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• W1966703403 endingPage "1151" @default.
• W1966703403 startingPage "1143" @default.
• W1966703403 abstract "Summary. A Glanzmann thrombasthenia variant with a β3 Ser 752 →Pro cytoplasmic domain substitution has platelets that fail to aggregate or bind soluble fibrinogen (Fg) after activation. Despite this, Fg is normally present in the α‐granules. We have used immunoelectron microscopy to examine the reactivity of Fg with the different pools of αIIbβ3 in the patient's platelets. Immunogold labelling was performed on cryosections using an anti‐ligand‐induced binding site (LIBS) monoclonal antibody (mAb), which binds to αIIbβ3 only when Fg is bound, or a mixture of two anti‐receptor‐induced binding site (RIBS) mAbs that specifically recognize receptor‐bound Fg. Labelling of the α‐granule membrane and channels of the surface‐connected canalicular system in unstimulated platelets confirmed that the mutated αIIbβ3 retains the capacity to transport Fg. When the patient's platelets were stimulated with ADP in the presence of Fg, as expected there was a much‐decreased activation of surface‐exposed αIIbβ3. However, thrombin‐induced activation was associated with both secretion and a rapid increase in the labelling of internal membrane systems by anti‐RIBS and anti‐LIBS mAbs, with mobilization of theinternal Fg pool. Yet labelling on the surface of the patient's platelets was transient. Our studies implied that αIIbβ3 in platelets may bind fibrinogen in different activation states and that this patient specifically lacked high‐affinity binding." @default.
• W1966703403 created "2016-06-24" @default.
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• W1966703403 date "2002-08-29" @default.
• W1966703403 modified "2023-10-16" @default.
• W1966703403 title "A Ser⁷⁵²→Pro substitution in the cytoplasmic domain of β3 in a Glanzmann thrombasthenia variant fails to prevent interactions between the αIIbβ3 integrin and the platelet granule pool of fibrinogen" @default.
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• W1966703403 doi "https://doi.org/10.1046/j.1365-2141.2002.03758.x" @default.
• W1966703403 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12199799" @default.
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