Abstract

Platelet membrane glycoproteins IIb and IIIa were reconstituted into liposomes containing phosphatidylcholine. The reconstituted vesicles bound antiplatelet antibodies and showed specific binding to thrombin-activated platelets. Prostacyclin, a known inhibitor of thrombin-activated platelet aggregation, inhibited the binding of the proteoliposomes to thrombin-activated platelets. The reconstituted vesicles also specifically bound 125I-labeled fibrinogen. This binding was insensitive to ADP but dependent on calcium ions. These data indicate that platelet glycoproteins IIb and IIIa have been successfully reconstituted into phospholipid vesicles such that their behavior is similar to that in intact platelets.

Keywords

PlateletVesicleThrombinLiposomeChemistryPhospholipidPhosphatidylcholineBiochemistryPhosphatidylserinePlatelet membrane glycoproteinFibrinogenGlycoproteinPlatelet activationBiophysicsMembraneBiologyImmunology

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Publication Info

Year
1985
Type
article
Volume
75
Issue
1
Pages
35-39
Citations
36
Access
Closed

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Joseph J. Baldassare, Richard Kahn, Michael A. Knipp et al. (1985). Reconstruction of platelet proteins into phospholipid vesicles. Functional proteoliposomes.. Journal of Clinical Investigation , 75 (1) , 35-39. https://doi.org/10.1172/jci111693

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DOI
10.1172/jci111693