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GP6 encodes a platelet membrane glycoprotein of the immunoglobulin superfamily. Zusätzlich bieten wir Ihnen GP6 Antikörper (83) und GP6 Kits (39) und viele weitere Produktgruppen zu diesem Protein an.
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This suggests whereas platelet receptor shedding is mainly modulated by calcium-dependent signals, either platelet-surface interactions with the container walls during storage or induced shear stress under long-term agitation, might be also involved in the excessive shedding of GPVI during the storage of PRP (zeige C4BPA Proteine)-platelet concentrates.
There was no evidence to suggest that polymorphisms of GP VI T13254C and GP Ibalpha VNTR were associated with CAD.
Platelet adhesion to collagen induces GPVI dimer clustering. GPVI clustering increases both avidity for collagen and the proximity of GPVI-associated signaling molecules, which may be crucial for the initiation and persistence of signaling
Loss of the platelet surface receptors GPIbalpha (zeige GP1BA Proteine) and GPVI in heart failure, CF-VAD (zeige KCTD1 Proteine) and ECMO patients may contribute to ablated platelet adhesion/activation, and limit thrombus formation under high/pathologic shear conditions
Novel antithrombotic peptides derived from trowaglerix that acts through GPVI antagonism with greater safety-no severe bleeding.
results support the idea that genetic variability of GP6 regulatory regions can be associated with platelet hyperaggregability - a possible cause of miscarriage
These results demonstrate that GP6 is a receptor for fibrin and provide evidence that this interaction contributes to thrombus growth and stability.
data suggest a novel role for FAK (zeige PTK2 Proteine) in GPVI-dependent ROS (zeige ROS1 Proteine) formation and platelet activation and elucidate a proximal signaling role for FAK (zeige PTK2 Proteine) within the GPVI pathway.
This study identifies GPVI as a platelet receptor for polymerized fibrin with 2 major functions: (1) amplification of thrombin (zeige F2 Proteine) generation and (2) recruitment of circulating platelets to clots.
Glaucocalyxin A inhibits platelet activation and thrombus formation preferentially via GPVI signaling pathway.
In conclusion, the present study unraveled ceramidase as a crucial player in sphingosine-induced platelet activation following GPVI-dependent signaling.
These results reveal a novel and unexpected function of hepatic Fc-gamma-RIIB in the targeted downregulation of GPVI in vivo.
collagen-I-mediated inhibition of proplatelet formation is specifically controlled by GPVI.
platelet GP6 and thromboxane A2 receptor (zeige TBXA2R Proteine) have a role in promoting inflammatory macrophage phenotype in skin inflammation
TULA-2 (zeige STS1 Proteine) Protein Phosphatase Suppresses Activation of Syk (zeige SYK Proteine) through the GPVI Platelet Receptor for Collagen by Dephosphorylating Tyr (zeige TYR Proteine)(P)346, a Regulatory Site of Syk (zeige SYK Proteine).
Inhibition of platelet activation by an anti-GPVI antibody significantly reduces infarct size.
These results demonstrate that GPVI is a receptor for fibrin and provide evidence that this interaction contributes to thrombus growth and stability.
data demonstrate that genetic deletion of GPVI receptor, FcRgamma (zeige FCER1G Proteine) chain, or the alpha2beta1 integrin changes the thrombotic potentials of these platelets to collagen dependent on the stimulus mechanism.
This gene encodes a platelet membrane glycoprotein of the immunoglobulin superfamily. The encoded protein is a receptor for collagen and plays a critical role in collagen-induced platelet aggregation and thrombus formation. The encoded protein forms a complex with the Fc receptor gamma-chain that initiates the platelet activation signaling cascade upon collagen binding. Mutations in this gene are a cause of platelet-type bleeding disorder-11 (BDPLT11). Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
, platelet collagen receptor
, platelet glycoprotein VI
, glycoprotein VI (platelet)
, glycoprotein 5
, glycoprotein 6 (platelet)
, glycoprotein VI