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Biomedical subjects

C A Jennings

Publications and source records attributed to C A Jennings.

26 records · Page 2Linked to original sources
PubMed1988

The three-dimensional localization of internal mammary lymph nodes by radionuclide lymphoscintigraphy.

In breast cancer patients, radiation therapy planning must account for individual anatomy to ensure optimal coverage of tumor and internal mammary nodes. To achieve this, three-dimensional radionuclide lymphoscintigraphy (RNLS) was performed in 167 patients by obtaining two images of the nodes using a 30-degree slant hole collimator rotated 180 degrees between images. Analysis of 768 nodes (mean 4.6/patient) visualized from the level of rib 1 through interspace 5 was performed. The number of nodes seen was not a function of patient age. Cross-communication to the contralateral node chain occurred in 13.8% of cases. Eighty-two percent of nodes were located near the first three ribs and interspaces; 23% were located beyond 3.0 cm from the mid-sternal line. At the level of the radiation beam match line (second rib or interspace), 4.5% of nodes were deeper than 3.0 cm. From rib 3 through interspace 5, 3.9% were deeper than 3.0 cm. Using an idealized tangential field, at least one node would have been missed in 16.2% of patients. Three-dimensional RNLS allows definition and localization of normal sized nodes and ensures that radiation therapy portals can be tailored for each individual under treatment.

Adult↗
PubMed1987

Inhibition of the tissue factor-factor VII complex: involvement of factor Xa and lipoproteins.

Inhibition of the procoagulant activity of a tissue factor-Factor VII (TF-FVII) complex by Al(OH)3-adsorbed plasma (AP) was found to require the presence of Factor Xa (FXa). Inhibitory activity seems to be generated through the interaction of FXa with a component in AP rather than with the TF-FVII complex. Quantitation of inhibitor activity was carried out using an amidolytic assay for TF-FVII activity. Incubation of AP with various antisera demonstrated that the inhibition was mainly associated with the presence of apolipoprotein B (apo B) rather than alpha 2-macroglobulin or antithrombin III. Purified lipoprotein-rich fractions prepared from AP, using density gradient ultracentrifugation, all contained some inhibitory activity. Incubation with anti-apo B greatly reduced the inhibitor in the very low density lipoprotein (VLDL)- and low density lipoprotein (LDL)-rich fractions but had essentially no effect on inhibition by the high density lipoprotein (HDL) fraction, which was rich in apo A. The inhibitory activity of AP was 60% that of normal plasma and this correlated well with the relative apo A and apo B concentrations. It is proposed that inhibition requires the interaction of FXa with plasma lipoproteins or associated components and that the product of this interaction is then able to bind to and inhibit the TF-FVII complex.

Adsorption↗
PubMed1986

Anticoagulant activities of pentosan polysulphate (Hémoclar) due to release of hepatic triglyceride lipase (HTGL).

Subcutaneous injections of 50 mg pentosan polysulphate (Hémoclar) were given to normal volunteers and the effects on anti-Factor Xa activity, thrombin generation and lipase release measured. Concentrations of pentosan polysulphate were measured by a competitive binding assay and the mean peak level found to be 1.6 micrograms/ml. Anti-Xa clotting activity rose to 0.034 iu/ml and thrombin generation induced by lipid peroxides was inhibited by approximately 50%. Neither of these effects could be accounted for by the direct action of pentosan polysulphate at the concentrations measured. Pentosan polysulphate was very effective in releasing lipase, approximately 70-80% of the total enzyme activity being due to hepatic triglyceride lipase (HTGL). In vitro addition of purified HTGL to plasma markedly enhanced anti-Xa clotting activity, and caused a 70% inhibition of lipid peroxide induced thrombin generation. Anti-Xa activity of post-injection plasma was increased rather than neutralised by addition of polybrene, and this effect could be mimicked by addition of polybrene to plasma containing pentosan polysulphate and purified HTGL. It is concluded that, when given in low doses subcutaneously, pentosan polysulphate acts as an indirect anticoagulant, its major effects being due to release of HTGL.

Adult↗
PubMed1986

Inhibition of tissue thromboplastin-mediated blood coagulation.

Factors affecting the inhibition of tissue thromboplastin (TP)-mediated blood coagulation have been investigated. Human brain thromboplastin progressively loses procoagulant activity when incubated in the presence of defibrinated plasma and CaCl2. Inhibition is maximal at a CaCl2 concentration of 1.5 mM during incubation and involves the calcium dependent binding of a plasma component(s) to the TP-FVII complex, preventing the activation of FX. Chelation of calcium ions using EDTA releases active TP and FVII from the inhibited complex. No inhibition occurs during incubation of TP with Al (OH)3 adsorbed plasma and calcium ions unless a Factor VII concentrate (or purified FVII and FX) is also present. Incubation of TP with antithrombin III-deficient plasma and calcium ions also leads to inhibition. Moreover, purified AT III cannot substitute for adsorbed plasma in producing TP inhibition. The data are consistent with the presence in plasma of a potent AT III independent inhibitor of TP-mediated blood coagulation.

Blood Coagulation↗
PubMed1985

Neutralisation of heparan sulphate and low molecular weight heparin by protamine.

The neutralisation by protamine sulphate (PS) of heparan sulphate (HS), a low molecular weight heparin (LMWH), and a reference preparation of unfractionated heparin (UH), was studied by activated partial thromboplastin time (APTT) and anti-Xa clotting assays. UH was most easily neutralised in the APTT assay by PS (on a weight for weight basis), followed by LMWH and HS. The neutralisation of APTT activity by PS closely followed the loss of activity in the anti-Xa clotting assay, when plasma was used as the source of At III. When the anti-Xa clotting assay was carried out using purified At III in place of plasma, HS and LMWH were neutralised by much lower amounts of PS and resembled UH neutralisation more closely. Resistance of HS anti-Xa activity to PS neutralisation decreased with increasing plasma dilution. The presence of bovine albumin with purified At III concentrate increased the resistance of HS to PS neutralisation. It is concluded that PS binding to UH, HS and LMWH is probably related more to their degree of sulphation than molecular weight and that non-specific interactions between PS and plasma proteins inhibit the binding of PS to HS and LMWH.

Factor X↗
PubMed1985

Clinical comparison of two radiocolloids for internal mammary lymphoscintigraphy.

Recent studies suggest that 99mTc-labeled radiocolloid (SC) compounded with hydrogen sulfide can be used to visualize lymph channels and nodes. Our study prospectively compared SC with 99mTc antimony sulfide (SbS) colloid, in 28 patients undergoing internal mammary lymphoscintigraphy. Images were recorded on a scintillation camera and computer at 0.5, 1.0, and 3.0 hr. Quantitative analysis included assessment of percent (%) injected dose in nodes, the percent remaining at the injection site, and the relative intensity of the most cephalad node compared to a 57Co standard. The mean (means) % injected dose of both radiocolloids within visualized nodes was less than 1% at each time interval, with no significant differences between means's. The means % injected dose remaining at the injection site at 3.0 hr was 83 for SbS and 76 for SC not statistically significant (N.S.). The means of the ratio of counts within the most cephalad node at 3.0 hr to counts within a 57Co standard was 0.98 for SbS and 1.03 for SC (N.S.). Clinical assessment of number of nodes visualized and extent of radiocolloid migration showed no difference between the two agents. The biological and clinical parameters for the two colloids appear similar when used for internal mammary lymphoscintigraphy.

Adult↗
PubMed1984

Anticoagulant properties in vitro of heparan sulphates.

The anticoagulant properties in vitro of eight heparan sulphate preparations were studied using clotting (APTT, anti-Xa) and amidolytic (anti-Xa, anti-thrombin) assays. Activities ranged from very low levels (less than 5 iu/mg) up to values similar to those of heparin. Activities measured by APTT assay showed the best correlation with the sulphate to carboxylate ratio of the heparan sulphates. Highest activities were obtained in the anti-Xa clotting assay, these being approximately two-fold greater than activities in the anti-Xa amidolytic assay. Five of the heparan sulphate preparations were readily neutralised by protamine sulphate, whereas the three heparans with the lowest sulphate to carboxylate ratio were much more resistant to neutralisation. After fractionating each heparan sulphate into At III-binding and non-binding material, it was found that the anti-coagulant properties were associated only with the former. It is concluded that these properties are dependent on the activation of At III.

Animals↗