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Expression of phosphatidylserine (PS) on wild‐type and Gerbich variant erythrocytes following glycophorin‐C (GPC) ligation
Author(s) -
Head David J.,
Lee Zoe E.,
Poole Joyce,
Avent Neil D.
Publication year - 2005
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.2005.05407.x
Subject(s) - phosphatidylserine , biology , glycophorin , microbiology and biotechnology , red blood cell , biochemistry , immunology , antigen , phospholipid , membrane
Summary Glycophorin‐C (GPC) is a 40 kDa glycoprotein expressed on erythrocytes and is a receptor for the malarial parasite Plasmodium falciparum to invade these cells. A link between GPC binding (ligation) and phosphatidylserine (PS) expression on erythrocytes has been suggested by its appearance on P. falciparum ‐infected erythrocytes. Phosphatidylserine expression has also been shown to be a marker of cellular death in a number of biological pathways including some in erythrocytes. Using Annexin V binding, we demonstrated that ligation of GPC with mouse mAb (BRIC‐10) induced PS expression on normal erythrocytes. Phosphatidylserine exposure was prevented following tryptic digestion of intact erythrocytes. In addition, GPC variant phenotypes Yus (Δ exon 2) and Gerbich (Δ exon 3), which express a truncated extracellular domain, did not express PS following BRIC‐10 binding, whereas PS was exposed on Ls a erythrocytes (duplication of exon 3). GPC ligation was also shown to result in a concomitant loss of erythrocyte viability in wild‐type erythrocytes after 24 h in vitro . These results identify a potential pathway linking GPC to PS exposure on erythrocytes that may have a role in regulating red cell turnover. Further characterization of this pathway may also identify new targets for the treatment of P. falciparum malaria.