A method for purifying the platelet membrane glycoprotein IIb-IIIa complex
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Cited by (122)
Antibodies causing thrombocytopenia in patients treated with RGD-mimetic platelet inhibitors recognize ligand-specific conformers of α <inf>IIb</inf>/β<inf>3</inf> integrin
2012, BloodCitation Excerpt :RGDW peptide was synthesized and purified by the Peptide Core Laboratory (BloodCenter of Wisconsin). Murine mAbs specific for αIIb/β3 were produced in BALB/c mice immunized with αIIb/β3 purified from human platelets.27 Details of the immunization protocol and selection for hybridomas secreting αIIb/β3-specific mAbs have been described previously.28
Heparin promotes platelet responsiveness by potentiating αIIbβ3-mediated outside-in signaling
2011, BloodCitation Excerpt :Interestingly, and relevant to this discussion, heparin has been shown to bind a number of transmembrane glycoproteins, including the Ig-superfamily member G6b,42 as well as the cell-surface integrins αvβ343,44 and α5β1.44 Whether heparin similarly binds αIIbβ3 has been controversial, as Fitzgerald et al purified αIIbβ3 from heparin-binding contaminants by allowing it to flow unbound through heparin-Sepharose beads as part of an early chromatographic purification protocol for this integrin,45 whereas Sobel et al reported that not only could detergent solubilized αIIbβ3 specifically bind to and become eluted from this affinity matrix, tritiated heparin became photoaffinity cross-linked to cell surface αIIbβ3 in intact platelets.12 Our observation that either of 2 different anti-glycoprotein IIb-IIIa receptor antagonists, abciximab and eptifibatide, are able to prevent platelet spreading on immobilized heparin (Figure 4A) and downstream heparin-initiated signal transduction (Figure 4B; supplemental Figure 4), taken together with the observation that both murine (Figure 3) and human (Figure 4C) platelets lacking functional αIIbβ3 receptors fail to react with or become activated by immobilized UFH, LMWH (supplemental Figure 1), or fondaparinux (supplemental Figure 2), all under conditions in which the major αIIβ3 ligand, fibrinogen, is absent, provide compelling evidence that these clinically used compounds interact directly with αIIbβ3, and not another platelet receptor, to initiate outside-in signaling.
Integrin reconstituted in GUVs: A biomimetic system to study initial steps of cell spreading
2009, Biochimica et Biophysica Acta - Biomembranes