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Biomedical subjects

C Larue

Publications and source records attributed to C Larue.

At least 37 records · Page 2Linked to original sources
PubMed1992

New monoclonal antibodies as probes for human cardiac troponin I: epitopic analysis with synthetic peptides.

Forty monoclonal antibodies (MAbs) specific for human cardiac troponin I (TnI) were selected to develop a new alternative for specific biological diagnosis of acute myocardial infarction. Using an immunoenzymatic sandwich assay, these MAbs were employed in the mapping of human cardiac TnI and showed six different epitopes. Parts of the TnI peptide sequences were synthesised; the sequences were chosen from the published sequences of mammalian TnI. Immunological assays showed that 8 out of 40 MAbs recognised a RAYATEPHAK (P2) N-terminus cardiac-specific sequence of human TnI. The information obtained from epitopic mapping of TnI and the properties of the peptides allowed pairs of MAbs to be selected for the development of a future specific TnI assay.

Amino Acid Sequence↗
PubMed1992

[Evaluation of the size of thrombolysed myocardial infarction by serum myosin determination].

The prognosis of myocardial infarction is very dependent on the size of the infarct. The measurement of the infarct size after thrombolysis remains difficult despite the large number of methods available, all of which have drawbacks. This parameter is however essential to assess prognosis and the efficacy of thrombolytic therapy. Serum beta heavy chain myosin determination is a recently introduced method of evaluating infarct size; there are relatively few published studies, especially concerning post-thrombolytic patients. A prospective study was undertaken in 40 patients (37 men and 3 women: average age 55.6 years) with a primary myocardial infarction treated by thrombolysis. Myosin levels (peak and area under curve of 5 samples in 10 days) were compared with other methods of assessing infarct size: electrocardiogram (number of leads with Q waves, ST segment analysis), cardiac enzymes (peak and release integrals of CK abd LDH), contrast ventriculography (segmental asynergy score, ejection fraction), coronary angiography and resting MIBI myocardial scintigraphy. The peak and integral of myosin release correlated well with the other methods (p < 0.01): a correlation was particularly apparent between the integral of myosin release and MIBI scintigraphy scores (r = 0.77, p < 0.001). Complex myosin release kinetics were observed significantly more often in patients with large infarcts (p < 0.01) or in those with occlusion of the artery responsible for infarction at coronary angiography on the 6th day (p = 0.001). In conclusion, with 5 blood samples over a 10 day period, it is possible to estimate the infarct size after thrombolysis in everyday cardiological practice: this method could help identify high risk subjects (complex kinetics of myosin release and high peak myosin levels) and also could be used to assess efficacy of thrombolytic therapy in large scale trials.

Adult↗
PubMed1991

Imaging of myocardial infarction in dogs and humans using monoclonal antibodies specific for human myosin heavy chains.

The use of three different monoclonal antibodies specific for human ventricular myosin heavy chains in the visualization of the location and extent of necrosis in dogs with experimental acute myocardial infarction and in humans is described. Using a classic immunohistochemical method or ex vivo analysis of heart slices in dogs with acute myocardial infarction subjected to intravenous injection of unlabeled antimyosin antibodies or antimyosin antibodies labeled with indium-111, it was observed that all antibody fragments specifically reached the targeted necrotic zone less than 2 h after antibody injection and remained bound for up to 24 h. In a limited but significant number of cases (5 of the 12 humans and 11 of 43 dogs), it was possible to image the necrotic zone in vivo as early as 2 to 4 h after antibody injection. In other cases, individual blood clearance variations retarded or even prevented in vivo necrosis detection. Higher antimyosin fixation values were obtained in the necrotic zones in dogs with a rapid blood clearance relative to that of the other dogs. It is concluded that antimyosin antibodies always reached necrotic areas within 2 h. If blood clearance was rapid, in vivo imaging of the necrotic area was possible 2 to 6 h after necrosis, even in humans. In some cases, however, uncontrolled individual variations in the timing required for sufficient blood clearance hampered this rapid in vivo detection of myocardial necrosis.

Aged↗
PubMed1991

Immunoradiometric assay of myosin heavy chain fragments in plasma for investigation of myocardial infarction.

Estimation of the extent and location of infarct is important for the prognosis and hence therapeutic strategy in patients with acute myocardial infarction (AMI). Because cardiac myosin is the major structural protein of the myocardium, and may thus reflect the extent of injured tissue, we established a new sensitive immunoradiometric assay, using a pair of monoclonal antibodies (Mabs) that specifically bind the myosin heavy chain fragments liberated from the myocyte into plasma after a heart attack. A first Mab is linked to a magnetic solid phase. A second Mab, radiolabeled with 125I, is used to detect myosin trapped on the solid phase by the first Mab during a 3-h incubation. This assay can detect 10 micro-units of myosin per liter and is highly reproducible.

Antibodies, Monoclonal↗
PubMed1990

Assay of serum cardiac myosin heavy chain fragments in patients with acute myocardial infarction: determination of infarct size and long-term follow-up.

To evaluate the correlation between myosin heavy chain release and the necrosis mass, serum levels of myosin heavy chain fragments were determined serially in 55 patients with acute myocardial infarction. Eight of these patients were successfully treated with thrombolytic agents: the others were not treated. The same myosin titration was applied to the sera of 25 dogs with an experimental myocardial infarction. Six of the dogs were successfully treated with thrombolytic agents. The time courses of the myosin concentrations are typical and monophasic for all patients with a noncomplex myocardial infarction. The values for the kinetic parameters of myosin release are comparable to those previously reported. We have now determined that cumulative myosin release significantly correlates with cumulative creatine kinase (CK), CK-MB, and lactate dehydrogenase release, as well as with thallium-201 distribution, as determined for different patient groups. Thrombolytic treatment does not seem to qualitatively upset myosin kinetics. The results obtained in dogs with or without thrombolysis conclusively indicate that myosin release is a quantitative index of the necrosis mass. From a practical point of view, a few serial determinations of serum levels of myosin heavy chains are enough to estimate the necrosed mass in patients with acute myocardial infarction. More generally, serum myosin titration could be useful in detecting any cardiac disturbance involving myocardial injury resulting in membrane leakage of cardiac cells.

Adult↗
PubMed1989

Myosin: a highly sensitive indicator of myocardial necrosis after cardiac operations.

Plasma levels of ventricular myosin fragments, determined with monoclonal antibodies to myosin heavy chains, were studied in 27 patients after cardiac operations (17 aorta-coronary bypass grafts and 10 valve replacements) to assess their possible role as a marker of perioperative myocardial necrosis. Five patients had perioperative myocardial necrosis after aorta-coronary bypass grafts as indicated by changes in the electrocardiogram and elevated levels of the MB isoenzyme of creatine kinase. Six more patients were also studied after thoracic operations performed by the same sternotomy approach. After cardiac operations, myosin levels increased from postoperative day 3 and reached peak values on day 7. Peak myosin values in patients with perioperative myocardial necrosis after aorta-coronary bypass grafting were significantly higher than in patients after an identical operation but without perioperative myocardial infarction (3793 +/- 592 versus 369 +/- 47 ng/ml; p less than 0.001). These results suggest that plasma myosin is a sensitive marker of myocardial necrosis. Furthermore, peak plasma levels of ventricular myosin after coronary bypass grafting without myocardial infarction (mean value 369 +/- 47 ng/ml) were not significantly different from peak levels after thoracic operations (mean value 253 +/- 52 ng/ml), whereas they were significantly higher after valve replacement (mean value 794 +/- 149 ng/ml; p less than 0.01). These results indicate that a certain degree of myocardial necrosis occurs during value replacement that is undetectable by the usual diagnostic criteria for perioperative myocardial infarction. We conclude that the plasma level of ventricular myosin fragments is a more specific and accurate marker of perioperative myocardial necrosis than changes in the electrocardiogram or elevated creatine kinase MB levels. Therefore the detection of myosin fragments, which appear in the serum on the third day after cardiac operations, may be useful for precise comparisons of different techniques of myocardial protection.

Biomarkers↗
PubMed1986

An extracorporeal hollow-fiber reactor for phenylketonuria using immobilized phenylalanine ammonia lyase.

A hollow-fiber hemodialyzer with immobilized phenylalanine ammonia lyase was tested in vitro for depletion of blood phenylalanine in a recirculating system. A sustained reduction of phenylalanine was obtained in less than 1 h. The product of phenylalanine deamination, trans-cinnamic acid, is a nontoxic compound metabolized to benzoic acid by the liver and eliminated in the urine as hippuric acid. As a model, this reactor may be relevant not only for the short-term management of hyperphenylalaninemia (particularly in pregnant phenylketonuric mothers), but for other metabolic diseases as well, provided that a biocatalyst effective on the accumulating substance is available.

Ammonia-Lyases↗
PubMed1985

Suitable hollow fibre immunobioreactors for specific ex vivo removal of antibodies and antigens from plasma.

Studies were undertaken to determine the applicability and effectiveness of a new immunoadsorbent, constituted of cellulose hollow fibres chemically modified (BrCN) to link selected proteins. The method has been assayed on a simple model of antibody elimination: myeloma IgG or BSA as antigens were covalently linked to cellulose; such an immunoadsorbent can selectively and efficiently deplete circulating antibodies in vitro and ex vivo (on immunized dogs) from whole blood, without releasing linked protein into the hosts' circulation. The original approach of using this method to remove antibodies has been extended to specifically remove antigens (for this purpose, antibodies were conjugated to cellulose), in order to investigate an immunoadsorption therapy in familial hypercholesterolemia, characterized by a plasmatic overload of low-density-lipoproteins (LDL), of which apolipoprotein B is the major protein. After covalent linkage of isolated anti-apolipoprotein B antibodies to cellulose, human plasma LDL levels were effectively and specifically reduced by this procedure.

Animals↗
PubMed1975

Prandial drinking and the disruption of meal patterns in olfactory bulbectomized rats.

In order to determine the cause of the disrupted feeding pattern in bulbectomized and recovered LH lesioned rats and to study the role of prandial drinking in producing this feeding pattern, feeding and drinking patterns were simultaneously recorded in these lesioned preparations. It was found that in normal rats drinking occurred mainly before and after the meals. In bulbectomized rats, drinking occurred also before and after the meal, but the main part of the meal associated takes place during the numerous short pauses within the meal. In LH recovered rats the meal associated drinking occurred in a very rapid alternation between eating and drinking during feeding bouts (prandial drinking) and not during the meal pauses. It is suggested that the nibbling pattern seen in LH recovered rats as well as in bulbectomized rats is not due to the prandial drinking but results from the loss of an olfactory input to the LH area.

Animals↗
PubMed1975

[Comparison of the effects of anosmia induced by either peripheral lesion or bulbectomy upon the feeding pattern of the rat (author's transl)].

In order to support the contention that the feeding pattern seen after olfactory bulb removal is due to a sensory loss, the feeding pattern of rats was studied after a peripheral chemical lesion of the olfactory mucosa. A conditioned smell aversion procedure was used to assess the occurence and duration of anosmia after the topical application of zinc sulfate to the olfactory mucosa. It was found that the sensory deficit induced by the peripheral lesion lasted from four to six days. The occurrence of the disrupted feeding pattern in the peripherally lesioned rats coincided in time with the short period of anosmia. Thus, the disruption of the feeding pattern after bulbectomy and after lesions of the central olfactory pathways is clearly the result of anosmia and not of the loss of other non-sensory functions of the olfactory bulbs.

Animals↗