F11R Human

The F11 receptor was first identified and characterized in 1990 as a glycoprotein expressed on the surface of human platelets . Later, in 1998, its presence was described at tight junctions of vascular endothelial and epithelial cells, where it was referred to as JAM-1 or JAM-A . The recombinant form of this protein is typically expressed in HEK293 cells and is known for its high biological activity and stability .

F11R plays a significant role in platelet activation, aggregation, and adhesion. It is involved in the initial steps of atherogenesis, where exposure of endothelial cells to pro-inflammatory cytokines leads to the insertion of F11R molecules into the luminal surface of ECs. This results in homologous interactions between F11R molecules of platelets and ECs, causing the adhesion of platelets to the inflamed ECs .

The de novo transcription and translation of F11R in ECs are crucial for this process. Inhibition of F11R transcription and translation significantly blocks the adhesion of human platelets to inflamed ECs, highlighting its importance in the initiation of atherogenesis, which can lead to atherosclerosis, heart attacks, and strokes .

Elevated levels of soluble F11R (sF11R) have been associated with various cardiovascular diseases, including hypertension and coronary artery disease (CAD). Genetic variants in the human F11R gene have been shown to influence systolic blood pressure, and higher levels of sF11R have been detected in hypertensive patients compared to normotensive individuals . Additionally, sF11R levels correlate with systolic and diastolic blood pressures, further supporting its role in the pathophysiology of hypertension .

Research on F11R has provided valuable insights into its role in inflammatory thrombosis and its potential as a therapeutic target. The recombinant form of F11R is used in various experimental studies to understand its function and to develop potential therapeutic interventions for cardiovascular diseases .