Pernicious Anemia Case Analysis

Abstract

The cardiac, digestive, and immune systems are all highly interconnected systems that communicate with one another through cytokines, hormones, and neurotransmitters. Many physical or psychological stresses may disrupt their equilibrium, resulting in inflammation, endothelial dysfunction, tissue damage, and other problems. Here, we study and evaluate Teri’s case systems to comprehend their independence and collaboration in keeping her body functioning effectively. This research will look at how this information affects overall physiological health, especially the composition and function of hematocrit, antibodies, and immunoglobulins, all of which are important immune and cardiovascular systems components. It will also highlight the need for a multidisciplinary approach to health care, in which medical specialists collaborate to address complex health conditions caused by imbalances in several physiological systems. ALL bodily systems interact with one another in big and little ways for our bodies to function and thrive. Nobody can live without others. Moreover, the body cannot function without one of the systems and their critical linkages.

Pernicious Anemia Case Analysis

Many health issues and diseases occur when the cardiovascular, immune, and digestive systems fail because they are key organ systems that work together to keep the body healthy. Teri’s predicament exemplifies the complicated interaction of various systems in protecting the body’s overall health. This article investigates the relationships between these systems and how they influence Teri’s health in light of her diagnosis of pernicious anemia. We also investigate the roles of hematocrit, antibodies, and immunoglobulins in maintaining normal body processes. This article’s fundamental argument is the need for a multidisciplinary approach to healthcare, in which healthcare experts collaborate to tackle complex health problems caused by imbalances in various physiological systems.

Teri Is Deficient in Which Substance as A Result of the Destruction of the Parietal Cell?

Teri’s missing chemicals in her body due to degradation must be identified to treat her and care for her sickness. In her instance of pernicious anemia, or the loss of parietal cells in the stomach, she is deficient in a critical chemical essential for overall bodily health. Pernicious anemia is a kind of megaloblastic anemia caused by a deficiency of vitamin B12 (cobalamin). DNA synthesis requires vitamin B12 (Vit.B12). Vitamin B12 is absorbed in the terminal ileum in conjunction with the intrinsic factor, which is secreted by parietal cells in the stomach. Intrinsic factor antibodies in PA obstruct ileum vitamin B12 absorption by inhibiting intrinsic factor binding to vitamin B12 (Murphy et al., 2015). PA also includes antibodies against parietal cells, which have been linked to atrophic gastritis. Autoimmune atrophic gastritis is caused by an autoimmune response involving parietal cell antibodies.

As a result, parietal cells, which border the stomach, generate hydrochloric acid (HCl) and intrinsic factor (IF). Although IF necessitates vitamin B12 absorption in the small intestine, the primary function of HCl is to lower the stomach’s pH to help digestion (Murphy et al., 2015). Parietal cell antibodies destroy parietal cells, lowering the intrinsic factor produced by parietal cells. Because of this deficiency, vitamin B12 is malabsorbed, lowering the amount of vitamin B12 in circulation. Vitamin B12 is required for both red blood cell production and the proper functioning of the nervous system. A shortage of vitamin B12 may cause megaloblastic anemia since the body cannot produce healthy red blood cells without it (Sun et al., 2012). This kind of anemia is characterized by large, light red blood cells incapable of delivering oxygen effectively. Additionally, a lack of vitamin B12 may impair the nerve system, resulting in symptoms such as tingling in the hands and feet, muscular weakness, and difficulty walking.

Is There a Link Between Vitamin B12 Deficiency and Parietal Cell Destruction?

Pernicious anemia develops when the body is deficient in vitamin B12. This vitamin is only needed in trace amounts by the body, although it is essential. Vitamin B12 is available in many meals, but its absorption requires a second molecule made by the stomach. This second component is referred to as the intrinsic factor. As the stomach lining atrophies (degrades), it no longer produces intrinsic factors and hydrochloric acid (Murphy et al., 2015). An alteration that happens with age is the atrophy of the stomach lining.

Vitamin B12 is stored in the body. This shop may endure for years since it is required to produce red blood cells (RBCs) and properly function the brain and nerve system. Anemia develops when this is finally exhausted. Unlike other types of anemia, pernicious anemia does not need blood loss or an iron deficit. As a result, when parietal cells die, as occurs in pernicious anemia (Sun et al., 2012), there is insufficient IF. Since the body cannot absorb vitamin B12 without IF, there is less in the blood. This insufficiency might lead to anemia and decreased red blood cell formation over time (RBCs).

Teri Is Deficient in Pepsin as A Result of Her Condition. Please Explain Why.

Parietal cells in the stomach lining release hydrochloric acid, which lowers the stomach’s pH. Pepsin is activated by a low pH (1.5 to 2). Acetylcholine, gastrin, and histamine activate the proton pump in parietal cells, releasing hydrogen ions and causing the pH to fall. For protein digestion, pepsin requires an acidic environment. As a result, it works best at pH levels ranging from 1.5 to 2. Pepsinogen may cleave itself and create active pepsin when the pH is low. As it reaches the duodenum, however, it becomes inactive when the pH climbs over 6. (Dutta & Dr. Sanchari, 2018).

Nevertheless, protein digestion continues in the small intestines due to the actions of pancreatic enzymes such as trypsin, chymotrypsin, elastase, and carboxypeptidase. As a result, pepsin is not required for life, and protein digestion may still proceed without pepsin. It is worth noting that pepsin stays structurally stable until at least an 8; therefore, it can always be reactivated if the pH remains below 8, explaining why Teri’s predicament is still curable.

Producing HCl and intrinsic factors reduce pernicious anemia caused by parietal cell autoimmune death. The less acidic environment in the stomach induced by the reduction in HCl generation impedes pepsinogen activation into pepsin (Murphy et al., 2015). Pepsin activity and production fall as a result, resulting in pernicious anemia. Without pepsin, protein digestion may be hampered, resulting in gastrointestinal symptoms such as bloating, indigestion, and diarrhea. Undigested proteins may also reach the small intestine and cause inflammation, leading to nutritional loss and other problems.

Describe What Teri’s RBCs Would Look Like if She Were Healthy.

Teri’s RBCs would be small, spherical, and red if healthy. They would also be concave, which increases surface area and enhances oxygen transport capacity. Healthy RBCs are biconcave, meaning they have a thin concave disc on both sides with a 6-8 micrometers diameter. A typical RBC count would be males 4.0 to 5.9 x 1012/L, women 3.8 to 5.2 x 1012/L, with women having a lower RBC count than men, with the number of red blood cells decreasing with age. The biconcave shape of RBCs increases their surface area-to-volume ratio, enabling them to fit through narrow capillaries and perform their gas exchange function more efficiently (Dutta & Dr. Sanchari, 2018).

Additionally, healthy RBCs include hemoglobin, a protein that attaches to and carries oxygen throughout the body, giving them a crimson tint. Because of hemoglobin, RBCs have a characteristic red hue, and the quantity of hemoglobin impacts how vivid the color is. RBCs in optimal health have the proper size, shape, and color to transport oxygen throughout the body.

What Exactly is Hematocrit?

Hematocrit is the proportion of red cells in your blood by volume. Red blood cells, white blood cells, and platelets are suspended in plasma to form blood. They make up around 45% of human blood volume, although the percentages of each might vary. RBCs take up a specified proportion or fraction of the blood volume. Normal hematocrit levels vary depending on age and race. Men’s normal levels in adulthood range from 41% to 50%. The usual range for women is lower: 36% -44 %. Hematocrit is an important indicator of blood health since it indicates how efficiently the blood can transport oxygen.

Hemoglobin, a protein in red blood cells, binds to oxygen and carries it throughout the body. Thavendiranathan et al. (2005) define anemia as a hematocrit level below the normal range, indicating that the individual has too few red blood cells. A hematocrit result that is higher than normal, indicating an excess of red blood cells may suggest polycythemia or erythrocytosis. Hematocrit is a useful diagnostic tool since it indicates how healthy a person’s blood is and how efficiently it can transport oxygen.

Which of Her Body’s Mechanisms Is Stimulated by Low Oxygen Levels to Produce More RBCs?

This process, known as erythropoiesis, is carefully controlled by an evolved oxygen-sensing system to keep RBC counts within a restricted physiological range of 1- 3. Erythropoietin (EPO), a cytokine released by the kidney in response to low blood oxygen tension, is important to this process. Circulating EPO interacts with its cognate receptor (EPOR) on bone marrow erythroid progenitors, activating numerous signaling pathways that promote RBC development. Hematologic stem cells transform into erythroblasts, the building blocks of red blood cells, during erythropoiesis (RBCs).

As they mature, erythroblasts generate hemoglobin, the protein that binds oxygen and gives RBCs their unique red color. After the nuclei of erythroblasts are ejected, they grow into reticulocytes, which are immature RBCs. Reticulocytes circulate in the circulation for around 1-2 days before maturing into RBCs. RBC synthesis must increase in response to low oxygen levels for tissues to continue obtaining enough oxygen. Polycythemia, a condition characterized by abnormally high RBC levels in the blood, may occur from excessive RBC production (Sun et al., 2012). Blood clots and other complications may arise due to polycythemia’s propensity to thicken blood, making it more difficult for the heart to pump blood.

What Protein Describes the Structure of the Oxygen Transported by Our Bodies?

The protein hemoglobin is a molecule that transports almost all the oxygen in the blood. It comprises four subunits, each with a heme group and a globin chain. The heme group comprises a porphyrin ring with an iron (Fe) atom in the core. Usually, the Fe is in the +2 redox state (ferrous) and may bind oxygen reversibly. In humans, at least six genes influence globin synthesis, creating six structurally distinct polypeptide chains known as and chains (Dutta & Dr. Sanchari, 2018). All normal and pathological hemoglobin molecules are tetramers of two distinct pairs of polypeptide chains, each forming a monomeric component.

As oxygen attaches to hemoglobin, the protein changes shape, making additional oxygen molecules connect to it easier. Hemoglobin may transport oxygen from the lungs to the tissues where it is required by using cooperative binding. Changes in the heme group or amino acid sequence might impair hemoglobin’s capacity to bind to oxygen, making hemoglobin’s structure critical to its function.

What Cell Secretes Antibodies, and How Do Antibodies Carry Out Their Many Functions?

Antibodies are produced by white blood cells, known as B cells. Antibiotics may recognize and bind to certain antigens, such as infections or foreign chemicals. Antibodies binding to antigens may neutralize them, activate complement proteins, or induce phagocytosis (Dutta & Dr. Sanchari, 2018). Immunoglobulins, often known as antibodies, are produced by plasma cells, a B cell triggered by an antigen.

The principal applications of antibodies include Neutralization: Antibodies, by binding to a pathogen’s surface features, might directly inhibit the pathogen’s capacity to infect cells, hence minimizing harm. Antibodies may label infections or foreign substances, allowing immune cells such as phagocytes to eat and eliminate the marked cells swiftly. Antibodies may activate complements, a group of proteins that work together to eliminate infections by creating holes in their membranes and prompting immune cells to destroy them. Certain antibodies, for example, may guide natural killer cells to attack and destroy contaminated or cancerous cells. It is called antibody-dependent cellular cytotoxicity (ADCC) (Dutta & Dr. Sanchari, 2018). Antibodies are critical components of the immune response and are required to protect our bodies from infections and other potentially harmful chemicals.

What Are the Several Varieties of Antibodies and Their Two Characteristics?

According to Dutta and Dr. Sanchari (2018), the biggest antibody and main antibody generated during an initial immune response may complement proteins and promote phagocytosis. It is often found in blood and lymph fluid. IgG, the most common antibody in the body, can neutralize toxins, opsonizing infections, and cross the placenta to provide passive immunization to the baby. It also has a long half-life, allowing it to provide pathogen resistance over time.

Second, large quantities of IgA are found in biological fluids such as saliva, tears, and breast milk, which help prevent infections from entering the body. It helps to boost mucosal immunity by scavenging viruses and bacteria. Ultimately, IgE contributes to allergic responses as well as parasite infection resistance. As histamine attaches to allergens, it releases histamine and other chemicals, causing allergic symptoms such as hives and itching. Finally, IgD is a low-level blood protein with an unknown function but is considered to contribute to B cell activation.

Describe the Structure of Immunoglobulin.

Immunoglobulins, or antibodies, are Y-shaped proteins with four polypeptide chains: two identical heavy chains and two identical light chains connected by disulfide bonds. The variable regions of the light and heavy chains generate two antigen-binding sites that act together to identify and bind to certain antigens. Moreover, the heavy chains have a consistent region that specifies the antibody class, such as IgM, IgG, IgA, IgE, and IgD. (2018) (Dutta & Dr. Sanchari). The distribution and functions of each type are different. Immunoglobulins are critical components of the immune system since they neutralize infections and promote phagocytosis and the complement system. Because of their structure, they can identify and bind to various antigens.

Teri’s experience, in the end, demonstrates the importance of understanding how the different physiological systems in the human body interact. Pernicious anemia is caused by a shortage of vitamin B12, oxygen, and pepsin caused by the loss of parietal cells in the stomach. It appears as depression, convulsions, and abnormal RBCs. It is important to know how the different parts of the immune, cardiovascular, and digestive systems work together to find and treat these diseases. Moreover, the proper functioning of the body depends on the structures and activities of hematocrit, antibodies, and immunoglobulins. A lack or malfunction in any of these sections might have catastrophic consequences. Teri’s example underscores the need for comprehensive and integrated approaches to healthcare, emphasizing the importance of interdisciplinary collaboration among healthcare providers.

Reference

Dutta & Dr. Sanchari Sinha. “Types of Antibodies.” News, 20 Dec. 2018, https://www.news-medical.net/life-sciences/Types-of-Antibodies.aspx

Murphy, G., Dawsey, S. M., Engels, E. A., Ricker, W., Parsons, R., Etemadi, A., … & Freedman, N. D. (2015). Cancer risk after pernicious anemia in the US elderly population. Clinical Gastroenterology and Hepatology, 13(13), 2282-2289.

Sun, A., Lin, H. P., Wang, Y. P., & Chiang, C. P. (2012). Significant association of deficiency of hemoglobin, iron, and vitamin B12, high homocysteine level, and gastric parietal cell antibody positivity with atrophic glossitis. Journal of oral pathology & medicine, 41(6), 500-504.

Thavendiranathan, P., Bagai, A., Ebidia, A., Detsky, A. S., & Choudhry, N. K. (2005). Do blood tests cause anemia in hospitalized patients? The effect of diagnostic phlebotomy on hemoglobin and hematocrit levels. Journal of general internal medicine, 20, 520-524.