Diagnostic value of glycophorin-A in comparison with P57 immunohistochemical staining method in differentiating complete and partial molar pregnancies.
These results are consistent with malaria acting as a selective pressure on GYPA but also suggest that another selective force has resulted in a similar pattern of variation in Europeans. Accordingly GYPA has perhaps a more complex evolutionary history wherein on a global scale spatially varying selective pressures have governed its natural history.
Cell viability and surface expression of transferrin receptor (CD71) and glycophorin A (GPA) were analyzed before and after re-culture by flow cytometry. These studies show differential sensitivities of these surface proteins on K562 cells to proteases and suggest molecular mechanisms of transmembrane protein transport and cycling.
a complex structural rearrangement involving the loss of GYPB and gain of two GYPB-A hybrid genes reduces the risk of severe malaria by 40% and has recently increased in frequency in parts of Kenya
The authors show that Plasmodium falciparum EBA-175 mediates substantial changes in the deformability of erythrocytes by binding to glycophorin A and activating a phosphorylation cascade that includes erythrocyte cytoskeletal proteins resulting in changes in the viscoelastic properties of the host cell.
While weak interactions between glycophorin and band 3 undoubtedly exist glycophorin A and band 3 must have separate interactions in the membrane that control their lateral mobility.
Glycophorin-A-rich microparticles are released from evolving growing thrombi into the distal perfusing blood and can be measured in peripheral blood. CD235a(+) cMPs may constitute a novel systemic biomarker of ongoing thrombosis.
The authors demonstrate that the initial vacuolar membrane around internalized Babesia divergens is formed from protein and lipid components of the red blood cells plasma membrane including band 3 glycophorin A and spectrin.
These data demonstrate the importance of PfEBA175 regions other than the DBL domains in the interaction with GYPA and merit their inclusion in an EBA175-based vaccine.
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