Urate Lab Report

With all living organisms, a process known as cell respiration is integral in order to provide the body with an essential form of energy, adenosine triphosphate (ATP). Oxygen, although an essential part of this process, can form reactants from colliding with electrons associated with carrier molecules. (pb101.rcsb.org, 2017). Hydrogen peroxide is an integral product of this reaction but is known to impose negative effects on the body if high levels are introduced. Explicitly, this reaction is caused “If oxygen runs into (one of these) carrier molecules, the electron may be accidentally transferred to it. This converts oxygen into dangerous compounds such as superoxide radicals and hydrogen peroxide, which can attack the delicate sulphur atoms and metal ions in proteins.” (pdbh101.rcb.org, 2017). Research has suggested that the hydrogen peroxide can be converted into hydroxyl radicals, known to mutate DNA, which can potentially cause bodily harm due to DNA’s role in the synthesis of proteins. These radicals can cause detrimental effects on the human body, and studies have suggested a link to ageing. Due to the harmful effects of these H2o2, it is important that the body finds a way to dispose of hydrogen peroxide before concentrations are too great.

Under normal condition, ROS production in the brain is balanced by the endogenous enzymatic and non-enzymatic anti-oxidative mechanisms. The enzymes include superoxide dismutase (SOD), glutathione peroxidase (GPX) and catalase. SOD catalyzes dismutation of superoxide to hydrogen peroxide, providing the first line against ROS damage [46, 70]. GPX and catalase further metabolize hydrogen peroxide to water and oxygen [71]. In the process, reduced glutathione (GSH) is oxidized to oxidized glutathione (GSSG) and it can be recycled by the NADPH-dependent GSSG reductase [72]. Non-enzymatic endogenous anti-oxidative small molecules also play very important roles in defending against oxidative stress, especially in extracellular space that the enzymes are absent or in very low levels [73]. Small-molecule anti-oxidant can be water-soluble or lipid-soluble, these molecules include glutathione, vitamin E and C (inhibits

Many of these compounds have been demonstrated to be correlated with various disease states. One of the most heavily studied EBC biomarkers is hydrogen peroxide (H2O2). H2O2 concentration in EBC has been shown

The kidney is greatly susceptible to damage caused by reactive oxygen species (ROSs), due to oxidative stress by polyunsaturated fatty acids in the composition of renal lipids (Ozbek, 2012). In addition this damage also can be caused by 1) high volume of blood flows through kidney and 2) large amounts of toxins

Risk factors such as smoking, hypercholesterolemia and hypertension have been proved to increase oxidative stress in the vessel (Davignon and Ganz, 2004). The oxidized LDL (ox-LDL) increases the synthesis of caveolin-1 and it inactivates endothelial NO synthase to produce NO. The free radical superoxide anion rapidly deactivates NO and destroys tetrahydrobiopterin, a cofactor for NO synthesis (Briasoulis et al., 2012). These result in inadequate blood flow into the arteries as the smooth muscle cells within the vessel walls can no longer relax sufficiently. Therefore, the total peripheral resistance in the arteries will increase (Hare and Stamler, 2005). Hypertension can be caused by high intake of salt. This raises both the osmolarity and body temperature, increases oxidative stress and causes damage to the vessel. Also, LDL and ox-LDL stimulate the production of reactive oxygen species (ROS) by inducing vascular endothelium inflammation and cause impaired endothelial function (Briasoulis et al., 2012). Smoking results in inflammation, thrombosis and oxidation of LDL, which increase oxidative stress in numerous cells. The reaction between NO and superoxide anion form peroxynitrire, the latter can cause vascular dysfunction(Mathur, 2010).Both active and passive exposure to smoking are reported to increase the risk of atherosclerosis and coronary heart disease by decreasing the

Cardiovascular risk factors such as elevated levels of cholesterol and lipids in the blood, high blood pressure, and smoking cigarettes are causing the reduction in nitrogen oxide (NO) bioavailability, thus resulting into endothelium dysfunction.2 This further gives a rise to reactive oxidative species such as superoxide.6 NADPH oxidase is the principal source of reactive oxygen species, therefore fully understanding the function of NADPH oxidase in cardiovascular disease can bring a new insight in the treatment of cardiovascular diseases via controlling oxidative stress.15 An ultimate product of NADPH oxidase (O2- ) and endothelial nitric oxide synthase-derived product NO combine with one another to form peroxynitrite (ONOO-). Peroxynitrite

URO-synthase is an enzyme involved in the metabolism of the tetrapyrrole compound porphyrin, which composes heme. Heme performs a variety of biological functions but is most commonly known for being a component of hemoglobin, helping it to provide oxygen to tissues throughout the body. Specifically, URO-synthase functions to convert a linear chain of four porphobilinogen molecules, hydroxymethylbilane (HMB), into the first metabolic intermediate in the biosynthesis of heme, the cyclic tetrapyrrole uroporphyrinogen III [3, 4]. This conversion of hydroxymethylbilane by URO-synthase into uroporphyrinogen III (URO-III) is necessary to facilitate the continuation of the pathway and the successful production of heme. URO-synthase performs this function primarily within the mitochondria and cytoplasm of erythrocyte precursor cells in bone marrow, although the liver also functions to produce heme by the same biosynthetic pathway [5].

Oxidative stress can be closely compared to “rusting” of mammal’s cells. Free radicals are unstable molecules that ravage or “oxidize” cells throughout the body in a process

To affirm that the theorized mechanism of halogenation for sulfilimine bond formation they tested the ability of peroxidasin to form crosslinks in the absence of halides. As expected minimal crosslinking occurred, and it was supported that crosslinks formed as a result of halogenation. The rest of figure 3 investigates the role of peroxidase in hypohalous acid production specifically; HBr and HCl. Different peroxidases showed preferentiality in which hypohalous acid they formed.

Urate’s pro-oxidant effects could link hyperuricemia and inflammatory disease, yet the mechanism is obscure. For humans, dietary purine is broken down and released as urate. Urate builds up in human serum because we lack the enzyme Uricase to promote its excretion. In healthy doses urate acts as an antioxidant and scavenges reactive oxygen species. Yet, high serum urate (hyperuricemia) is associated with gout, metabolic syndrome and cardiovascular disease, the link being oxidative stress. Urate promotes oxidative stress by generating reactive oxygen species or promoting biomolecule oxidation. Concentration affects urate’s antioxidant or pro-oxidant activity, ergo the ‘dose makes the poison’.

Introduction When an animal drinks water and eats food, the amount of sodium chloride and water put into the plasma of the blood can be either hypertonic, isotonic, or hypotonic to the homeostatic concentration of sodium chloride in the plasma, which is maintained around 280 to 300 mOsmols (Sherwood 2013). Once the solution has reached the plasma, it will equilibrate with the interstitial fluids, and then the intercellular fluids. To maintain this equilibrium, it is necessary to excrete excess salts and water from the body cells. The kidneys are the functional organs of the urinary system, and within the kidneys is the nephron, the functional unit that carries out the equilibration. The nephrons, through filtration, reabsorption, and secretion, produce the urine that is excreted by an animal.

Alzheimer’s disease (AD) is a debilitating illness of the nervous system, affecting millions of geriatric population worldwide. Numerous factors are involved in the disease etiology viz. tau phosphorylation, amyloid β protein (Aβ) accumulation, lipid dysregulation, oxidative stress and inflammation. Among all factors oxidative stress plays a central role in the pathogenesis of AD leading to neuronal dysfunction and cell death (1). Oxidative stress is caused due to the increased production of reactive oxygen species (ROS) which denatures biomolecules such as proteins, lipids and nucleic acids through pathological redox reactions(2). Increased oxidative stress also results in excessive lipid peroxidation, weakening the cell membranes, causing

Oxidative stress is widely accepted to be associated with dysfunction of pancreatic β-cells as well as insulin resistance in type 2 diabetes (Henriksen et al., 2011). Experimental evidences suggest the involvement of free radicals in the onset of diabetes and more importantly in the development of diabetic complications (Lipinsky, 2001). Studies have revealed decreases in expression of genes for antioxidant enzymes, such as superoxide dismutase (SOD), glutathione peroxidase, and catalase in diabetic models (Lenzen et al., 1996). Also a decrease in the activities of the antioxidant/ antioxidant enzyme systems in diabetics are linked to the progressive glycation of the enzyme proteins (Hartnet et al., 2000). The interrelationship between the antioxidative potentials and antidiabetic activities of bioactive compounds is still unclear. In the present study, the extent of free radical damage orchestrated by STZ administration was significantly reduced by the antioxidant composition and combination treatment in a dose-dependent manner; thereby reducing the extent of pancreatic β-cell damages among the rats co-treated with combination therapy and STZ, relative to normal and STZ-only rats. The HFD/STZ-induced diabetic control rats had significantly lower (p< 0.05) of total SOD, CAT, GST and GPx activities among the extracts, cell gevity, antioxidant composition and combination therapy co-treated rats (Figure 4.2.34, Figure 4.2.35, Figure 4.2.36, Figure 4.2.37). HFD/STZ decreased the

Gout is a condition of the joint that causes the patient severe pain. It is characterized by an increase of uric acid in the blood that lasts for some time. This elevation of uric acid in the blood is called hyperuricemia. In normal development, uric acid is chemical that is produced in the body. This chemical is created when the body breaks down substances called purines. Normally, uric acid dissolves in the blood and is excreted by the kidneys and passes through the urine. If the patient’s body produces an excess of uric acid or doesn 't remove enough if it, they can get sick. However, not all patients that have elevated uric acid levels will develop gout (Edwards, 2013). Under-excretion or over-production of uric acid by the

Uric acid comes from the breakdown of substances called purines. Purines are found in all body tissues. These purines are also found in many foods, such as liver, dried beans, peas, anchovies, red meat, fructose, and even beer (Katz). Uric acid dissolves in the blood, filters through the kidneys, and exits the body via urine excretion. This bodily function can be affected if the body increases the amount of uric acid it makes or intakes, and if the kidneys