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Selenium is an essential micronutrient that plays a crucial role in development and a wide variety of physiological processes including effect immune responses. The immune system relies on adequate dietary selenium intake and this nutrient exerts its biological effects mostly through its incorporation into selenoproteins. The selenoproteome contains 25 members in humans that exhibit a wide variety of functions. The development of high-throughput omic approaches and novel bioinformatics tools has led to new insights regarding the effects of selenium and selenoproteins in human immuno-biology. Equally important are the innovative experimental systems that have emerged to interrogate molecular mechanisms underlying those effects. This review presents a summary of the current understanding of the role of selenium and selenoproteins in regulating immune cell functions and how dysregulation of these processes may lead to inflammation or immune-related diseases.

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As a web developper I love writing integration tests to ensure my code is still running properly after every commit / deploy.

I used to have docker + selenium and it looks like :

Here is my previous post about running tests on docker ( @sbounmy/docker-compose-rails-react-selenium-capybara-65fa74250fa7)

After moving to Bubble and my app grew bigger it become essential to write tests.

I could have write my own custom code to test my bubble app however

It would be great to be able to create an app that write tests against a bubble app so other people can test their code too !

However a few questions strikes me :

It would be a real hack job, but have a selenium script outside of Ignition running periodically (via a cronjob or similar) that writes expected output to a file. You could then use Ignition to read in that file via a Gateway Event script and process out the result.

The essential trace mineral, selenium, is of fundamental importance to human health. As a constituent of selenoproteins, selenium has structural and enzymic roles, in the latter context being best-known as an antioxidant and catalyst for the production of active thyroid hormone. Selenium is needed for the proper functioning of the immune system, and appears to be a key nutrient in counteracting the development of virulence and inhibiting HIV progression to AIDS. It is required for sperm motility and may reduce the risk of miscarriage. Deficiency has been linked to adverse mood states. Findings have been equivocal in linking selenium to cardiovascular disease risk although other conditions involving oxidative stress and inflammation have shown benefits of a higher selenium status. An elevated selenium intake may be associated with reduced cancer risk. Large clinical trials are now planned to confirm or refute this hypothesis. In the context of these health effects, low or diminishing selenium status in some parts of the world, notably in some European countries, is giving cause for concern.

Five selenium-containing glutathione peroxidases (GPx1-4 and GPx6) have been identified: GPx1 (cytosolic GPx), GPx2 (epithelial cell-specific GPx expressed in intestinal lining and lungs), GPx3 (highly expressed in thyroid gland and kidneys), GPx4 (phospholipid-hydroperoxide GPx; PHGPx), and GPx6 (expressed in the olfactory epithelium) (4). GPx isoenzymes are all antioxidant enzymes that reduce potentially damaging reactive oxygen species (ROS), such as hydrogen peroxide and lipid hydroperoxides, to harmless products like water and alcohols by coupling their reduction with the oxidation of glutathione (Figure 2). Spermatogenesis and male fertility are highly dependent on GPx4 and selenoprotein P (SEPP1; see below). In the testes, GPx4 reduces phospholipid hydroperoxides, hence protecting immature spermatozoa cells against oxidative stress. GPx4 is also a major structural protein of the capsule embedding mature sperm mitochondrial helix involved in sperm motility. SEPP1 is essential for selenium supply to the testes, and animal models lacking the SEPP1 gene are infertile due to poor selenium tissue bioavailability, defective GPx4 synthesis, and impaired sperm maturation (5).

The thyroid gland releases very small amounts of biologically active thyroid hormone (triiodothyronine or T3) and larger amounts of an inactive form of thyroid hormone (T3 precursor: thyroxine or T4) into the circulation. Most of the biologically active T3 in the circulation and inside cells is generated by the removal of one iodine atom from T4 in a reaction catalyzed by selenium-dependent iodothyronine deiodinase enzymes. Two different selenium-dependent iodothyronine deiodinases (DIOs type 1 and 2) can deiodinate T4, thus increasing circulating T3, while a third iodothyronine deiodinase (DIO type 3) can convert both T3 and T4 to inactive metabolites (Figure 3) (8). Of note, inactivation of the genes encoding DIOs in rodent models has revealed a role for DIO type 1 in iodine homeostasis and the importance of DIOs type 2 and 3 in the maturation of auditory and visual systems during fetal development (8). Thus the importance of selenium in normal development, growth, and metabolism is not limited to its role in the regulation of thyroid gland function.

Selenoprotein P (SEPP1) is predominantly produced by the liver, a major storage site for selenium, and secreted in the plasma. The full-length glycoprotein contains a selenium-rich domain with nine selenocysteine residues, as well as a thioredoxin-like catalytic site with one selenocysteine residue. SEPP1 constitutes the major form of selenium transport to peripheral tissues (9). SEPP1 also functions as an antioxidant that protects cells from oxidative damage by enabling full activity of thioredoxin reductases and glutathione peroxidases through adequate supply of selenium to extrahepatic tissues (see Glutathione peroxidases). SEPP1 appears to be especially critical for selenium homeostasis in the brain and testes where apolipoprotein E receptor 2 (apoER2) facilitates the uptake of SEPP1. Megalin is another SEPP1-specific lipoprotein receptor that helps limit urinary selenium loss through SEPP1 re-uptake by the kidneys (10). Moreover, SEPP1 has been recently implicated in the regulation of glucose metabolism and insulin sensitivity (11).

Selenoprotein W (SEPW or SelW) exists in different isoforms (homologues) and is highly conserved across species. In humans, SEPW is expressed in numerous tissues, with highest levels found in skeletal muscle and heart (12). SEPW contains a selenocysteine residue and a cysteine residue that binds to a glutathione molecule, suggesting a role in redox regulation (13). The expression of SEPW is correlated with selenium status and appears to be sensitive to low-selenium supply (14, 15). SEPW expression in the brain has been found to confer protection against oxidative stress-induced neuronal cell death (16). SEPW also appears to be a negative regulator for 14-3-3 proteins. Indeed, 14-3-3 inhibition by SEPW in breast cancer cells was found to increase cell proliferation and cell survival through increasing resistance to genotoxic stress (17). In skeletal muscle cells, SEPW was shown to reduce the binding of 14-3-3 to TAZ, allowing TAZ translocation to the nucleus and subsequent activation of muscle cell differentiation genes (18). Finally, SEPW was found to prevent the degradation of the epidermal growth factor receptor (EGFR) in breast and prostate epithelial cells in culture. EGFR is constitutively activated in many tumors, and evidence of a role for SEPW in EGFR activation and signaling may help shed light on the relationship between selenium status and cancer risk (19).

The importance of selenium to biological systems, and specifically to the cellular redox (pro-oxidant/antioxidant) balance, is derived from its presence as selenocysteine in the catalytic site of selenoproteins (see Function). Other minerals that are critical components of antioxidant enzymes include copper (as superoxide dismutase), zinc (as superoxide dismutase), and iron (as catalase). Selenium acts in synergy with the antioxidant vitamins, vitamin C (ascorbic acid) and vitamin E (-tocopherol), by regenerating them from their oxidized forms and promoting maximal antioxidant protection (36-38).

While iodine is an essential component of thyroid hormones, the selenium-containing iodothyronine deiodinases (DIOs) are enzymes required for the conversion of thyroxine (T4) to the biologically active thyroid hormone, triiodothyronine (T3) (see Function). DIO1 activity may also be involved in regulating iodine homeostasis (39). The selenoenzymes, glutathione peroxidases, also play a critical role in thyroid function because they catalyze the degradation of peroxides generated during thyroid hormone synthesis (8). The epidemiology of coexisting iodine and selenium deficiencies in central Africa, but not in China, has been linked to the prevalence of myxedematous cretinism, a severe form of congenital hypothyroidism accompanied by mental and physical retardation. Selenium deficiency may be only one of several undetermined factors that might exacerbate the detrimental effects of iodine deficiency (40). Interestingly, selenium deficiency in rodents was found to have little impact on DIO activities as it appears that selenium is being supplied in priority for adequate synthesis of DIOs at the expense of other selenoenzymes (8).

Insufficient selenium intake may negatively affect the activity of several selenium-responsive enzymes, including glutathione peroxidases (GPx1 and GPx3), iodothyronine deiodinases, selenoprotein W, and methionine-R-sulfoxide reductase B1 (MsrB1). Even when severe, isolated selenium deficiency does not usually result in obvious clinical illness. Yet, compared to subjects with adequate selenium status, selenium-deficient individuals might be more susceptible to additional physiological stresses (41). Prolonged selenium deficiency may likely contribute to Keshan and Kashin-Beck diseases (see below). 17dc91bb1f