Recombinant Human GYPC protein (His tag)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The protein GYPC also known as Glycophorin C is integral to the red blood cell membrane. It is a small protein with a molecular weight of approximately 31 kDa. GYPC is predominantly expressed on the surface of erythrocytes where it plays a role in maintaining cell shape and stability. This protein helps anchor the membrane to the underlying cytoskeleton providing structural integrity to red blood cells. GYPC interacts with other proteins in the membrane to facilitate these mechanical functions.

Biological function summary

Glycophorin C acts as a part of the larger membrane complex involving other glycophorins. It contributes to the cellular recognition and signaling processes. This protein also plays a role in the receptor activity for plasmodium species which is critical in certain bloodstream infections. GYPC aids in maintaining membrane integrity by interacting with cytoskeletal proteins such as ankyrin influencing the deformation and mechanical properties of erythrocytes.

Pathways

The role of Glycophorin C involves hematological and immunological pathways. It participates in the ankyrin-spectrin cytoskeletal network pathway which is key in stabilizing the membrane structure of red blood cells. This pathway involves other proteins like spectrin and band 3 protein which work alongside GYPC to manage cell shape and resilience. Additionally GYPC engages with immune response pathways interacting with various surface receptors and transporters important in pathogen recognition and response.

Glycophorin C has been associated with malaria susceptibility and hereditary elliptocytosis. Malaria-causing parasites exploit GYPC as a receptor to invade red blood cells highlighting its role in this infectious disease. Additionally mutations or alterations in the GYPC gene or protein can lead to hereditary elliptocytosis a condition characterized by abnormal red blood cell shapes. In this disorder defective GYPC disrupts interactions with the cytoskeleton such as with ankyrin and spectrin causing cell fragility and hemolysis.