Identification of glycoprotein Ib as a target for autoantibody in idiopathic (autoimmune) thrombocytopenic purpura. Blood 1986 Feb;67(2):310-5
Date
02/01/1986Pubmed ID
2935206Scopus ID
2-s2.0-0022650749 (requires institutional sign-in at Scopus site) 77 CitationsAbstract
An antibody (DIL) from a patient with idiopathic thrombocytopenic purpura (ITP) was shown to have autospecificity on the basis of reactions with autologous platelets that were identical to those obtained with platelets from normal subjects. DIL antibody also reacted strongly in an immunofluorescence test with platelets from a patient with Glanzmann's thrombasthenia, but failed to react with platelets from a patient with the Bernard-Soulier syndrome who was known to be deficient in glycoprotein Ib (GPIb). Purified GPIb and control platelets, but not Bernard-Soulier platelets, inhibited the lytic activity of DIL. Using the GPIb-specific monoclonal antibody AP1 and one-dimensional rocket electrophoresis into gels containing rabbit antihuman platelet membrane antibody, it was shown that staphylococcal protein A-Sepharose beads coated with DIL antibody selectively remove GPIb from solubilized platelet preparations. By crossed immunoelectrophoresis it was found that DIL recognizes a determinant on GPIb on the membrane side of the cleavage site of the platelet calcium-activated protease (calpain). These studies provide direct evidence for binding of a platelet autoantibody to a determinant on GPIb relatively close to the site of insertion of this protein into the platelet membrane.
Author List
Szatkowski NS, Kunicki TJ, Aster RHAuthor
Richard H. Aster MD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Antibody SpecificityAutoantibodies
Complement Fixation Tests
Fluorescent Antibody Technique
Glycoproteins
Humans
Immunoenzyme Techniques
Membrane Proteins
Platelet Aggregation
Platelet Membrane Glycoproteins
Purpura, Thrombocytopenic
