. Van den Berg WB. Osteoarthritis year 2010 in review: pathomechanisms. Osteoarthritis Cartilage 2011; 19: 338-41. Kellgren JH, Lawrence JS. Radiological assessment of osteo-arthrosis. Ann Rheum Dis 1957; 16: 494-502. Albig AR, Neil JR, Schiemann WP. Fibulins 3 and 5 antagonize tumor angiogenesis in vivo. Cancer Res 2006; 66: 2621-9. 2007; 19 2004; 50 2004; 279 2011; 1 2010; 18 2006; 66 2002; 23 2007; 361 2006; 14 2007; 9 2003; 3 1986; 29 2007; 6 2006; 5 2011; 13 2010; 391 1992; 38 2011; 19 1957; 16 2007; 56 1993; 3 2005; 13 2003; 44 e_1_2_7_5_2 e_1_2_7_4_2 e_1_2_7_3_2 e_1_2_7_2_2 e_1_2_7_9_2 e_1_2_7_8_2 e_1_2_7_7_2 e_1_2_7_6_2 e_1_2_7_19_2 Zweig MH (e_1_2_7_27_2) 1992; 38 e_1_2_7_18_2 e_1_2_7_17_2 e_1_2_7_16_2 e_1_2_7_15_2 e_1_2_7_14_2 e_1_2_7_13_2 e_1_2_7_12_2 e_1_2_7_11_2 e_1_2_7_10_2 e_1_2_7_26_2 e_1_2_7_28_2 e_1_2_7_29_2 e_1_2_7_25_2 e_1_2_7_24_2 e_1_2_7_23_2 e_1_2_7_22_2 e_1_2_7_21_2 e_1_2_7_20_2 |
| References_xml | – reference: Altman R, Asch E, Bloch D, Bole G, Borenstein D, Brandt K, et al. Development of criteria for the classification and reporting of osteoarthritis: classification of osteoarthritis of the knee. Arthritis Rheum 1986; 29: 1039-49. – reference: Blackburn J, Tarttelin EE, Gregory-Evans CY, Moosajee M, Gregory-Evans K. Transcriptional regulation and expression of the dominant drusen gene FBLN3 (EFEMP1) in mammalian retina. Invest Ophthalmol Vis Sci 2003; 44: 4613-21. – reference: Felson DT. Identifying different osteoarthritis phenotypes through epidemiology. Osteoarthritis Cartilage 2010; 18: 601-4. – reference: Henrotin Y, Addison S, Kraus V, Deberg M. Type II collagen markers in osteoarthritis: what do they indicate? Curr Opin Rheumatol 2007; 19: 444-50. – reference: Mobasheri A, Henrotin Y. Biomarkers of osteoarthritis: a review of recent research progress on soluble biochemical markers, published patents and areas for future development. Recent Pat Biomark 2011; 1: 25-43. – reference: Klenotic PA, Munier FL, Marmorstein LY, Anand-Apte B. Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a binding partner of epithelial growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1): implications for macular degenerations. J Biol Chem 2004; 279: 30469-73. – reference: Deberg M, Labasse A, Christgau S, Cloos P, Bang Henriksen D, Chapelle JP, et al. New serum biochemical markers (Coll 2-1 and Coll 2-1 NO2) for studying oxidative-related type II collagen network degradation in patients with osteoarthritis and rheumatoid arthritis. Osteoarthritis Cartilage 2005; 13: 258-65. – reference: Ehlermann J, Weber S, Pfisterer P, Schorle H. Cloning, expression and characterization of the murine Efemp1, a gene mutated in Doyne-Honeycomb retinal dystrophy. Gene Expr Patterns 2003; 3: 441-7. – reference: Zweig MH, Broste SK, Reinhart RA. ROC curve analysis: an example showing the relationships among serum lipid and apolipoprotein concentrations in identifying patients with coronary artery disease. Clin Chem 1992; 38: 1425-8. – reference: Kraus VB, Burnett B, Coindreau J, Cottrell S, Eyre D, Gendreau M, et al, the OARSI FDA Osteoarthritis Biomarkers Working Group. Application of biomarkers in the development of drugs intended for the treatment of osteoarthritis. Osteoarthritis Cartilage 2011; 19: 515-42. – reference: Golightly YM, Marshall SW, Kraus VB, Renner JB, Villaveces A, Casteel C, et al. Serum cartilage oligomeric matrix protein, hyaluronan, high-sensitivity C-reactive protein, and keratan sulfate as predictors of incident radiographic knee osteoarthritis: differences by chronic knee symptoms [abstract]. Osteoarthritis Cartilage 2010; 18 Suppl 2: 62-3. – reference: Pappin DJ, Hojrup P, Bleasby AJ. Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol 1993; 3: 327-32. – reference: Wakabayashi T, Matsumine A, Nakazora S, Hasegawa M, Iino T, Ota H, et al. Fibulin-3 negatively regulates chondrocyte differentiation. Biochem Biophys Res Commun 2010; 391: 1116-21. – reference: Kamphorst JJ, van der Heijden R, DeGroot J, Lafeber FP, Reijmers TH, van El B, et al. Profiling of endogenous peptides in human synovial fluid by NanoLC-MS: method validation and peptide identification. J Proteome Res 2007; 6: 4388-96. – reference: Takei S, Hoshino T, Matsunaga K, Sakazaki Y, Sawada M, Oda H, et al. Soluble interleukin-18 receptor complex is a novel biomarker in rheumatoid arthritis. Arthritis Res Ther 2011; 13: R52. – reference: Albig AR, Neil JR, Schiemann WP. Fibulins 3 and 5 antagonize tumor angiogenesis in vivo. Cancer Res 2006; 66: 2621-9. – reference: Gobezie R, Kho A, Krastins B, Sarracino DA, Thornhill TS, Chase M, et al. High abundance synovial fluid proteome: distinct profiles in health and osteoarthritis. Arthritis Res Ther 2007; 9: R36. – reference: Kellgren JH, Lawrence JS. Radiological assessment of osteo-arthrosis. Ann Rheum Dis 1957; 16: 494-502. – reference: Sahebjam S, Khokha R, Mort JS. Increased collagen and aggrecan degradation with age in the joints of Timp3−/− mice. Arthritis Rheum 2007; 56: 905-9. – reference: Ruiz-Romero C, Blanco FJ. Proteomics role in the search for improved diagnosis, prognosis and treatment of osteoarthritis. Osteoarthritis Cartilage 2010; 18: 500-9. – reference: Vincourt JB, Lionneton F, Kratassiouk G, Guillemin F, Netter P, Mainard D, et al. Establishment of a reliable method for direct proteome characterization of human articular cartilage. Mol Cell Proteomics 2006; 5: 1984-95. – reference: Wu J, Liu W, Bemis A, Wang E, Qiu Y, Morris EA, et al. Comparative proteomic characterization of articular cartilage tissue from normal donors and patients with osteoarthritis. Arthritis Rheum 2007; 56: 3675-84. – reference: 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. – reference: Nemirovskiy OV, Dufield DR, Sunyer T, Aggarwal P, Welsch DJ, Mathews WR. Discovery and development of a type II collagen neoepitope (TIINE) biomarker for matrix metalloproteinase activity: from in vitro to in vivo. Anal Biochem 2007; 361: 93-101. – reference: Kevorkian L, Young DA, Darrah C, Donell ST, Shepstone L, Porter S, et al. Expression profiling of metalloproteinases and their inhibitors in cartilage. Arthritis Rheum 2004; 50: 131-41. – reference: Van Spil WE, DeGroot J, Lems WF, Oostveen JC, Lafeber FP. Serum and urinary biochemical markers for knee and hip-osteoarthritis: a systematic review applying the consensus BIPED criteria. Osteoarthritis Cartilage 2010; 18: 605-12. – reference: Bauer DC, Hunter DJ, Abramson SB, Attur M, Corr M, Felson D, et al. Classification of osteoarthritis biomarkers: a proposed approach. Osteoarthritis Cartilage 2006; 14: 723-7. – reference: Van den Berg WB. Osteoarthritis year 2010 in review: pathomechanisms. Osteoarthritis Cartilage 2011; 19: 338-41. – volume: 56 start-page: 905 year: 2007 end-page: 9 article-title: Increased collagen and aggrecan degradation with age in the joints of Timp3 mice publication-title: Arthritis Rheum – volume: 19 start-page: 444 year: 2007 end-page: 50 article-title: Type II collagen markers in osteoarthritis: what do they indicate? publication-title: Curr Opin Rheumatol – volume: 18 start-page: 500 year: 2010 end-page: 9 article-title: Proteomics role in the search for improved diagnosis, prognosis and treatment of osteoarthritis publication-title: Osteoarthritis Cartilage – volume: 1 start-page: 25 year: 2011 end-page: 43 article-title: Biomarkers of osteoarthritis: a review of recent research progress on soluble biochemical markers, published patents and areas for future development publication-title: Recent Pat Biomark – volume: 13 start-page: 258 year: 2005 end-page: 65 article-title: New serum biochemical markers (Coll 2‐1 and Coll 2‐1 NO2) for studying oxidative‐related type II collagen network degradation in patients with osteoarthritis and rheumatoid arthritis publication-title: Osteoarthritis Cartilage – volume: 44 start-page: 4613 year: 2003 end-page: 21 article-title: Transcriptional regulation and expression of the dominant drusen gene FBLN3 (EFEMP1) in mammalian retina publication-title: Invest Ophthalmol Vis Sci – volume: 18 start-page: 62 issue: Suppl 2 year: 2010 end-page: 3 article-title: Serum cartilage oligomeric matrix protein, hyaluronan, high‐sensitivity C‐reactive protein, and keratan sulfate as predictors of incident radiographic knee osteoarthritis: differences by chronic knee symptoms publication-title: Osteoarthritis Cartilage – volume: 5 start-page: 1984 year: 2006 end-page: 95 article-title: Establishment of a reliable method for direct proteome characterization of human articular cartilage publication-title: Mol Cell Proteomics – volume: 19 start-page: 515 year: 2011 end-page: 42 article-title: Application of biomarkers in the development of drugs intended for the treatment of osteoarthritis publication-title: Osteoarthritis Cartilage – volume: 6 start-page: 4388 year: 2007 end-page: 96 article-title: Profiling of endogenous peptides in human synovial fluid by NanoLC‐MS: method validation and peptide identification publication-title: J Proteome Res – volume: 3 start-page: 327 year: 1993 end-page: 32 article-title: Rapid identification of proteins by peptide‐mass fingerprinting publication-title: Curr Biol – volume: 18 start-page: 601 year: 2010 end-page: 4 article-title: Identifying different osteoarthritis phenotypes through epidemiology publication-title: Osteoarthritis Cartilage – volume: 16 start-page: 494 year: 1957 end-page: 502 article-title: Radiological assessment of osteo‐arthrosis publication-title: Ann Rheum Dis – volume: 3 start-page: 441 year: 2003 end-page: 7 article-title: Cloning, expression and characterization of the murine Efemp1, a gene mutated in Doyne‐Honeycomb retinal dystrophy publication-title: Gene Expr Patterns – volume: 279 start-page: 30469 year: 2004 end-page: 73 article-title: Tissue inhibitor of metalloproteinases‐3 (TIMP‐3) is a binding partner of epithelial growth factor‐containing fibulin‐like extracellular matrix protein 1 (EFEMP1): implications for macular degenerations publication-title: J Biol Chem – volume: 361 start-page: 93 year: 2007 end-page: 101 article-title: Discovery and development of a type II collagen neoepitope (TIINE) biomarker for matrix metalloproteinase activity: from in vitro to in vivo publication-title: Anal Biochem – volume: 391 start-page: 1116 year: 2010 end-page: 21 article-title: Fibulin‐3 negatively regulates chondrocyte differentiation publication-title: Biochem Biophys Res Commun – volume: 18 start-page: 605 year: 2010 end-page: 12 article-title: Serum and urinary biochemical markers for knee and hip‐osteoarthritis: a systematic review applying the consensus BIPED criteria publication-title: Osteoarthritis Cartilage – volume: 38 start-page: 1425 year: 1992 end-page: 8 article-title: ROC curve analysis: an example showing the relationships among serum lipid and apolipoprotein concentrations in identifying patients with coronary artery disease publication-title: Clin Chem – volume: 50 start-page: 131 year: 2004 end-page: 41 article-title: Expression profiling of metalloproteinases and their inhibitors in cartilage publication-title: Arthritis Rheum – volume: 29 start-page: 1039 year: 1986 end-page: 49 article-title: Development of criteria for the classification and reporting of osteoarthritis: classification of osteoarthritis of the knee publication-title: Arthritis Rheum – volume: 23 start-page: 3445 year: 2002 end-page: 56 article-title: Mass spectrometric proteome analyses of synovial fluids and plasmas from patients suffering from rheumatoid arthritis and comparison to reactive arthritis or osteoarthritis publication-title: Electrophoresis – volume: 9 start-page: R36 year: 2007 article-title: High abundance synovial fluid proteome: distinct profiles in health and osteoarthritis publication-title: Arthritis Res Ther – volume: 66 start-page: 2621 year: 2006 end-page: 9 article-title: Fibulins 3 and 5 antagonize tumor angiogenesis in vivo publication-title: Cancer Res – volume: 56 start-page: 3675 year: 2007 end-page: 84 article-title: Comparative proteomic characterization of articular cartilage tissue from normal donors and patients with osteoarthritis publication-title: Arthritis Rheum – volume: 19 start-page: 338 year: 2011 end-page: 41 article-title: Osteoarthritis year 2010 in review: pathomechanisms publication-title: Osteoarthritis Cartilage – volume: 13 start-page: R52 year: 2011 article-title: Soluble interleukin‐18 receptor complex is a novel biomarker in rheumatoid arthritis publication-title: Arthritis Res Ther – volume: 14 start-page: 723 year: 2006 end-page: 7 article-title: Classification of osteoarthritis biomarkers: a proposed approach publication-title: Osteoarthritis Cartilage – ident: e_1_2_7_10_2 doi: 10.1002/art.1780290816 – ident: e_1_2_7_15_2 doi: 10.1002/1522-2683(200210)23:19<3445::AID-ELPS3445>3.0.CO;2-J – ident: e_1_2_7_9_2 doi: 10.1016/j.joca.2010.08.019 – ident: e_1_2_7_11_2 doi: 10.1136/ard.16.4.494 – ident: e_1_2_7_8_2 doi: 10.1016/S1063-4584(10)60151-3 – ident: e_1_2_7_4_2 doi: 10.1016/j.joca.2010.01.012 – ident: e_1_2_7_13_2 doi: 10.1016/j.joca.2009.11.012 – ident: e_1_2_7_28_2 doi: 10.1186/ar3295 – ident: e_1_2_7_7_2 doi: 10.1016/j.joca.2004.12.002 – ident: e_1_2_7_16_2 doi: 10.1186/ar2172 – ident: e_1_2_7_2_2 doi: 10.1016/j.joca.2010.01.007 – volume: 38 start-page: 1425 year: 1992 ident: e_1_2_7_27_2 article-title: ROC curve analysis: an example showing the relationships among serum lipid and apolipoprotein concentrations in identifying patients with coronary artery disease publication-title: Clin Chem doi: 10.1093/clinchem/38.8.1425 – ident: e_1_2_7_12_2 doi: 10.1016/0960-9822(93)90195-T 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| Snippet | Objective
This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and... This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and quantify... Objective This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect and... OBJECTIVE: This study was undertaken to identify new biomarkers of osteoarthritis (OA) by proteomics analysis and to develop specific immunoassays to detect... |
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| SubjectTerms | Adult Aged Aged, 80 and over Arthroplasty, Replacement, Knee Biological and medical sciences Biomarkers Biomarkers - urine Cartilage, Articular - metabolism Chondrocytes - metabolism Diseases of the osteoarticular system Extracellular Matrix Proteins - urine Female Human health sciences Humans Joint replacement surgery Knee Joint - metabolism Knee Joint - surgery Medical sciences Miscellaneous. Osteoarticular involvement in other diseases Osteoarthritis Osteoarthritis, Knee - diagnosis Osteoarthritis, Knee - surgery Osteoarthritis, Knee - urine Peptides Proteomics Rheumatology Rhumatologie Sciences de la santé humaine |
| Title | Fibulin 3 peptides Fib3-1 and Fib3-2 are potential biomarkers of osteoarthritis |
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