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J R Delanghe

Publications and source records attributed to J R Delanghe.

50 records · Page 3Linked to original sources
PubMed1992

Acute myocardial infarction size and myoglobin release into serum.

The kinetics of myoglobin release after acute myocardial infarction were studied. Various algorithms for calculation of infarct size, based on immunonephelometric determination of myoglobin and cumulative myoglobin release into the circulation were compared. The cumulative myoglobin release and maximal serum myoglobin concentration were compared with various measures of infarct size: cumulative release of creatine kinase, electrocardiographic changes, and left ventricular ejection fraction. After acute myocardial infarction, time to peak for myoglobin in serum was correlated with time to peak for creatine kinase (r = 0.645). On average, the myoglobin concentration peaked 8.8 h earlier than creatine kinase activity. The rate of elimination of myoglobin showed a large variation (0.041-0.628 h-1) and was not correlated with the elimination rate of creatine kinase. The elimination rate of myoglobin after acute myocardial infarction was shown to depend on the patient's age and infarct size. The elimination constant of myoglobin is preferably estimated on an individual basis in large and complicated infarctions. Cumulative myoglobin release correlated with algorithms based on the cumulative release of creatine kinase (r = 0.622) and its isoenzyme MB (r = 0.660), and to a lesser extent with the residual left ventricular ejection fraction (r = 0.513) and the sum of ST-segment deviations on electrocardiography (r = 0.469). Maximal myoglobin values in serum correlated moderately with the calculated infarct size (r = 0.488; based on creatine kinase-MB) and electrocardiographic changes (r = 0.554). In combination with fast immunological methods for myoglobin determination, myoglobin peak height offers the advantage of providing reliable results within 12 h after onset of symptoms.(ABSTRACT TRUNCATED AT 250 WORDS)

Aged↗
PubMed1990

Mass concentration measurements of creatine kinase BB isoenzyme as an index of brain tissue damage.

A new two-site immunoenzymometric method using monoclonal antibodies was developed for measuring CK-BB mass concentrations in cerebrospinal fluid (CSF). Within- and between-assay coefficient of variation values for the method varied between 6 and 9%. Assay results are not affected by presence of sulfate and sialic acid groups on the enzyme. In comparison to catalytic activity measurements, a steady decline in the enzyme's specific activity was observed after acute head trauma. Repetitive measurements of CK-BB mass concentration in cerebrospinal fluid during the first 24 h after trauma enabled the estimation of brain lesion size. Clinical outcome of acute head trauma patients evaluated by Glasglow Outcome Scale, correlated well with cumulative CK-BB release after trauma. Also in neonates, CK-BB determinations in CSF correlated well with clinical findings.

Adolescent↗
PubMed1990

Post-transcriptional modification of serum creatine kinase in infected intensive care patients.

Low creatine kinase (CK) activities in serum are associated with high fatality rates in intensive care patients. The underlying mechanisms for this phenomenon were investigated. No correlation was found with other biochemical markers of inflammation (CRP, alpha-1 acid glycoprotein, alpha-2 macroglobulin). In the patients' serum a factor is described which is capable of increasing the activation energy of normal CK-MM, indicating molecular changes in CK-structure. This factor is likely to be an enzyme which is present in liver tissue and in fibroblasts. Similar results were obtained after in vitro treatment of normal serum samples with arylsulfatase. Furthermore, bacterial strains isolated in the serum of intensive care patients were found to alter human CK structure. In the investigated patient group, changes in CK activation energy are influenced by serum factors other than carboxypeptidase N activity.

Adolescent↗
PubMed1990

Enzymatic erythrocyte creatine determinations as an index for cell age.

Creatine concentration in red blood cells was determined after ammoniumsulfate precipitation on a clear hemoglobin-free filtrate with a new enzymatic assay making use of bacterial creatinase. The method described is more specific than Griffiths' method and can easily be mechanised and adapted for use in a routine laboratory using classical automated equipment. By contrast with Griffiths' method no significant interferences of amino acids and creatine-like molecules were found. Reference values for this method were 0.379 +/- 0.076 mmol/l. In patients with high turnover of erythrocytes, e.g. haemodialysis patients (0.529 +/- 0.122 mmol/l), and renal insufficiency patients (0.565 +/- 0.145 mmol/l), significantly increased creatine concentration in erythrocytes were observed. Low erythrocyte creatine concentrations were found in chronic ambulatory dialysis patients (0.311 +/- 0.042 mmol/l).

Adult↗
PubMed1990

Quantitative nephelometric assay for determining myoglobin evaluated.

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.

Adult↗
PubMed1990

Mass concentration and activity concentration of creatine kinase isoenzyme MB compared in serum after acute myocardial infarction.

We compared three current methods (immunoinhibition, "Isomune-CK" immunoprecipitation, and the Tandem-E CKMB II immunoenzymometric assay) for determination of creatine kinase (CK; EC 2.7.3.2) isoenzyme MB in serum. Although results inter-correlated well, the immunoinhibition assay gave higher activity values. Atypical CK forms did not interfere with the immunoprecipitation and immunoenzymometric methods. In acute myocardial infarction the catalytic properties of CK decreased with the enzyme's age, as reflected by a steady increase in activation energy of the catalyzed reaction. In septicemia patients with very low CK and CK-MB catalytic activity, mean CK-MB mass concentration exceeded the upper reference limit, suggesting an increased rate of loss of activity concentration in these patients' sera. Because of the assay's lesser susceptibility to conformational changes at the active site of the enzyme, we suggest that measurement of CK-MB mass concentration is better suited for infarct sizing than measurement of catalytic activity.

Acute Disease↗
PubMed1989

Activation energy and lectin affinity chromatography of gamma-glutamyltransferase as a marker for enzyme heterogeneity.

Lectin affinity chromatography of gamma-glutamyl transferase (GGT,EC 2.3.2.2) is able to detect differences in the carbohydrate moiety of the enzyme. Binding of tissue GGT towards lectins is significantly different from serum GGT, showing increased galactosylation in tissue forms. Kidney GGT is less glycosylated than GGT from other tissues (liver, pancreas, prostate, vesiculae seminales). Increases in sialic acid content of GGT are associated with an increase in the activation energy of the catalyzed reaction. Differences in galactose, fucose and N-acetylhexosamine content induce much smaller effects on activation energy. In liver diseases, serum GGT is characterized by an altered affinity against lectins recognizing galactose, fucose and N-acetyglucosamine and by increased activation energy. In patients with liver disease, use of fixed temperature conversion factors can lead to erroneous calculations of serum GGT enzyme activity (errors up to 13.3%).

Adult↗
PubMed1989

Anti-myosin humoral immune response following cardiac injury.

A sensitive and highly specific ELISA assay was developed to determine the anti-myosin humoral immune response (AMA) in various heart diseases: acute viral myocarditis, infective endocarditis, acute myocardial infarction, and valve and coronary bypass surgery. The mean study entry AMA titer of each patient group was already significantly increased compared with age matched controls. During further follow-up (90 d) all the groups except for endocarditis showed a significant increase of AMA titer compared with their entry titer. Anti-myosin antibody titer were higher after cardiac surgery than after myocardial infarction or inflammatory heart disease. These results suggest that anti-myosin immune response is not limited to infectious processes in which the pathogen induces antibodies which cross-react with heart constituents but is merely caused by direct cardiac injury. Myosin as a major compound of heart cellular proteins turned out to be a good candidate to trigger immune response after cardiac injury.

Adolescent↗
PubMed1989

Measurement of autoimmune response against collagen types I, III, and IV by enzyme-linked immunosorbent assay, and its application in infective endocarditis.

In these enzyme-linked immunosorbent assays for determination of autoantibodies (IgG, IgM) against collagen type I (ACA I), III (ACA III), and IV (ACA IV), we use commercially available antigen preparations. Inhibition curves showed limited cross-reactivity between these different collagen preparations, the major interference being observed after addition of collagen type III in the ACA I procedures. Imprecision (CVs) for high- and low-titer samples ranged between 1.5% and 7.9% (within-run) and 5.5% and 12.7% (between-run) for ACA I, between 2.2-8.7% and 4.5-10.7% for ACA III, and between 1.3-5.9% and 7.4-11.6% for ACA IV. Significantly increased humoral immune response against collagen types I and III (P less than 0.001) could be demonstrated during the first month of infective endocarditis. In contrast, only borderline increases, however constant, of autoimmune response against basement-membrane collagen (ACA IV) were noticed during 90 days of follow-up.

Adult↗
PubMed1987

Lectin-affinity chromatography of serum gamma-glutamyltransferase in liver disease.

The variation of the carbohydrate chain of gamma-glutamyltransferase was studied in 45 liver patients by means of lectin affinity chromatography. Five lectins were used: concanavalin A, Ricinus communis I and II, Maclura pomifera and Ulex europaeus agglutinin. The binding towards Con A was shown to be independent from the binding towards the other lectins. Parallel variations of binding results against the galactose- and fucose-recognizing lectins were obtained. In liver steatosis, the binding results were comparable to those obtained in normal patients. Cirrhosis and metastasis patients showed a decreased binding towards Con A, while the binding against the various galactose- and fucose-recognizing lectins was increased. After neuraminidase treatment, an increased affinity towards all lectins was observed. However, differences in RCA I and RCA II binding between patients and controls still persisted. Besides sialic acid, also galactose and fucose residues contribute to serum gamma-glutamyltransferase heterogeneity.

Adult↗