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Human physiology, hazards and health risks
Published in Stephen Battersby, Clay's Handbook of Environmental Health, 2023
Revati Phalkey, Naima Bradley, Alec Dobney, Virginia Murray, John O’Hagan, Mutahir Ahmad, Darren Addison, Tracy Gooding, Timothy W Gant, Emma L Marczylo, Caryn L Cox
Red blood cells – There are approximately 5 million red blood cells per cubic mm of blood that contain the pigment haemoglobin, which is bright red in colour when combined with oxygen and is purple-blue in colour when no oxygen is present. Every 100 ml of blood has about 15 g of haemoglobin. Haemoglobin plays an important role in the carriage of not only oxygen but also of carbon dioxide. The life span of the red cell is about 120 days. It has no nucleus. The main requirements for the formation of red blood cells are iron, folic acid and vitamin B12. The hormone erythropoietin which is formed in the kidney also plays a role in the production of red blood cells.
Revolutionary Approaches of Induced Stem Cells in Disease Prevention
Published in Jyoti Ranjan Rout, Rout George Kerry, Abinash Dutta, Biotechnological Advances for Microbiology, Molecular Biology, and Nanotechnology, 2022
Sickle cell anemia is an inherited red blood cell disorder caused by a single point mutation in the β-globin gene of hemoglobin. The creation of induced pluripotent stem cell lines by gene targeting and replacement therapy repairs gene defects in hematopoietic progenitors. And the resulting progenitors produced normal red blood cells and cured the disease (Hanna et al., 2007). Cord blood is a suitable source of iPSCs due to its accessibility and minor genetic alterations (Giorgetti et al., 2009; Takenaka et al., 2009). Peripheral blood is another important source of iPSCs for instance; T-lymphocytes can be transformed into iPSCs using transient expression methods (Okita et al., 2013). This protocol can now be applied to many other diseases for which treatment or medicine.
Toxic Responses of the Blood
Published in Stephen K. Hall, Joana Chakraborty, Randall J. Ruch, Chemical Exposure and Toxic Responses, 2020
Hemoglobin is the oxygen-carrying protein of the red blood cells. The globin, or protein chains, has irregularly folded conformations that enclose the heme group in a hydrophobic pocket that forms the oxygen binding site. The active site of the heme group is a Fe2+ ion situated in a porphyrin ring. Of the two remaining coordination bonds, one is associated with an imidazole residue from the globin chain and the remaining bond is available for reversible binding with oxygen. No ligand is known to occupy this latter site in the case of deoxyhemoglobin. The reversible binding of oxygen by hemoglobin is called oxygenation. Four oxygen molecules bind to a hemoglobin. When the hemoglobin molecule is fully saturated, all four oxygen molecules are thought to be equivalent, and any one of them may be the first to be released. The release of the first oxygen, however, will greatly facilitate the release of the second oxygen molecule. In the same manner, the release of the second oxygen facilitates the release of the third oxygen. Release of the fourth oxygen does not occur under normal physiologic conditions.
Non-invasive and non-contact automatic jaundice detection of infants based on random forest
Published in Computer Methods in Biomechanics and Biomedical Engineering: Imaging & Visualization, 2023
Fatema-Tuz-Zohra Khanam, Ali Al-Naji, Asanka G. Perera, Danyi Wang, Javaan Chahl
Jaundice or hyperbilirubinemia is defined as the yellow discoloration of the skin and sclera of the eyes due to an excess level of bilirubin (Dzulkifli et al. 2018). Generally, jaundice is noticeable when serum bilirubin level exceeds 2.0 mg/dl in the blood (Puppalwar 2012). Bilirubin is a water-soluble tetrapyrrolic yellowish pigment that is present in the blood and whose excess accumulation in the skin results in neonatal jaundice symptoms (Ansong-Assoku and Ankola 2018). Bilirubin is created due to the breakdown of old red blood cells. In the human body, new red blood cells are produced, and old ones are broken down continuously. In an adult, the red blood cells survive for about 120 days; however, in a newborn infant, they survive for a significantly shorter time. Hence, newborns have higher than average quantities of red blood cells, which leads to excess bilirubin level due to the breakdown of more red blood cells (Ansong-Assoku and Ankola 2018). Normally, the damaged blood cells that produce bilirubin are metabolised by the liver for excretion. Later, bilirubin is secreted through urine and bile (Chee et al. 2018). Short-term excess of bilirubin is mostly harmless and self-limiting. But a high level of bilirubin in newborn infants is neurotoxic and can permanently damage the brain, which is called kernicterus. It may cause cerebral palsy, deafness or hearing loss, language difficulties, and developmental delay or can be fatal in the worst cases (Ullah et al. 2016; Chee et al. 2018).
A Novel Design of Epidermal Flexible Antenna on Supraorbital Nerve to Correlate Diabetes and Anemia
Published in IETE Journal of Research, 2023
Kannagi V, A Jawahar, Vijay Nath
Diabetic people have minimal or no insulin secretion from beta cells of the pancreas. The hormone insulin from the pancreas facilitates the liver and muscles to use glucose for energy. Insulin deficiency increases the blood glucose level, known as hyperglycemia. Diabetes is classified as type I and type II diabetes depending on insulin secretion. In type I diabetes, insulin secretion from the pancreas stops completely. This makes cells unable to process blood glucose and causes hyperglycemia. In type II diabetes, the cells do not respond to insulin secreted from the pancreas. The pancreas stops secreting insulin after prolonged diabetes. Left untreated, diabetes can cause blindness, anemia, and renal failure. Anemia reduces the levels of red blood cells and hemoglobin to lower their normal values in the blood.
A Deep Learning-based System for Detecting Anemia from Eye Conjunctiva Images Taken from a Smartphone
Published in IETE Technical Review, 2023
Bijit Basumatary, Rahul Shukla, Rakesh Kumar, Bodhisatwa Das, Ashish Kumar Sahani
Body ANEMIA is a condition in which the number or size of red blood cells, or the hemoglobin (Hb) concentration, falls below an established cut-off value, consequently impairing the capacity of the blood to transport oxygen around the body. The limited supply of oxygen in the body reduces physical and mental capacity. It raises the rates of maternal mortality and miscarriages in pregnant women and increases the occurrence of stillbirths, infant mortality, and low birth weight [1]. The Hb level needed to meet the physiological needs is differentiated according to gender, age group, and pregnancy condition. The major causes of anemia are nutritional deficiencies (particularly iron, folate, vitamins A, and B12 deficiency), hemoglobinopathies, and infectious diseases (such as malaria, tuberculosis, HIV, and parasitic infections) [2]. It is a severe condition worldwide; about 40% of pregnant women and 39.9% of children worldwide are anemic. Conditions are worse in South Asia, Central Africa, and West Africa. In India, 53% of women of reproductive age and 54% of children between 6 months to 4.9 years are anemic [3]. WHO targets to reduce anemia by 50% among women of reproductive age as per their “Global Nutrition Target 2025- Anemia” [4]. To achieve the given target, there is a requirement for time-efficient, cost-effective and easy-to-use tools to perform mass screening. However, the current standard methods for hemoglobin testing like Sahil’s test, Hemiglobincyanide Method, Vanzeetti’s Azide Methemoglobin, and Reagent-less method do not provide compelling evidence to achieve the same. Moreover, the chemicals employed in the tests are biohazardous and pollute the environment [5]. In India, the hemoglobin test costs up to Rs.100 as of 12 July 2021 [6].