Distribution, prevalence and intensity of Anguillicola crassus (Nematoda) infection in Anguilla anguilla in the Republic of Ireland.

This study is the first comprehensive documentation of the geographical range of Anguillicola crassus in its host, the European eel Anguilla anguilla, in the Republic of Ireland. The prevalence and intensity of infections across 234 sites and 93 river basins in Ireland comprising rivers, lakes and transitional waters (estuaries) were analysed. While only 32% of the river basins were affected by this nematode, they correspond to 74% of the total wetted area. Significant differences in infection levels among water body types were found with lakes and transitional waters yielding the highest values, which can be attributed to the proportions of juvenile (total length, L(T) < 300 mm) A. anguilla caught. There were no significant differences in infection levels between water body types for adult A. anguilla or between sexes for any water body type. Prevalence was significantly lower in juvenile compared with adult A. anguilla captured in rivers and a positive correlation between infection levels and host size-classes was found. Future efforts should focus on monitoring the spread of A. crassus infections and assessing the swimbladder health of A. anguilla in Ireland.

Spatial and temporal variation in the infestation of sea trout (Salmo trutta L.) by the caligid copepod Lepeophtheirus salmonis (Krøyer) in relation to sources of infection in Ireland.

Infestations of post-smolt sea trout (Salmo trutta L.) by the salmon louse (Lepeophtheirus salmonis Krøyer) were characterized in 42 estuaries over a 5 year period in Ireland. Spatial variation in infestation was more significant than temporal trends and existed at 3 levels; between regions (regions > 100 km of coastline), between bays within regions (bays < 50 km in length) and between estuaries within bays (distance between estuaries < 10 km). The observed spatial structure in infestations inferred that production of the infective larvae varied between regions and bays and that there was limited movement of fish and infective larvae between regions and bays. In addition the different levels of infestation recorded between estuaries in the same bay indicated short spatial scale variability in parasite transmission. Significantly higher infestations occurred in bays that contained lice-infested farmed salmon. Lice-infested wild spring salmon, which were present in estuaries of some systems, did not have a significant positive impact on infestations.

Cardiopulmonary thromboembolism detected by Tc-99m MH-1 antifibrin antibody.

A patient with shortness of breath had a high probability lung scan for pulmonary embolism, but no obvious embolic source. Whole-body scintigraphy using Tc-99m labeled Fab' antifibrin monoclonal antibody showed large central pulmonary emboli as well as tracer uptake in the right atrium and aortic arch. No lower extremity clot was detected. This case shows significant differences in the appearance of pulmonary embolism as assessed by direct clot and ventilation-perfusion scintigraphy. It shows the importance of the heart as the origin of pulmonary emboli and the utility of direct thrombus visualization.

Thrombus precursor protein (TpP): marker of thrombosis early in the pathogenesis of myocardial infarction.

We have developed an enzyme-linked immunosorbent immunoassay for quantifying the immediate precursor proteins to intravascular thrombi. This thrombus precursor protein (TpP) assay identifies active thrombosis in several clinical conditions, including early myocardial infarction (MI). In a study of patients recruited for the GUSTO intervention study, MI patients had concentrations of TpP 4-20-fold that of controls; patients diagnosed without MI had concentrations similar to the control subjects. In a separate study of subjects presenting at the emergency room with chest pain, MI patients who presented early after the onset of chest pain had TpP concentrations significantly (P <0.01) higher than controls. Patients presenting late or diagnosed with other chest pain had concentrations within the reference range. The potential utility of the TpP assay as an aid for the diagnosis of thrombotic MI and other thrombotic conditions is described.

A rapid latex agglutination assay for the determination of plasma fibrinogen.

A monoclonal antibody to intact fibrinogen has been employed to develop a rapid latex agglutination assay for the estimation of plasma fibrinogen. The monoclonal antibody, 45J, recognizes an epitope located in the mid-section of the carboxy terminal end of the A alpha-chain. The epitope is destroyed by plasmin digestion of fibrinogen and there is no immunoreactivity with soluble cross-linked fibrin degradation products. The latex agglutination assay developed with the antibody is unaffected by aprotinin or anticoagulants, such as citrate, heparin or EDTA. When this method was compared with functional clotting assays, excellent correlation was observed with normal and pathological samples. After sample collection and dilution, the assay takes just two minutes to complete. Therefore, this procedure offers a simple and rapid assay for the measurement of intact fibrinogen in plasma.

Immunochemical evidence for intramolecular interaction of the carboxy terminal A alpha-appendages of plasma fibrinogen.

A monoclonal antibody (Mab), 45J, which reacts with intact fibrinogen, has been employed to demonstrate the interaction of the carboxy terminal regions of the A alpha-chain in non-denatured plasma fibrinogen. The 45J Mab recognizes an epitope in the mid section of the carboxy terminal end of the A alpha chain. The epitope is destroyed by plasmin and trypsin digestion. The 45J Mab and a horseradish peroxidase conjugate of the 45J Mab (45J-HRP) were used in an ELISA to demonstrate that the antibody could recognize two copies of the same epitope on purified fibrinogen or denatured plasma fibrinogen. Fibrinogen in non-denatured plasma could not be detected by this single antibody ELISA. This immunochemical study demonstrates that only one copy of the epitope on the C-terminal protuberance of the A alpha-chain is exposed in non-denatured plasma. However, once the plasma fibrinogen has been denatured, as in the purification process, both copies of the epitope are available for antibody binding. This finding suggests that in plasma there is an intramolecular interaction between the carboxy terminal ends of the fibrinogen A alpha-chains which can be destroyed by denaturation.

A model system for the in vivo determination of the thrombolytic effect of plasminogen activators.

An in vivo model system for measuring the thrombolytic efficiency of plasminogen activators was used. The formation of radiolabelled microthrombi was induced by infusion with I-125 labelled fibrinogen and thrombin. Reactive fibrinolysis was inhibited by administration of suboptimal levels of e-aminocaproic acid. The thrombolytic and subsequent fibrinolytic events were followed in the capillary bed of the lungs of anesthetized rats by external monitoring of the I-125 activity over the lung field. The model was successfully employed to demonstrate the thrombolytic effect of plasminogen activator produced by a transplanted spontaneous rat prostate adenocarcinoma cell line (PA III). The system proved to be reproducible with detection limits of 6000 I.U. using the PA-III cell line derived activator.

A fibrin specific monoclonal antibody which interferes with the fibrinolytic effect of tissue plasminogen activator.

Monoclonal antibodies to human fibrin have been prepared from stable hybridomas, obtained by fusion of a mouse myeloma cell line (NS-1) and spleen cells of Balb/c mice immunized with a suspension of human fibrin. One cell line, DG1, producing a monoclonal antibody of the IgG1, kappa subclass, reacted specifically with human fibrin (KD = 1.2 nM). Western blotting analysis indicates that DG1 crossreacts with the fibrin fragment D-dimer. Using both a chromogenic and an 125I-fibrin release assay it was illustrated that in the presence of the fibrin specific antibody the t-PA mediated generation of plasmin was significantly inhibited. An animal model system, developed to monitor thrombosis and induced reactive fibrinolysis, was used to investigate the interference of plasminogen activation, by the antibody, in vivo. This fibrin specific antibody prolonged the onset of reactive fibrinolysis in a dose dependent manner.