Glycophorin

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Glycophorin is a sialic acid-rich glycoprotein found in the plasma membrane of red blood cells. It plays a crucial role in maintaining the stability and functionality of the red blood cell membrane. Glycophorin is also significant in the context of blood group antigens and malaria infection.

Structure[edit | edit source]

Glycophorin is a transmembrane protein that spans the lipid bilayer of the red blood cell membrane. It consists of an extracellular domain rich in sialic acid, a single transmembrane helix, and a cytoplasmic tail. The extracellular domain is heavily glycosylated, contributing to the negative charge on the red blood cell surface.

Function[edit | edit source]

The primary function of glycophorin is to provide structural support to the red blood cell membrane. The sialic acid residues on glycophorin contribute to the cell's negative surface charge, which helps prevent red blood cells from clumping together. Additionally, glycophorin serves as a receptor for certain pathogens, including the Plasmodium falciparum parasite responsible for malaria.

Blood Group Antigens[edit | edit source]

Glycophorin is associated with several blood group antigens, including the MNS antigen system. Variations in the glycophorin gene can lead to different blood group phenotypes, which are important in blood transfusion compatibility and hemolytic disease of the newborn.

Clinical Significance[edit | edit source]

Mutations or alterations in glycophorin can lead to various medical conditions. For example, changes in glycophorin expression or structure can affect red blood cell stability, leading to conditions such as hereditary spherocytosis. Additionally, glycophorin serves as a binding site for the malaria parasite, making it a target for research in malaria prevention and treatment.

Research[edit | edit source]

Ongoing research is focused on understanding the role of glycophorin in red blood cell physiology and its interactions with pathogens. Studies are also exploring the potential of glycophorin as a therapeutic target for preventing malaria infection.

See Also[edit | edit source]

References[edit | edit source]

External Links[edit | edit source]


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Contributors: Prab R. Tumpati, MD