The benefits and risks of androgen therapy in the aging male: prostate disease, lipids and vascular factors
Barry G. Wren in Progress in the Management of the Menopause, 2020
Few interactions of androgens with other drugs have been reported. In patients using anticoagulants, anabolic steroids may reduce the dose which a patient requires by up to 25%. This is in part owing to the effect on coagulation factors; they may decrease the synthesis or increase the degradation of coagulation factors. Also, an increase of the natural anticoagulant antithrombin III has been found. Although not all patients are affected equally this should be taken into account when anticoagulants are given to patients using androgenic hormones, requiring a dose reduction of anticoagulants in these patients. There is some evidence from invitro and animal experiments that the inhibitory effect of aspirin on platelet aggregation occurs only in the presence of androgens, an effect distinct from the above action of androgens on coagulation factors63,64.
Ecology
Paul Pumpens in Single-Stranded RNA Phages, 2020
The phages MS2 and Qβ were compared as models by the aluminum coagulation (Shirasaki et al. 2009b) and aluminum coagulation-ceramic microfiltration (Shirasaki et al. 2009a) processes by using river water spiked with these phages. As a result, the phage Qβ was found more sensitive to the virucidal activity of the aluminum coagulant. Furthermore, the mechanisms of the phage inactivation during coagulation with aluminum coagulants were revealed (Matsushita et al. 2011). Shirasaki et al. (2012) involved the phage f2, together with the DNA phage f1, in the studies on virus removal during the aluminum coagulation−rapid sand filtration and coagulation−microfiltration processes. The high-basicity polyaluminum coagulants improved removal of the phages MS2 and Qβ from river water, in comparison with commercially available aluminum-based coagulants (Shirasaki et al. 2014). The influence of flocculation parameters on the phages MS2 and Qβ was examined in a mechanistic study of flocculation with polyaluminum chloride (Kreißel et al. 2014).
Plasma Protein Function in Hemostasis
Genesio Murano, Rodger L. Bick in Basic Concepts of Hemostasis and Thrombosis, 2019
Factor VIII is a glycoprotein with a molecular weight exceeding one million.68-70 Its subunit structure constitutes components with a molecular weight of about 200,000.68-70 Three major properties of Factor VIII have been defined: (1) shortening of the clotting time (Factor VIIICoee.), (2) precipitin reaction with rabbit antibody (VIIICoee,), and (3) correction of defective platelet aggregation in von Willebrand’s disease in the presence of the antibiotic ristocetin (VIIIVWF).70,71 The coagulant activity can be separated in the laboratory from the other two activities, and it is associated with one of the low molecular weight subcomponents.70-74 More specifically, the portion involved in the formation of the complex responsible for Factor X activation, is the Factor VIIICoag.The role of Factor VIIIVWF is discussed in Chapters 6 and 7.
Risedronate-loaded aerogel scaffolds for bone regeneration
Published in Drug Delivery, 2023
Nahla El-Wakil, Rabab Kamel, Azza A. Mahmoud, Alain Dufresne, Ragab E. Abouzeid, Mahmoud T. Abo El-Fadl, Amr Maged
An aqueous solution mixture containing NaOH, urea, and distilled water (7:12:81 by weight) was prepared in a 250 mL beaker. To produce a clear cellulose solution with a concentration of 3%, the aqueous solution was precooled to -12 °C, and cellulose pulp was added to it. The resulting cellulose solution was stored in a refrigerator at 4 °C for 48 hours. Cellulose fibers were regenerated from the cellulose solution through coagulation. The coagulant was formed by adding water to the aqueous solution and then filtration (El-Wakil & Hassan, 2008). The regenerated fibers were washed with distilled water. The regenerated cellulose was disintegrated using a Masuko grinder (Masuko Sangyo Co., Ltd., Japan) at 1500 rpm while varying the gap between the rotating disks and running the fibers through it for 120 minutes (El-Wakil et al., 2022).
Neutralization of Bitis arietans venom-induced pathophysiological disorder, biological activities and genetic alterations by Moringa oleifera leaves
Published in Toxin Reviews, 2021
Babafemi Siji Ajisebiola, Solomon Rotimi, Ullah Anwar, Akindele Oluwatosin Adeyi
Coagulant activity was assayed using citrated bovine plasma (Gomes and Pallabi 1999). 0.2 ml of various amounts of BAV (5.0, 2.5, 0.25 and 0.625 mg) from a serial dilution of 10 mg of venom in 1 ml of phosphate buffer solution (PBS, pH 7.2) was added to 0.2 ml of bovine citrated plasma and 0.2 ml of CaCl2. All mixtures are in triplicates. The mixtures were incubated at 37 °C and coagulation time was recorded and the minimum coagulant dose (MCD) was determined as the venom dose, which induced clotting of plasma within 60 s (Theakston and Reid 1983). Plasma incubated with PBS alone served as control. In neutralization assays constant amount of venom (3 × MCD) was mixed with 0.2 ml of various dilutions of MOLE (100, 200, 300 mg/ml) and polyvalent antivenin (0.2 ml) separately. Mixtures are in triplicates. The mixtures were incubated for 30 min at 37 ° C. Then 0.2 ml of mixture was added to 0.2 ml of citrated plasma and calcium chloride (CaCl2) and clotting times recorded. In control tubes plasma was incubated with either venom alone or plant extracts alone. Neutralization was expressed as effective dose (ED), defined as the ratio μl antivenin (plant extracts)/mg venom at which the clotting time decreased three times when compared with clotting time of plasma incubated with three MCD of venom alone.
Thromboembolic Risk of C1 Esterase Inhibitors: A Systematic Review on Current Evidence
Published in Expert Review of Clinical Pharmacology, 2020
Kevin Burnham, Justin P. Reinert
Multiple studies, utilizing animal models, have provided information about the impact of C1-INHs on coagulation [32–36]. Vast differences in doses used, methods, and measured outcomes make interpretation of these animal studies difficult, but both detrimental and beneficial effects on coagulation were shown. Mice with induced ischemic stroke, from middle cerebral artery occlusion, benefited from 15 IU of C1-INH, with a reduction in infarct volumes and fibrinogen mean optical densities [35]. Fibrin deposition in the lungs and muscle was also found to be lower in another study evaluating the use of 50 IU/kg of C1-INH in a rat model of ischemic-reperfusion injury after femoral artery occlusion [33]. C1-INH substitution with a 400 IU/kg bolus followed by a 400 IU/kg/4 hour of infusion improved venous oxygen saturation, and reduced fibrin deposition by 70% in the lungs and liver of rabbits with induced disseminated coagulation [36]. More recently, doses of C1-INH up to 800 IU/kg given to rabbits did not promote thrombus formation during venous stasis [32]. In lieu of these findings, cardioprotective effects of C1-INH in a pig model were examined by Horstick et al. [34]. After an hour of coronary artery occlusion, the group of pigs receiving a C1-INH dose of 40 IU/kg benefited, but severe coagulation disorders occurred in 4 of the 27 pigs on doses ≥100 IU/kg (1 with the 100 IU/kg dose and 3 with the 200 IU/kg) [34].
Related Knowledge Centers
- Cell Adhesion
- Fibrin
- Hemostasis
- Endothelium
- Platelet
- Thrombus
- Blood
- Gel
- Platelet-Activating Factor
- Tissue Factor