The snake venom toxin alboaggregin-A activates glycoprotein VI [PDF]
The glycoprotein (GP)–Ib-IX-V receptor complex has recently been reported to signal through a pathway similar to that used by the collagen receptor GPVI, with a critical role described for the Fc receptor γ-chain. The evidence for this was based in part on studies with the GPIbα-selective snake venom toxin, alboaggregin-A.
Naoki Asazuma+7 more
openalex +4 more sources
Platelet glycoprotein VI genetic quantitative and qualitative defects
Platelet membrane glycoprotein VI (GPVI) is increasingly recognized as an important receptor for thrombus formation and growth. Numerous arguments have been published indicating that GPVI plays a major role in thrombosis without being essential for ...
Martine Jandrot-Perrus+2 more
doaj +5 more sources
Platelet GPVI (Glycoprotein VI) and Thrombotic Complications in the Venous System. [PDF]
The immunoglobulin receptor GPVI (glycoprotein VI) is selectively expressed on megakaryocytes and platelets and is currently recognized as a receptor for not only collagen but also a variety of plasma and vascular proteins, including fibrin, fibrinogen, laminin, fibronectin, and galectin-3.
Perrella G+3 more
europepmc +4 more sources
Platelet glycoprotein VI promotes folic acid-induced acute kidney injury through interaction with tubular epithelial cell-derived galectin-3 [PDF]
Background Acute kidney injury (AKI) is defined by a significant reduction in renal function, which subsequently impairs coagulation and activates the inflammatory immune response, ultimately resulting in damage to renal tubular epithelial cells (TECs ...
Ya-Wei Guo+8 more
doaj +2 more sources
Janus kinase inhibitors ruxolitinib and baricitinib impair glycoprotein-VI mediated platelet function [PDF]
Several Janus kinase (JAK) inhibitors (jakinibs) have recently been approved to treat inflammatory, autoimmune and hematological conditions. Despite emerging roles for JAKs and downstream signal transducer and activator of transcription (STAT) proteins ...
Iván Parra-Izquierdo+9 more
doaj +2 more sources
Interaction of calmodulin with the cytoplasmic domain of platelet glycoprotein VI [PDF]
The platelet collagen receptor, glycoprotein VI (GPVI), and GPIb-IX-V, which binds von Willebrand factor, initiate platelet aggregation at low or high shear stress, respectively. We recently reported that positively charged, membrane-proximal sequences within cytoplasmic domains of GPIbβ and GPV of GPIb-IX-V bind calmodulin.
Robert K. Andrews+5 more
openalex +4 more sources
Atroxlysin-III, A Metalloproteinase from the Venom of the Peruvian Pit Viper Snake Bothrops atrox (Jergón) Induces Glycoprotein VI Shedding and Impairs Platelet Function [PDF]
Atroxlysin-III (Atr-III) was purified from the venom of Bothrops atrox. This 56-kDa protein bears N-linked glycoconjugates and is a P-III hemorrhagic metalloproteinase.
Luciana S. Oliveira+8 more
doaj +2 more sources
Functional characterization of a nanobody-based glycoprotein VI-specific platelet agonist [PDF]
Background: Glycoprotein (GP)VI is a platelet-specific collagen receptor required for platelet activation during hemostasis. Platelet reactivity toward collagen is routinely assessed during diagnostic workup of platelet disorders.
Minka Zivkovic+74 more
doaj +2 more sources
Glycoprotein VI in securing vascular integrity in inflamed vessels. [PDF]
Glycoprotein VI (GPVI), the main platelet receptor for collagen, has been shown to play a central role in various models of thrombosis, and to be a minor actor of hemostasis at sites of trauma. These observations have made of GPVI a novel target for antithrombotic therapy, as its inhibition would ideally combine efficacy with safety.
Boulaftali Y+3 more
europepmc +4 more sources
Selective Blockade of Glycoprotein VI Clustering on Collagen Helices [PDF]
Platelet activation by collagen relies on the interaction of the receptor glycoprotein VI (GPVI) with collagen helices. We have previously generated two recombinant single chain human antibodies (scFvs) to human GPVI. The first, 10B12, binds to the collagen-binding site on the apical surface between the two immunoglobulin-like domains (D1D2) of the ...
Marie O’Connor+7 more
openalex +5 more sources