Fab-mediated binding of drug-dependent antibodies to platelets in quinidine- and quinine-induced thrombocytopenia.
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Findings suggest that binding of drug-induced antibodies to platelets occurs at the Fab domains of the IgG molecule.Abstract:
Platelets coated with quinine- or quinidine-induced antibodies form rosettes around protein A-Sepharose beads and normal platelets form rosettes about protein A-Sepharose beads coated with these antibodies. These reactions occurred only in the presence of sensitizing drug. Platelets also formed rosettes about protein A-Sepharose beads coated with an anti-PIA1 antibody, but drug was not required. Formation of rosettes between antibody-coated platelets and protein A-Sepharose was inhibited by F(ab')2 fragments of goat antibody specific for the Fc portion of human IgG, while rosette formation between antibody-coated protein A-Sepharose and platelets was inhibited by F(ab')2 fragments directed against the F(ab')2 portion of the IgG molecule. Since binding of IgG to protein A is known to occur via the Fc region, these findings suggest that binding of drug-induced antibodies to platelets occurs at the Fab domains of the IgG molecule.read more
Citations
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Cefotetan-induced immunologic thrombocytopenia.
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Adverse drug reactions affecting blood cells.
TL;DR: This chapter discusses idiosyncratic drug reactions affecting blood and blood forming tissues with an emphasis on those thought to be immune-mediated, as would be expected since cellular immune effector cells have little direct access to circulating blood cells.
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Quinine-mediated disseminated intravascular coagulation
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CHAPTER 49 – Drug-Induced Thrombocytopenia
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Drug-mediated thrombocytopenia.
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TL;DR: Thrombocytopenia due to drug-dependent antibodies most frequently occurs with quinine/quinidine and with heparin and the mode of action of these antibodies and the nature of their antigenic determinants remain unclear.
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TL;DR: Results of this study were consistent with the possibilities that the protein moiety of a haptenic antigen involved in development of an antibody which attaches to a cell is not necessarily a component of the cell, and that the cell reacts with the antibody by virtue of having a surface favorable for non-specific adsorption of certain haptene-antibody complexes.
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Journal ArticleDOI
Drug-Antibody-Platelet Interaction in Quinine- and Quinidine-induced Thrombocytopenia
TL;DR: It is demonstrated that in quinine- and quinidine-induced thrombocytopenia, drug and antibody combine first in the soluble phase to form a complex, which then binds with high affinity to a receptor on the platelet surface (innocent bystander reaction), and that these antibodies are heterogeneous in respect to the amount of drug required to promote their binding to platelets, the number of platelet receptors they recognize, and their binding affinities.