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Sickle cell disease (SCD), also simply called sickle cell, is a group of hemoglobin-related blood disorders that are typically inherited. [2] The most common type is known as sickle cell anemia. [2] Sickle cell anemia results in an abnormality in the oxygen-carrying protein haemoglobin found in red blood cells. [2]
The hemoglobin structural variants can be broadly classified as follows: [19] Sickle cell disorders, which are the most prevalent form of hemoglobinopathy. Sickle hemoglobin (HbS) is prone to polymerize when deoxygenated, precipitating within the red blood cell. This damages the RBC membrane resulting in its premature destruction and consequent ...
The sickle cell trait provides a survival advantage against malaria fatality over people with normal hemoglobin in regions where malaria is endemic. The trait is known to cause significantly fewer deaths due to malaria, especially when Plasmodium falciparum is the causative organism.
Hemoglobin C is found most abundantly in areas of West Africa, such as Nigeria, where Yorubas live. [15] [16] [17] Hemoglobin C gene is found in 2-3% of African-Americans [4] while 8% of African-Americans have hemoglobin S (Sickle) gene. Thus Hemoglobin SC disease is significantly more common than Hemoglobin CC disease.
Hemoglobin S (α 2 β S 2) – A variant form of hemoglobin found in people with sickle cell disease. There is a variation in the β-chain gene, causing a change in the properties of hemoglobin, which results in sickling of red blood cells.
As the amount of fetal hemoglobin decreases and hemoglobin S increases, a mild hemolytic anemia appears in the early stage of development. Patients with this disease experience some of the symptoms of sickle cell anemia, including mild-moderate anemia, increased risk of infection, and painful sickling crises. [5]
For people living with the disease, a sickle cell crisis can happen at any time. When it does, their rigid, sickle-shaped red blood cells become stuck in their blood vessels, blocking flow and ...
Hemoglobin D has the basic structure and composition of normal adult hemoglobin. It is a globular protein containing prosthetic (non-protein) group called heme. There are four individual peptide chains, namely two α- and two β-subunits, each made of 141 and 146 amino acid residues, respectively.