Related Experiment Video
Updated: Sep 12, 2026

A Uniform Shear Assay for Human Platelet and Cell Surface Receptors via Cone-plate Viscometry
Published on: June 5, 2019
Platelet-activating factor-binding protein in human serum
Abstract:
The occurrence of a kind of protein (PBP) with stronger PAF-binding ability than albumin was shown in human serum. The molecular weight of PBP was approximately 160K to 180K. PBP seemed to be a pentamer composed of five 32K subunits. PAF bound to PBP revealed platelet aggregation and was resistant to acetyl-hydrolase. PAF synthesized in neutrophils stimulated with the ionophore A23187 was released by PBP from cells.
Insights
Researchers discovered a novel protein in human serum, Platelet-Binding Protein (PBP), which binds strongly to Platelet-Activating Factor (PAF). This PBP facilitates PAF-induced platelet aggregation and release from neutrophils.
Area of Science:
- Biochemistry
- Immunology
- Hematology
Background:
- Platelet-Activating Factor (PAF) is a potent lipid mediator involved in inflammation and allergic reactions.
- The binding and transport mechanisms of PAF in human serum are not fully understood.
- Albumin is a major serum protein, but its role in PAF binding is less characterized compared to specific binding proteins.
Purpose of the Study:
- To identify and characterize proteins in human serum with high Platelet-Activating Factor (PAF)-binding capabilities.
- To investigate the functional consequences of PAF binding to identified serum proteins.
- To explore the role of these proteins in PAF release from stimulated immune cells.
Main Methods:
- Serum protein isolation and purification.
- Platelet aggregation assays.
- Biochemical characterization of protein-ligand interactions (molecular weight, subunit composition).
- Analysis of PAF release from ionophore-stimulated neutrophils.
Main Results:
- A novel protein, Platelet-Binding Protein (PBP), was identified in human serum with significantly higher PAF-binding affinity than albumin.
- PBP has an estimated molecular weight of 160-180 kDa and appears to be a pentamer of 32 kDa subunits.
- PAF bound to PBP induced platelet aggregation and was resistant to acetylhydrolase degradation.
- PBP mediated the release of newly synthesized PAF from neutrophils stimulated with A23187.
Conclusions:
- Human serum contains a specific protein (PBP) that avidly binds PAF.
- PBP plays a role in PAF-mediated platelet activation and modulates PAF release from neutrophils.
- These findings suggest PBP is a key component in regulating PAF's biological activities.

