Glycophorin A (GYPA)

Glycophorin A is the major sialoglycoprotein of the human erythrocyte (red blood cell) membrane, encoded by the GYPA gene. It forms as a single-pass transmembrane protein, heavily glycosylated (approximately 60%), with abundant sialic acid residues contributing to the negative surface charge and hydrophilic properties of the red cell membrane[2][3][4][5][6]. Glycophorin A functions as the carrier of the antigenic determinants for the M and N blood groups—key components in transfusion medicine[3][10]. It exists mainly as a dimer in the cell membrane and participates in interaction with the band 3 anion transporter (anion exchanger 1), influencing the trafficking and activity of this transporter in red blood cells[1]. Variants and mutations in Glycophorin A give rise to numerous blood group phenotypes and have been associated with protection against certain severe malaria infections[3][6]. Although not a direct pharmacological target, Glycophorin A is an important biomarker for blood group typing and erythroid cell identification[3][10].

Other names

CD235aMN sialoglycoproteinMNS blood group glycoproteinsialoglycoprotein A

Not applicable for standard pharmacology; anti-GPA antibodies may mediate cell depletion (e.g., in laboratory or rare clinical settings)