Abstract
Blood platelets have a receptor for macromolecular adhesive glycoproteins, located on a heteroduplex membrane glycoprotein complex (GPIIb/IIIa) that only becomes "exposed" when platelets are activated. Binding of the adhesive glycoproteins, in particular fibrinogen, to the receptor is required for platelet aggregation, which in turn is required to arrest bleeding. A murine monoclonal antibody whose rate of binding to the receptor is affected by platelet activation was both cross-linked and fragmented to assess the effects of changes in molecular size on its rate of binding to unactivated and activated platelets. The results indicate that small molecules can bind more rapidly to the receptors on unactivated platelets than can large molecules and that activation involves a conformational and/or microenvironmental change that permits the large molecules to bind more rapidly.
Keywords
GlycoproteinPlatelet membrane glycoproteinPlateletReceptorPlatelet activationBiologyCell biologyFibrinogenMonoclonal antibodyMembrane glycoproteinsPlatelet adhesivenessCell surface receptorBiochemistryBiophysicsAntibodyImmunologyPlatelet aggregation
Related Publications
A new murine monoclonal antibody reports an activation-dependent change in the conformation and/or microenvironment of the platelet glycoprotein IIb/IIIa complex.
Considerable evidence indicates that the glycoprotein (GP) IIb/IIIa complex on human platelets functions as a receptor for fibrinogen, but little is known about the mechanism of...
Reconstruction of platelet proteins into phospholipid vesicles. Functional proteoliposomes.
Platelet membrane glycoproteins IIb and IIIa were reconstituted into liposomes containing phosphatidylcholine. The reconstituted vesicles bound antiplatelet antibodies and showe...
A highly conserved sequence of the Arg-Gly-Asp-binding domain of the integrin beta 3 subunit is sensitive to stimulation
The Arg-Gly-Asp (RGD)-binding domain of GPIIb-IIIa has been localized in a fragment of the GPIIIa subunit that includes the sequence between amino acids 109 and 171. To examine,...
Immobilized Arg-Gly-Asp (RGD) peptides of varying lengths as structural probes of the platelet glycoprotein IIb/IIIa receptor
Abstract The interactions between ligands containing the recognition sequence arginine-glycine-aspartic acid (RGD) and integrin receptors are important in many cell-cell and cel...
Human platelets and megakaryocytes contain alternately spliced glycoprotein IIb mRNAs.
The earliest marker of the megakaryocyte lineage in human bone marrow is a heterodimeric complex of glycoproteins IIb (GPIIb) and IIIa (GPIIIa). GPIIb-IIIa is a member of the in...
Publication Info
- Year
- 1986
- Type
- article
- Volume
- 103
- Issue
- 2
- Pages
- 451-456
- Citations
- 93
- Access
- Closed
External Links
Social Impact
Altmetric
PlumX Metrics
Social media, news, blog, policy document mentions
Citation Metrics
93
OpenAlex
Cite This
BS Coller
(1986).
Activation affects access to the platelet receptor for adhesive glycoproteins..
The Journal of Cell Biology
, 103
(2)
, 451-456.
https://doi.org/10.1083/jcb.103.2.451
Identifiers
- DOI
- 10.1083/jcb.103.2.451