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Related Concept Videos

Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Antiplatelet Drugs: Prostaglandin Synthesis, P2Y12 and Glycoprotein IIb/IIIa Inhibitors01:20

Antiplatelet Drugs: Prostaglandin Synthesis, P2Y12 and Glycoprotein IIb/IIIa Inhibitors

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Formation of the Platelet Plug01:22

Formation of the Platelet Plug

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Treatment for Pulmonary Arterial Hypertension: Prostacyclin Receptor Agonists01:23

Treatment for Pulmonary Arterial Hypertension: Prostacyclin Receptor Agonists

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Drug Binding to Blood Components

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Related Experiment Video

Updated: Jun 20, 2026

Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader
07:13

Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader

Published on: May 24, 2024

Selective binding site for [3H]prostacyclin on platelets.

A M Siegl, J B Smith, M J Silver

    The Journal of Clinical Investigation
    |February 1, 1979
    PubMed
    Summary
    This summary is machine-generated.

    Prostacyclin (PGI(2)) binds to platelets at two types of sites. The high-affinity site is likely the specific receptor mediating PGI(2)'s anti-platelet aggregation effects.

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    Last Updated: Jun 20, 2026

    Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader
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    An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers
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    Microfluidics in Assessing Platelet Function
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    Microfluidics in Assessing Platelet Function

    Published on: November 8, 2024

    Area of Science:

    • Biochemistry
    • Pharmacology
    • Hematology

    Background:

    • Prostacyclin (PGI(2)) is a potent natural inhibitor of platelet aggregation.
    • Understanding PGI(2) interaction with platelets is crucial for its therapeutic applications.

    Purpose of the Study:

    • To investigate the binding of prostacyclin (PGI(2)) to human platelets.
    • To characterize the binding sites and their affinity for PGI(2).

    Main Methods:

    • Synthesis of high specific activity [9-(3)H]PGI(2).
    • Platelet binding experiments using radiolabeled PGI(2) and platelet-rich plasma.
    • Scatchard analysis to determine binding site characteristics.

    Main Results:

    • Binding of [3H]PGI(2) to platelets reached equilibrium within 2 minutes and was reversible.
    • Scatchard analysis revealed two classes of binding sites: high-affinity (Kd=12.1 nM, 93 sites/platelet) and low-affinity (Kd=0.909 uM, 2700 sites/platelet).
    • The relative ability of various prostaglandins to displace [3H]PGI(2) correlated with their anti-aggregation potency, except for PGD(2).

    Conclusions:

    • Platelets possess specific binding sites for prostacyclin (PGI(2)).
    • The higher affinity binding site appears to be the functional receptor for PGI(2)"s anti-platelet activity.
    • This finding supports the role of specific PGI(2) receptors in mediating its physiological effects on platelet function.