Recombinant Human Glycophorin C/GPC protein (His tag)

Supplementary information

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

Glycophorin C also known as GPC is a membrane glycoprotein with a molecular mass of approximately 32 kDa. GPC is recognized by other names such as Glycophorin A-like and it is a significant component of the erythrocyte membrane. Researchers frequently refer to glycophorin C by its common abbreviation GPC. GPC expression occurs specifically in red blood cells where it plays a role in maintaining the cell structure and integrity by forming part of the interface between the cell membrane and the cytoskeleton.

Biological function summary

Glycophorin C modulates red blood cell characteristics by interacting with band 4.1 protein complex. The protein participates in the regulation of cell shape and mechanical flexibility which are important for the red blood cells to flow through capillaries effectively. This process involves interactions with spectrin and actin within the cytoskeleton underpinning the cellular architecture. The protein's function as an anchor for the band 4.1 complex links it with other glycophorins such as Glycophorin A.

Pathways

GPC integrates into erythrocyte membrane-associated pathways supporting membrane stability. It is key to the cytoskeleton-membrane linkage pathway where it interacts with proteins like spectrin and actin. Aimed at preserving the biconcave shape of erythrocytes these interactions enhance membrane elasticity and durability ensuring proper red blood cell function in the circulation. Additionally its association with the protein Rh-linked ankyrin connects GPC with pathways involving erythrocyte ion transport processes.

GPC plays a notable role in elliptocytosis and malaria. Elliptocytosis arises from mutations affecting GPC and other erythrocyte proteins such as band 4.1 leading to elongated and dysfunctional erythrocytes. Individuals with altered GPC expression show increased susceptibility or resistance to malaria caused by the Plasmodium parasite’s interaction with erythrocyte membrane proteins. Glycophorin C therefore remains an important focus of study for understanding the molecular basis of these conditions and designing therapeutic interventions.