Negative Regulation Of Sheepmeat Odour And Biogen ( SEPW1 )

diseases, fatty acid levels, and meat quality. The science of genetic engineering, however, is the

Selenium: An anti-oxidant that works as a shield to protect against the development of prostate cancer.

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.

Digestion is the result of competition between the rates of digestion and passage. As passage rate increases, the digesta flowing from the rumen will contain greater amounts of undigested feed particles, resulting in a lower DMD (Varga and Kolver, 1997). Mwenya et al. (2003) in comparing indigenous fat-tailed and Dorper sheep found that Dorper sheep had significantly (P<0.05) in Dorper than in Merino sheep and this occurred when fed the lower quality, wheaten chaff diet. Therefore glucose synthesis may potentially be higher in Dorper compared to Merino sheep. This is an important finding and this may have contributed to the superior production responses reported by several researchers including Scanlon et al. (2013) of Dorper compared to Merino sheep, especially when fed on low quality, roughage

Receptor proteins recognize bitter-tasting compounds on the surface of taste cells. There are approximately 30 genes for different bitter taste receptors. The gene for the PTC taste receptor, TAS2R38, was identified in 2003. Sequencing identified three nucleotide positions that vary within the human population (Kim et al.); each variable position is termed a single nucleotide polymorphism (SNP). One specific combination of the three SNPs, termed a haplotype, correlates most strongly with tasting ability. In this lab, non-tasters (homozygous recessive, tt) can determine their genotype without having to run the PCR and electrophoresis because non-taster gene is recessive. Thus, the only way for them to express recessive phenotype is to have the tt alleles of

Half of the animals will be euthanized on day 28 (before the second DSS cycle), and the other half on day 56. This will allow us to study ROS production and DNA stability before the onset of neoplasia (28 days), and once it is established (56 days). We have an extensive experience in this animal model6,8,10. Power calculations indicate we will need an n=8 mice per group to obtain significant results31. Colon will be processed for histology and epithelial cell isolation by chelation in EDTA. Part of these epithelial cells will be kept for RNA isolation, part will be used for ROS determination, and the rest will be seeded in extracellular matrices to grow them as organoids. Organoids will be cultured for 7 days to allow for additional divisions in the presence or absence of 1µg/mL LPS32. Epithelial cells in tissues and culture will be analyzed for DNA damage and genetic instability via γH2AX immunofluorescence (a marker for DNA damage), presence of anaphase bridges, and telomere staining. Dr. Verdun´s lab is very experienced in these techniques33,34. Epithelial cells will be interrogated for the expression of Duox2, SOD1, CAT, GPX2, and GPX4 (quantitative PCR) as markers of oxidative stress in epithelial cells35, and production of ROS will be measured by staining with DCFDA and Amplex Red probes. These experiments will indicate to which extent DNA damage induced by ROS is mediated by TLR4 activation in the

Introduction For almost all living organisms, the removal of hydrogen peroxide is necessary in maintaining the life and function of the cells within that organism (Zamocky, 2008). To remove the destructive chemical compound, the body produces an enzyme referred to as catalase. This particular enzyme speeds up the reaction that specifically breaks down H2O2 into H2O and O2. Catalases, as well as other enzymes, are able to speed up the chemical reaction by lowering the activation energy (Urry, 2016). There are multiple ways to affect how fast a catalase can lower the activation energy during the breakdown of hydrogen peroxide: Tissues of different materials each contain a different genetic makeup, which react differently when exposed to catalase.

Differentiation is also associated with changes in mitochondrial activity. The data presented in table 3 summaries XTT assay results where no significant difference in mitochondrial activity was seen between the DMSO-treated and untreated FLC cells. This resulting non-significant result does not follow what is expected between undifferentiated cells and the DMSO-treated, differentiated cells. A possible explanation for this is that the differentiated cells present in the DMSO-treated culture have not yet fully matured into an erythrocyte (mature erythroid phenotype). Overall, the results of this experiment support how differentiation leads to a loss of proliferation and accumulation of haemoglobin but do not support the hypothesis that change in mitochondrial content that is associated with differentiation.

Polymerase chain reaction will amplify the DNA segment needed to compare and analyze the results correctly. People should care about the PTC gene to see if there is an evolutionary history of a different function of this gene. The question to be answered in this lab is how the AVI haplotype alters the structure and function of the PTC receptor, which can lead to the non-taster phenotype in AVI homozygotes. We can further question the mechanism for the widespread appearance of the non-taster AVI haplotype in humans and its natural advantage, if there is one. The purpose of this project is to find the connection between taste sensitivity to the bitter compound phenylthiocarbamide (PTC) and single nucleotide polymorphism (SNPs) in the PTC bitter taste

Enhanced food quality is also a major attribute with genetically engineered animals. Ormandy, Dale, and Griffin (2011) explain the impact of enhanced food quality in pigs and sheeps by stating, “Pigs have been genetically engineered to express the △12 fatty acid desaturase gene (from spinach) for higher levels of omega-3, and goats have been genetically engineered to express human lysozyme in their milk.” These enhancements have been beneficial to the health of humans. If these enhancements had never been developed, the world would be looking for these supplements in other places, and may have never found them. Terry D. Etherton (2008) confirms that genetically engineered animals have enhanced food quality by stating, “ information by stating

During oxidation of oxymyoglobin, both superoxide anion and hydrogen peroxide are produced and further react with iron to produce hydroxyl radical. The hydroxyl radical has the ability to penetrate into the hydrophobic lipid region and hence facilitates lipid oxidation. The prooxidant effect of oxymyoglobin on lipid oxidation is concentration dependent. At equimolar concentrations, oxymyoglobin shows higher prooxidative activity towards lipid than metmyoglobin. However, the catalytic activity of metmyoglobin is promoted by hydrogen peroxide. The reaction between hydrogen peroxide and metmyoglobin results in the formation of two active hypervalent myoglobin species perferrylmyoglobin and ferrylmyoglobin. Those two hypervalent myoglobin species

In GSH-abundant tissues such as the retina, the most common type of protein oxidation is glutathionylation, which often affects the cysteines on the active sites of proteins and renders proteins dysfunctional (Hoppe et al., 2004). High amounts of PSSG eventually lead to cell injury and death due to the inactivation of multiple important proteins and enzymes (Ghezzi, 2013; Pastore and Piemonte, 2012). Therefore, reversing PSSG is vital to prevent cell damage and death. Specifically, the glutaredoxin family (Grxs) catalyzes the reduction of protein-glutathione mixed disulfides (PSSG) and therefore functions as powerful protein thiol oxidation repair enzymes (Holmgren, 2000; Lillig et al., 2008; Shelton et al., 2005). In mammalian cells, Grxs exist in two subsets: Grx1 and Grx2. Grx1 is primarily localized to the cytoplasm but has been implicated in the nucleus and inner mitochondrial membrane. Concentrated in the mitochondria ten times more than Grx1, Grx2 primarily exerts its protective effects in the mitochondrial matrix but has been associated with the nucleus as well (Gladyshev et al., 2001; Lundberg et al., 2001). Grx1 and Grx2 have a significant Cys-X-X-Cys active site motif. The two cysteine residues act as redox sensors and allow for a monothiol mechanism using the N-terminal cysteine to reduce

Understanding of the full complexity of genetic factors that underpin such observations is currently limited. However, a number of examples of single gene –diet interactions have been reported, resulting in the development of nutrigenetic testing as a new paradigm for health management. Nutrigenetic testing focuses on testing for DNA polymorphisms which are known to influence phenotypic responses to diet. The purpose of testing is to use this genotype information to provide more personalised advice about nutrition and health, the primary goal being to use an individual’s genetic information to predict their future health susceptibilities and to guide selection of ‘the best’ preventative

A previously documented paper by Perry et al. (2007) has already done extensive research on this topic. Perry and his team explored the relationship between AMY1 gene copy number and amylase protein level for a population of 50 European-American individuals. The R2 value was 0.351, indicating that a substantial portion of the variation in amylase protein levels is not explained by gene copy number (Perry et al. 2007). The variation was attributed to other genetic influences like regulatory region single nucleotide polymorphisms (SNPs) or towards more non-genetic factors such as individual hydration status, stress level, and short-term dietary habits (Perry et al. 2007). However, this investigation still resulted in a weak positive correlation between gene copy number and protein levels. Next, variations between large populations deemed either low or high starch diets were examined. For the high-starch populations, two agricultural populations, European-Americans (n = 50) and Japanese (n = 45) and Hadza hunter-gatherers group (n = 38) were sampled (Perry et al. 2007). While for the low-starch population, the Biaka (n = 36) and Mbuti (n = 15), rainforest hunter-gatherers, Datog pastoralists (n = 17), and the Yakut, a pastoralist/fishing society (n = 25) were sampled (Perry et al. 2007). Perhaps expectedly, the average mean of AMY1

Selenite , as an oral form of selenium, reduces oxidation-induced apoptosis, via blocking of the serine/threonine kinase ASK1 and its downstream pathway SEK1- JNK (Yoon et al. 2002; Savaskan et al. 2003).