F11R Human
Description
Cellular Expression and Localization
F11R is expressed in multiple cell types and tissues:
Subcellular localization:
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Tight junctions: Anchored to cytoskeletal proteins via PDZ interactions .
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Luminal surface: Exposed in inflamed endothelial cells, promoting platelet adhesion .
Tight Junctions and Barrier Function
F11R stabilizes epithelial and endothelial barriers by:
Platelet Activation and Thrombosis
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Adhesion: Binds platelet F11R to endothelial F11R under inflammatory conditions .
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Aggregation: Mediates platelet-platelet interactions via D1 domain .
Leukocyte Transmigration
Pathological Roles
RNA Editing
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A-to-I editing in the 3'UTR by ADAR1 enhances mRNA stability under hypoxia .
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Hyper-edited transcripts: Retained in the nucleus, reducing protein translation .
Phosphorylation
| Modification | Enzyme | Functional Impact | References |
|---|---|---|---|
| N-glycosylation | Oligosaccharyltransferase | Dimer stabilization, barrier function | |
| Phosphorylation | Kinases (e.g., Src) | TJ disassembly, cell migration |
Recombinant Proteins
F11R is produced in E. coli as a non-glycosylated, His-tagged protein (25.8 kDa) for functional studies .
| Property | Detail | Source |
|---|---|---|
| Sequence | 238 amino acids (26-238 a.a.) | |
| Purity | >90% (SDS-PAGE) | |
| Applications | Reovirus binding assays, platelet activation studies |
Gene Editing
Product Specs
RAFSNSSYVL NPTTGELVFD PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGV.
Product Science Overview
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 .
