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Characterization of GMP-140 (P-selectin) as a circulating plasma protein
L C Dunlop1, M P Skinner, L J Bendall
1Baker Medical Research Institute, Prahran, Victoria, Australia.
The Journal of Experimental Medicine
|April 1, 1992
Summary
Soluble granule membrane protein (GMP-140) detected in plasma, functioning anti-inflammatorily by downregulating neutrophil adhesion and activation, potentially preventing circulation issues.
Area of Science:
- Biochemistry
- Cell Biology
- Immunology
Background:
- GMP-140 (CD62P) is a granule membrane protein on activated platelets and endothelial cells, mediating neutrophil attachment.
- Cloning data suggested a soluble form of GMP-140 exists, with its transcript found in platelets.
Purpose of the Study:
- To detect and characterize soluble GMP-140 in human plasma.
- To investigate the functional properties of plasma-derived GMP-140.
Main Methods:
- Enzyme-linked immunosorbent assay (ELISA) for soluble GMP-140 detection in plasma.
- Protein purification from plasma and characterization using molecular mass, immunoblotting, and gel filtration.
- Functional assays assessing neutrophil binding to purified plasma GMP-140.
Main Results:
- Soluble GMP-140 was detected in plasma and purified.
- Plasma GMP-140 eluted as a monomer, lacking a transmembrane domain, unlike the tetrameric membrane form.
- Purified plasma GMP-140 bound neutrophils similarly to membrane GMP-140 and retained anti-inflammatory properties.
Conclusions:
- Soluble GMP-140 is present in plasma and functionally active.
- Plasma GMP-140 may play a crucial role in preventing neutrophil activation in circulation.
- This soluble form represents a potential therapeutic target for inflammatory conditions.