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See detailMonomeric calgranulins measured by SELDI-TOF mass spectrometry and calprotectin measured by ELISA as biomarkers in arthritis
De Seny, Dominique ULg; Fillet, Marianne ULg; Ribbens, Clio ULg et al

in Clinical Chemistry (2008), 54

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 ... [more ▼]

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. [less ▲]

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See detailOral contraception and lipid peroxidation
De Groote, D.; Pincemail, Joël ULg; Defraigne, Jean-Olivier ULg et al

in Clinical Chemistry (2007, June), 53(6, Suppl. S), 30-30

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See detailDiagnostic accuracy of blood lactate-to-pyruvate molar ratio in the differential diagnosis of congenital lactic acidosis.
DEBRAY, François-Guillaume ULg; Mitchell, Grant A; Allard, Pierre et al

in Clinical Chemistry (2007), 53(5), 916-21

BACKGROUND: Although the blood lactate-to-pyruvate (L:P) molar ratio is used to distinguish between pyruvate dehydrogenase deficiency (PDH-D) and other causes of congenital lactic acidosis (CLA), its ... [more ▼]

BACKGROUND: Although the blood lactate-to-pyruvate (L:P) molar ratio is used to distinguish between pyruvate dehydrogenase deficiency (PDH-D) and other causes of congenital lactic acidosis (CLA), its diagnostic accuracy for differentiating between these 2 types of CLA has not been evaluated formally. METHODS: We conducted a retrospective study of all patients followed for mitochondrial diseases between 1985 and 2005 in a tertiary care pediatric hospital. RESULTS: At the recommended cut point of approximately 25, individual median L:P ratio demonstrated low sensitivity and specificity (77% and 91%, respectively) for differentiating between patients with enzymatically proven PDH-D (n = 11) and those with mitochondrial disease but normal pyruvate dehydrogenase (PDH) activity (non-PDH; n = 35). We observed a strong positive association between L:P ratio and blood lactate in non-PDH CLA, whereas this association was weak in PDH-D CLA. Consequently, patient classification based on median L:P ratio showed improved diagnostic accuracy at higher lactate concentrations: for lactate <2.5 mmol/L the area under the ROC curve was not statistically different from 0.5 (P = 0.3), whereas it was statistically different for lactate >2.5 mmol/L. In the 2.5 to 5.0 mmol/L lactate category, the sensitivity and specificity at an optimal cut point of 18.4 were 93% (95% CI, 77%-99%) and 71% (95% CI, 20%-96%), respectively; for lactate >5.0 mmol/L, with an optimal cut point of 25.8, sensitivity and specificity were 96% (95% CI, 77%-99%) and 100% (95% CI, 59%-100%), respectively. CONCLUSION: Usefulness of the L:P ratio for differentiating non-PDH and PDH-D types of CLA increases at higher lactate concentrations. [less ▲]

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See detailCombined locked nucleic acid and molecular beacon technologies for sensitive detection of the JAK2(V617F) somatic single-base sequence variant
Sidon, P.; Heimann, P.; Lambert, Frédéric ULg et al

in Clinical Chemistry (2006), 52(7), 1436-1438

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See detailDesign of an ELISA specific for the measurement of equine neutrophil myeloperoxidase in biological fluids
Couderc, S.; Franck, Thierry ULg; Bougoussa, M. et al

in Clinical Chemistry (2005), 51(Suppl. 6), 211-212

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See detailImmunoquantitative PCR for prion protein detection in sporadic Creutzfeldt-Jakob disease.
Gofflot, Stéphanie ULg; Deprez, Manuel ULg; Elmoualij, Benaïssa ULg et al

in Clinical Chemistry (2005), 51(9), 1605-11

BACKGROUND: The most common human prion disorder is Creutzfeldt-Jakob disease (CJD); it includes sporadic, familial, iatrogenic, and variant subtypes. Diagnostic tests aim at detection with the highest ... [more ▼]

BACKGROUND: The most common human prion disorder is Creutzfeldt-Jakob disease (CJD); it includes sporadic, familial, iatrogenic, and variant subtypes. Diagnostic tests aim at detection with the highest specificity of very small deposits of abnormal prion protein (PrP). METHODS: We used immunoquantitative PCR (iqPCR) to detect proteinase K-resistant PrP (PrPRes) in tissue from the middle frontal gyrus of 7 patients with sporadic CJD and 7 non-CJD cases. We compared iqPCR with routine optimized ELISA, Western blotting, and immunohistochemical analyses. RESULTS: The 4 methods showed similar 100% sensitivity and specificity for the diagnosis of CJD. Along with high specificity, however, iqPCR had a threshold for PrP(Res) detection at least 10-fold lower than that of the classic ELISA. CONCLUSIONS: iqPCR is a new method for PrPRes detection that combines 100% specificity with a detection threshold at least 10-fold lower than classic techniques. This method may improve the detection of minute PrPRes deposits in tissues and body fluids and thus be useful for diagnostic and sterilization applications. [less ▲]

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See detailInterassay and interobserver variability in the detection of anti-neutrophil cytoplasmic antibodies in patients with ulcerative colitis.
Joossens, Sofie; Daperno, Marco; Shums, Zakera et al

in Clinical Chemistry (2004), 50(8), 1422-5

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See detailPrognostic significance of increased baseline plasma troponin I levels in PTCA patients
Chapelle, Jean-Paul ULg; Legrand, Victor ULg; Gielen, Jacques

in Clinical Chemistry (2000), 46(suppl), 82

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See detailEvaluation of the homocysteine assay on the Abbott IMx
Chapelle, Jean-Paul ULg; Lutteri, Laurence ULg; Gielen, J.

in Clinical Chemistry (1999), 45(6), 134

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See detailA study of within-laboratory variability based on data from the Belgian External Quality Assessment (EQA) programme
Zhang, Lixin; Albert, Adelin ULg; Hamers, N. et al

in Clinical Chemistry (1999), 45(6)

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See detailFirst Direct Assay for Intact Human Proinsulin
Houssa, P.; Dinesen, B.; Deberg, Michelle ULg et al

in Clinical Chemistry (1998), 44(7), 1514-9

We describe a sensitive two-site sandwich enzyme-linked immunosorbent assay for the measurement of intact human proinsulin in 100 microL of serum or plasma. The assay is based on the use of two monoclonal ... [more ▼]

We describe a sensitive two-site sandwich enzyme-linked immunosorbent assay for the measurement of intact human proinsulin in 100 microL of serum or plasma. The assay is based on the use of two monoclonal antibodies specific for epitopes at the C-peptide/insulin A chain junction and at the insulin B chain/C-peptide junction, respectively. Cross-reactivities with insulin, C-peptide, and the four proinsulin conversion intermediates were negligible. The detection limit in buffer was 0.2 pmol/L (3 standard deviations from zero). The working range was 0.2-100 pmol/L. The mean intra- and interassay coefficients of variation were 2.4% and 8.9%, respectively. The mean recovery of added proinsulin was 103%. Dilution curves of 40 serum samples are parallel to the proinsulin calibration curve. Proinsulin concentrations in 20 fasting healthy subjects were all above the limit of detection: median (range), 2.7 pmol/L (1.1-6.9 pmol/L). Six fasting non-insulin-dependent diabetes mellitus and five insulinoma patients had proinsulin concentrations significantly higher than healthy subjects: median (range), 7.7 pmol/L (3.2-18 pmol/L) and 153 pmol/L (98-320 pmol/L), respectively. [less ▲]

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See detailHighly Specific Radioimmunoassay for Human Insulin Based on Immune Exclusion of All Insulin Precursors
Deberg, Michelle ULg; Houssa, P.; Frank, B. H. et al

in Clinical Chemistry (1998), 44(7), 1504-13

We describe a rapid and simple insulin RIA in which proinsulin and conversion intermediates do not interfere. Three monoclonal antibodies (S1, S2, and S53) were selected for their specificity (directed ... [more ▼]

We describe a rapid and simple insulin RIA in which proinsulin and conversion intermediates do not interfere. Three monoclonal antibodies (S1, S2, and S53) were selected for their specificity (directed, respectively, against the B10 region, the junction between A chain and C-peptide, and the junction between B chain and C-peptide), their affinity constant (approximately 10(10) L/mol), and their interactive properties in mixture. S2 and S53 were able to bind simultaneously to the same proinsulin molecule, whereas neither could bind simultaneously with S1. Preincubation of serum samples with an excess of S2 resulted in capture of proinsulin and conversion intermediates modified at the junction between B chain and C-peptide into immune complexes that no longer reacted with S1. Similarly, preincubation with S53 prevented proinsulin and conversion intermediates modified at the junction between A chain and C-peptide from reacting with S1. Preincubation with an excess of both S2 and S53 left insulin as the sole reactant with S1. Thus, separation of insulin precursors from insulin by mutually exclusive antibodies is feasible, and on the basis of this new principle, a highly specific RIA for insulin was designed. The detection limit was 11 pmol/L, and the inter- and intraassay coefficients of variation were 11% and 5%, respectively. The potential of the assay for use in clinical studies was verified by application to serum samples from control subjects and patients with diabetes or insulinoma. [less ▲]

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See detailAnalytical and clinical evaluation of automated immunoassays for serum CK-MB and myoglobin using the OPUS MAGNUM analyser
Chapelle, Jean-Paul ULg; Spronck, Thierry; Ferir, Anne-Marie

in Clinical Chemistry (1995), 41

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See detailEvaluation of a rapid turbidimetric myoglobin immunoassay
Lammers, M.; Dati, F.; Kapmeyer, W. H. et al

in Clinical Chemistry (1991), 37

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See detailQuantitative nephelometric assay for determining myoglobin evaluated
Delanghe, J. R.; Chapelle, Jean-Paul ULg; Vanderschueren, S. C.

in Clinical Chemistry (1990), 36(9), 1675-8

A recently introduced automated nephelometric immunoassay involving shell/core particles for determination of myoglobin (Behringwerke) was evaluated with the BNA Nephelometer. Method precision was good ... [more ▼]

A recently introduced automated nephelometric immunoassay involving shell/core particles for determination of myoglobin (Behringwerke) was evaluated with the BNA Nephelometer. Method precision was good: the intra-assay CV varied between 1.5% and 6.1%; with daily calibration, the interassay CV ranged between 1.5% and 7.5%. For usual sample dilutions, the assay response varied linearly with myoglobin concentrations up to 23.1 nmol/L. After automatic dilution by the instrument, concentrations up to 2310 nmol/L could be measured without high-dose "hook" effect. Further manual dilution allowed measurement of myoglobin concentrations up to 26,000 nmol/L. Calibration was stable for at least seven days. We detected no significant interferences from hemoglobin, haptoglobin, bilirubin, iodine-containing contrast media, and rheumatoid factors. Treating lipemic samples with Lipoclean (Behringwerke) decreased test results. Simultaneously drawn serum and plasma samples from the same subject showed no consistent differences in myoglobin concentrations. The mean reference myoglobin concentration was 1.380 (SD 0.82) nmol/L for men and 0.878 (SD 0.45) nmol/L for women. In patients with renal insufficiency, serum creatinine values were moderately related to serum myoglobin values (r = 0.465). Although a commercial radioimmunoassay (Byk-Sangtec) and the nephelometric assay intercorrelated well (r = 0.929), values obtained by nephelometry were significantly lower (P less than 0.05). By both assays, results for heart and skeletal muscle tissue extracts showed no correlation, a finding that suggests the existence of multiple forms of myoglobin in human tissues. We conclude that immunonephelometry is a rapid, practical, and reliable method for measuring myoglobin in serum. [less ▲]

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See detailDetermination of myoglobin in serum by kinetic turbidimetry, using the turbitimesystem
Chapelle, Jean-Paul ULg; El Allaf, M.

in Clinical Chemistry (1990), 36(6), 1193

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