Glycophorin A: Difference between revisions
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Latest revision as of 13:53, 17 March 2025
Glycophorin A (GPA) is a protein that is encoded by the GYPA gene in humans. It is a member of the glycophorin family and plays a crucial role in the structure and function of red blood cells.
Structure[edit]
Glycophorin A is a transmembrane protein that spans the cell membrane of red blood cells. It is composed of 131 amino acids and has a molecular weight of approximately 16 kDa. The protein has a single transmembrane domain, a short cytoplasmic tail, and a large extracellular domain that is heavily glycosylated.
Function[edit]
The primary function of glycophorin A is to maintain the shape and flexibility of red blood cells. It achieves this by interacting with other proteins in the cell membrane, such as spectrin and actin, to form a network that provides structural support to the cell. Glycophorin A also plays a role in the cell adhesion process, which is important for the formation of red blood cell aggregates, or rouleaux.
Clinical significance[edit]
Mutations in the GYPA gene can lead to a variety of blood disorders, including hereditary elliptocytosis and hereditary spherocytosis. These conditions are characterized by abnormal red blood cell shapes and can lead to anemia, jaundice, and splenomegaly. Glycophorin A is also the receptor for the Plasmodium falciparum parasite, which causes malaria.
See also[edit]
References[edit]
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