Multiple domains of human PSG1 bind the platelet integrin αIIbβ3.
a, Integrin αIIbβ3 (2µg purified protein; lanes 1–3) pulls down PSG1 in an in vitro binding assay (lane 1). Negative controls are Protein G agarose beads with (lane 2) and without (lane 4) αIIbβ3, and with rabbit IgG instead of PSG1 (lane 3).
Melanie Ball (384026) +11 more
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Drug-induced activation of integrin alpha IIb beta 3 leads to minor localized structural changes.
Integrins are transmembrane proteins involved in hemostasis, wound healing, immunity and cancer. In response to intracellular signals and ligand binding, integrins adopt different conformations: the bent (resting) form; the intermediate extended form ...
Una Janke +5 more
doaj +1 more source
Structures of integrin αIIbβ3 in unliganded, closed and liganded, open conformations.
αIIb subunit is in blue color, β3 subunit is in pink color. A. Unliganded, closed structure of αIIbβ3 (PDB: 3FCS) [7] B. Liganded, open structure of αIIbβ3 (PDB: 3FCU)[7]. C. Structural details of unliganded, closed αIIbβ3.
Barry S. Coller (371201) +3 more
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Thiol isomerase ERp18 enhances platelet activation and arterial thrombosis
Background: Thiol isomerases regulate the thiol-disulfide exchange of functional proteins in cells. Using genetically modified mouse models and inhibitors, we and others demonstrated that 7 thiol isomerases (ERp57, protein diisulfide isomerase, ERp72 ...
Chao He +11 more
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The effect of anesthetics on αIIbβ3 cell surface expression.
Surface expression of αIIbβ3 WT (A) or β3-N305T (B) was probed by AP3 antibody and expressed using mean fluorescence intensity (MFI). Data was shown as [(MFI of αIIbβ3 exposed to anesthetic)/(MFI of αIIbβ3 of sample not exposed to anesthetic)]×100%, and ...
Koichi Yuki (398264) +3 more
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Expression of WT and Mutant αIIbβ3 Integrins.
Immunofluorescent flow cytometry. HEK293T transfectants were labeled with AP3 (anti-β3), 7E3 (anti-β3), 10E5 (anti-αIIb), and LM609 (anti-αV). Thick and thin lines show labeling of the αIIbβ3 transfectant and the mock transfectant, respectively.
Bing-Hao Luo (3810) +5 more
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Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3 [PDF]
Hemostasis and thrombosis (blood clotting) involve fibrinogen binding to integrin αIIbβ3 on platelets, resulting in platelet aggregation. αvβ3 binds fibrinogen via an Arg-Asp-Gly (RGD) motif in fibrinogen's α subunit.
Timothy A. Springer +5 more
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Normal Platelet Integrin Function in Mice Lacking Hydrogen Peroxide-Induced Clone-5 (Hic-5).
Integrin αIIbβ3 plays a central role in the adhesion and aggregation of platelets and thus is essential for hemostasis and thrombosis. Integrin activation requires the transmission of a signal from the small cytoplasmic tails of the α or β subunit to the
Michael Popp +3 more
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Strong Binding of Platelet Integrin αiIbβ3 to Fibrin Clots: Potential Target to Destabilize Thrombi
© 2017 The Author(s). The formation of platelet thrombi is determined by the integrin αIIbβ3-mediated interactions of platelets with fibrinogen and fibrin.
Weisel J. +7 more
core
All in the Family: Primary Megakaryocytes for Studies of Platelet αIIbβ3 Signaling
SummaryIntegrin αIIbβ3 mediates key platelet adhesive responses during hemostasis and thrombosis. Adhesive ligand binding to αIIbβ3 is regulated by “inside-out” signals, while adhesion-dependent cytoskeletal events are regulated by “outside-in” signals ...
Sanford Shattil, Andrew Leavitt
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