Platelet surface receptor glycoprotein VI-dimer is overexpressed in stroke: The Glycoprotein VI in Stroke (GYPSIE) study results. [PDF]
PLoS ONE, 2022 ObjectivesPlatelet activation underpins thrombus formation in ischemic stroke. The active, dimeric form of platelet receptor glycoprotein (GP) VI plays key roles by binding platelet ligands collagen and fibrin, leading to platelet activation.
Isuru Induruwa +17 more
doaj +7 more sources
Colchicine inhibits ROS generation in response to glycoprotein VI stimulation [PDF]
Scientific Reports, 2021 Colchicine inhibits coronary and cerebrovascular events in patients with coronary artery disease (CAD), and although known to have anti-inflammatory properties, its mechanisms of action are incompletely understood.
G. J. Pennings +5 more
doaj +6 more sources
Immobilized fibrinogen activates human platelets through glycoprotein VI [PDF]
Haematologica, 2018 Glycoprotein VI, a major platelet activation receptor for collagen and fibrin, is considered a particularly promising, safe antithrombotic target. In this study, we show that human glycoprotein VI signals upon platelet adhesion to fibrinogen.
Pierre H Mangin +18 more
doaj +7 more sources
Genetic variation of platelet glycoprotein VI and the risk of venous thromboembolism [PDF]
Haematologica, 2020 Family studies have indicated that heritability explains 50-60% of the venous thromboembolism (VTE) events, and in recent years, several single nucleotide polymorphisms (SNPs) have been found to influence the VTE risk. Glycoprotein 6 (GP6) rs1613662, also known as T13254C, is an A/G single nucleotide variation in amino acid 219, which results in a ...
Hanne Skille +9 more
doaj +8 more sources
Beyond antiplatelets: The role of glycoprotein VI in ischemic stroke. [PDF]
Int J Stroke, 2016 BACKGROUND: Platelets are essential to physiological hemostasis or pathological thrombus formation. Current antiplatelet agents inhibit platelet aggregation but leave patients at risk of systemic side-effects such as hemorrhage.
Induruwa I, Jung SM, Warburton EA.
europepmc +7 more sources
Efficient inhibition of collagen-induced platelet activation and adhesion by LAIR-2, a soluble Ig-like receptor family member. [PDF]
PLoS ONE, 2010 LAIR-1 (Leukocyte Associated Ig-like Receptor -1) is a collagen receptor that functions as an inhibitory receptor on immune cells. It has a soluble family member, LAIR-2, that also binds collagen and can interfere with LAIR-1/collagen interactions ...
Peter J Lenting +4 more
doaj +4 more sources
Differential effects of reduced glycoprotein VI levels on activation of murine platelets by glycoprotein VI ligands [PDF]
Biochemical Journal, 2002 We have investigated the effects of decreased levels of the complex between glycoprotein VI (GPVI) and the Fc receptor γ-chain (FcRγ) on responses to collagen and GPVI-specific ligands in murine platelets. We show that levels of GPVI—FcRγ of the order of 50% and 20% of wild-type levels caused 2- and 5-fold shifts to the right respectively in the dose ...
Daniel Snell +7 more
openalex +4 more sources
Minimal Collagen-Binding Epitope of Glycoprotein VI in Human and Mouse Platelets [PDF]
Biomedicines, 2023 Glycoprotein VI (GPVI) is a platelet-specific receptor for collagen and fibrin, regulating important platelet functions such as platelet adhesion and thrombus growth. Although the blockade of GPVI function is widely recognized as a potent anti-thrombotic
Chao Han +15 more
doaj +2 more sources
Sinomenium acutum Modulates Platelet Aggregation and Thrombus Formation by Regulating the Glycoprotein VI-Mediated Signalosome in Mice [PDF]
Pharmaceuticals, 2023 Sinomenium acutum (SA) has long been used as a traditional medicine in China, Japan, and Korea to treat a wide range of diseases. It has been traditionally used to ameliorate inflammation and improve blood circulation.
Yeon-Ji Kim +4 more
doaj +2 more sources
Platelet glycoprotein VI in the regulation of thrombus growth [PDF]
, 2022 Platelet glycoprotein VI (GPVI) is the principal signalling receptor for collagen, which is exposed upon damage to the extracellular matrix and at site of rupture of an atherosclerotic plaque.
Perrella, Gina
core +4 more sources