Selenium supplementation in the prevention of coronavirus infections (COVID-19).

Selenium (Se) is a ubiquitous element akin to sulfur (S) existing in the Earth crust in various organic and inorganic forms. Selenium concentration varies greatly depending on the geographic area. Consequently, the content of selenium in food products is also variable.

Pathophysiological significance of protein hydrophobic interactions: An emerging hypothesis.

Fibrinogen is a unique protein that is converted into an insoluble fibrin in a single enzymatic event, which is a characteristic feature of fibrinogen due to its susceptibility to fibrinolytic degradation and dissolution. Although thrombosis is a result of activated blood coagulation, no explanation is being offered for the persistent presence of fibrin deposits in the affected organs. A classic example is stroke, in which the thrombolytic therapy is effective only during the first 3-4 h after the onset of thrombosis.

Application of Sodium Selenite in the Prevention and Treatment of Cancers.

Selenium is an essential trace element that occurs in nature, in both inorganic and organic forms. This element participates in numerous biochemical processes, including antioxidant potential, but the mechanism of its anti-cancer action is still not well known. It should be noted that the anti-cancer properties of selenium depends on its chemical form, therapeutic doses, and the tumor type.

Redox-Active Selenium in Health and Disease: A Conceptual Review.

Although it is generally accepted that selenium (Se) is important for life, it is not well known which forms of organic and/or inorganic Se compound are the most biologically active. In nature Se exists mostly in two forms, namely as selenite with fourvalent and selenate with sixvalent cations, from which all other inorganic and organic species are derived. Despite a small difference in their electronic structure, these two inorganic parent compounds differ significantly in their redox properties.

Sodium Selenite as an Anticancer Agent.

Selenium (Se) is a ubiquitous, albeit not uniformly distributed metalloid present in earth crust. Consequently, its human intake with food products, particularly grains and vegetables, is also very uneven, and in certain cases can result in a severe Se deficiency. It was also documented that Se deficiency observed in some countries and/or geographic regions (e.

Physiochemical basis of human degenerative disease.

The onset of human degenerative diseases in humans, including type 2 diabetes, cardiovascular disease, neurological disorders, neurodevelopmental disease and neurodegenerative disease has been shown to be related to exposures to persistent organic pollutants, including polychlorinated biphenyls, chlorinated pesticides, polybrominated diphenyl ethers and others, as well as to polynuclear aromatic hydrocarbons, phthalates, bisphenol-A and other aromatic lipophilic species. The onset of these diseases has also been related to exposures to transition metal ions. A physiochemical mechanism for the onset of degenerative environmental disease dependent upon exposure to a combination of lipophilic aromatic hydrocarbons and transition metal ions is proposed here.

Iron-induced parafibrin formation in tumors fosters immune evasion.

Although efficacious in vitro, it is well known that adoptive immunotherapeutic modalities lose their potency when applied in vivo. Furthermore, malignant cell exposure to blood platelets attenuates the anticancer activity of natural killer (NK) cells. We argue that upon contact with redox iron, fibrinogen is converted to a hydrophobic fibrin-like polymer that coats tumor cells and provides protection from immune-mediated destruction.

Profound morphological changes in the erythrocytes and fibrin networks of patients with hemochromatosis or with hyperferritinemia, and their normalization by iron chelators and other agents.

It is well-known that individuals with increased iron levels are more prone to thrombotic diseases, mainly due to the presence of unliganded iron, and thereby the increased production of hydroxyl radicals. It is also known that erythrocytes (RBCs) may play an important role during thrombotic events. Therefore the purpose of the current study was to assess whether RBCs had an altered morphology in individuals with hereditary hemochromatosis (HH), as well as some who displayed hyperferritinemia (HF).

High ferritin levels have major effects on the morphology of erythrocytes in Alzheimer's disease.

Introduction: Unliganded iron both contributes to the pathology of Alzheimer's disease (AD) and also changes the morphology of erythrocytes (RBCs). We tested the hypothesis that these two facts might be linked, i.e.

Unusual clotting dynamics of plasma supplemented with iron(III).

Iron salts are used in the treatment of iron deficiency anemia. Diabetic patients are frequently anemic and treatment includes administration of iron. Anemic patients on hemodialysis are at an increased risk of thromboembolic coronary events associated with the formation of dense fibrin clots resistant to fibrinolysis.

The role of iron-induced fibrin in the pathogenesis of Alzheimer's disease and the protective role of magnesium.

Amyloid hypothesis of Alzheimer's disease (AD) has recently been challenged by the increasing evidence for the role of vascular and hemostatic components that impair oxygen delivery to the brain. One such component is fibrin clots, which, when they become resistant to thrombolysis, can cause chronic inflammation. It is not known, however, why some cerebral thrombi are resistant to the fibrinolytic degradation, whereas fibrin clots formed at the site of vessel wall injuries are completely, although gradually, removed to ensure proper wound healing.

Iron-induced fibrin in cardiovascular disease.

Accumulating evidence within the last two decades indicates the association between cardiovascular disease (CVD) and chronic inflammatory state. Under normal conditions fibrin clots are gradually degraded by the fibrinolytic enzyme system, so no permanent insoluble deposits remain in the circulation. However, fibrinolytic therapy in coronary and cerebral thrombosis is ineffective unless it is installed within 3-5 hours of the onset.

Albumin stabilizes fibrin fiber ultrastructure in low serum albumin type 2 diabetes.

Serum albumin is an essential plasma protein that serves an important function in maintaining osmotic pressure. Low levels of this protein are associated with the kidney failure and hemodialysis that are often seen in diabetic patients who are at high risk of thrombotic events. In diabetes, fibrin fiber nets are changed to form dense matted deposits (DMDs, or parafibrin).

Changes in red blood cell membrane structure in type 2 diabetes: a scanning electron and atomic force microscopy study.

Red blood cells (RBCs) are highly deformable and possess a robust membrane that can withstand shear force. Previous research showed that in diabetic patients, there is a changed RBC ultrastructure, where these cells are elongated and twist around spontaneously formed fibrin fibers. These changes may impact erythrocyte function.

Thromboembolic ischemic stroke changes red blood cell morphology.

Unlabelled: BACKGROUND OR INTRODUCTION: Stroke is one of the most debilitating diseases causing morbidity and mortality worldwide. During ischemic stroke, erythrocytes undergo oxidative and proteolytic changes resulting not only in inflammation but also in changes in cellular rheology. During the event, fibrin fibers, which are typically a fine net, clot abnormally to form a clot of dense matted deposits (DMDs).

Novel use of scanning electron microscopy for detection of iron-induced morphological changes in human blood.

Fibrinogen is key to the maintenance of hemostasis and is an acute phase protein that is part of the coagulation cascade of proteins. It plays a fundamental role in inflammation, particularly as indicator for a proinflammatory state and is a prominent marker for developing vascular inflammatory diseases. The ultrastructure of fibrin nets can be studied using scanning electron microscopy (SEM) with the addition of thrombin to plasma.

A novel method for assessing the role of iron and its functional chelation in fibrin fibril formation: the use of scanning electron microscopy.

Aims: Inflammatory diseases associated with iron overload are characterized by a changed coagulation profile, where there is a persistent presence of fibrin-like material of dense-matted deposits (DMDs). It is believed that one source of such material is a result of the activation of blood coagulation without the generation of thrombin, causing clots to become resistant to fibrinolytic dissolution. The aim of the current manuscript therefore is to apply a novel scanning electron microscopy method for assessing the role of functional chelation in the prevention or reversal of iron-induced fibrin formation.

Oxidation inhibits iron-induced blood coagulation.

Blood coagulation under physiological conditions is activated by thrombin, which converts soluble plasma fibrinogen (FBG) into an insoluble clot. The structure of the enzymatically-generated clot is very characteristic being composed of thick fibrin fibers susceptible to the fibrinolytic degradation. However, in chronic degenerative diseases, such as atherosclerosis, diabetes mellitus, cancer, and neurological disorders, fibrin clots are very different forming dense matted deposits (DMD) that are not effectively removed and thus create a condition known as thrombosis.

Iron enhances generation of fibrin fibers in human blood: implications for pathogenesis of stroke.

Stroke is associated with the intracerebral formation of fibrin clots which may lead to irreversible brain damage. Thrombolytic therapies employ a variety of natural and/or recombinant plasminogen activators to initiate fibrinolytic degradation of cerebral thrombi. However, such therapies when installed beyond 4- to 6-h window, may fail to achieve the expected outcome.

Interaction of fibrin with red blood cells: the role of iron.

Activation of coagulation pathways results in the formation of hemostatic fibrin plugs. Under normal physiologic conditions fibrin clots are gradually, albeit completely, degraded by a fibrinolytic enzyme system to ensure proper wound healing and/or blood vessel patency. Yet in pathological situations, thrombi are not effectively removed, leading to chronic thrombosis.

Novel pathway of iron‑induced blood coagulation: implications for diabetes mellitus and its complications.

Fibrinogen (FBG) is a high-molecular-weight protein and precursor to the enzymatically formed fibrin. It has been recently discovered that FBG can be converted into an insoluble, fibrin-like polymer by a nonenzymatic action of hydroxyl radicals (HRs). These free radicals are generated due to the reaction between hydroxyl groups of water and trivalent ferric ions without the participation of any redox agent.

Hydroxyl radical and its scavengers in health and disease.

It is generally believed that diseases caused by oxidative stress should be treated with antioxidants. However, clinical trials with such antioxidants as ascorbic acid and vitamin E, failed to produce the expected beneficial results. On the other hand, important biomolecules can be modified by the introduction of oxygen atoms by means of non-oxidative hydroxyl radicals.