Glycoprotein Ib platelet subunit beta (GP1BB)

Glycoprotein Ib platelet subunit beta (GP1BB) is an essential component of the GPIb-IX-V receptor complex, which is a major platelet surface receptor mediating adhesion to the subendothelial matrix at sites of vascular injury by binding to von Willebrand factor (VWF)[1][3][5][6][7]. The GP1BB subunit supports the expression and stability of the entire complex on the platelet surface and also participates in transmembrane signaling[3][6]. Defects or mutations in GP1BB cause Bernard-Soulier syndrome, a rare bleeding disorder characterized by abnormally large platelets, low platelet count (macrothrombocytopenia), and excessive bleeding, resulting from impaired platelet adhesion and aggregation[1][3][6][7]. GP1BB’s interaction with VWF is a key event in the initiation of primary hemostasis following vessel injury[5][6][7]. GP1BB has attracted interest as a therapeutic target for the modulation of thrombosis and bleeding, though direct-targeting drugs remain in early or experimental stages[5][6].

Other names

Platelet glycoprotein Ib beta chainGP1BBCD42cGP-Ib betaGPIb-betaGPIbBGPIbbetaAntigen CD42b-betaBDPLT1BS (Bernard-Soulier syndrome-related abbreviation)GPIBBPlatelet membrane glycoprotein Ib beta

Inhibitors or antibodies that block the interaction between Von Willebrand factor (VWF) and the GPIb-IX-V complex prevent platelet adhesion and aggregation. Agents that disrupt GPIb-IX-V complex formation or expression interfere with platelet plug formation and primary hemostasis.