Related Experiment Video
Updated: Aug 6, 2026

10:10
Platelet Adhesion and Aggregation Under Flow using Microfluidic Flow Cells
Published on: October 27, 2009
Antibody-detectable changes in fibrinogen adsorption affecting platelet activation on polymer surfaces
E Shiba1, J N Lindon, L Kushner
1Beth Israel Hospital, Boston 02215.
The American Journal of Physiology
|May 1, 1991
Summary
Platelet interaction with artificial surfaces depends on fibrinogen organization. Specific fibrinogen regions and platelet receptors (GpIIb/IIIa) are crucial for this interaction, influencing platelet retention on methacrylate polymers.
Area of Science:
- Biomaterials Science
- Hematology
- Surface Chemistry
Background:
- Platelet reactivity with artificial surfaces correlates with adsorbed fibrinogen concentration.
- The organization of adsorbed fibrinogen influences platelet interactions.
Purpose of the Study:
- To investigate how fibrinogen organization on hydrophobic surfaces affects platelet binding.
- To determine the role of specific fibrinogen epitopes and platelet receptors in this process.
Main Methods:
- Studied antibody binding to adsorbed fibrinogen on polyalkyl methacrylate polymers.
- Compared antibody binding with platelet retention in methacrylate bead columns.
- Utilized polyclonal and monoclonal antibodies against fibrinogen and its epitopes, and against the platelet receptor GpIIb/IIIa.
Main Results:
- Diluted plasma pretreatment increased platelet retention.
- Polyclonal anti-fibrinogen antibodies and antibodies against a specific gamma-peptide eliminated retention.
- Monoclonal antibodies against other COOH-terminal epitopes reduced retention.
- An antibody against the GpIIb/IIIa receptor completely inhibited platelet retention.
Conclusions:
- Methacrylate polymers alter adsorbed fibrinogen, impacting platelet interaction.
- Platelet retention involves the COOH-terminal end of fibrinogen's gamma-chain interacting with platelet GpIIb/IIIa receptors.
More Related Videos
Related Concept Videos
Intracellular Signaling Affects Focal Adhesions
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
Clot Retraction and Fibrinolysis
After a fibrin clot is formed, the next step is clot retraction, a vital process facilitated by platelet contractile proteins, such as actin and myosin. These proteins pull the fibrin strands closer together and condense the clot. This action reduces the size of the clot, creating a smaller, denser structure that effectively seals off the damaged vessel. Clot retraction consolidates the clot and helps with wound healing by bringing the edges of the damaged blood vessel closer together.

