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Glycophorin C (GYPC) is an integral, highly glycosylated membrane sialoglycoprotein primarily found in the human erythrocyte membrane[1][2][3]. It plays a key structural role by interacting with cytoskeletal proteins such as protein 4.1 and p55, helping maintain erythrocyte shape and mechanical stability[1][3]. GYPC is also the carrier of Gerbich blood group antigens, and genetic variants result in distinct blood group phenotypes, some associated with hereditary elliptocytosis (a disorder of red cell architecture)[1][3]. Through its extracellular domain, Glycophorin C acts as a receptor for the Plasmodium falciparum erythrocyte binding antigen (EBA-140), mediating parasite entry in malaria[1][2][3]. There is no current therapeutic drug targeting GYPC, but its relevance in transfusion medicine (blood compatibility) and infection biology (malaria) makes it an important molecule for clinical and research interests[1][2][3].
For malaria: Mediation of parasite (Plasmodium falciparum) binding and erythrocyte invasion
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