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Updated: Aug 8, 2026
10:55
Assays for Studying the Role of Vitronectin in Bacterial Adhesion and Serum Resistance
Published on: October 16, 2018
Homology with hemopexin suggests a possible scavenging function for S-protein/vitronectin
FEBS Letters
|April 21, 1986
Summary
S-protein, identical to vitronectin, binds to complement and coagulation complexes. Structural similarity to hemopexin suggests its role in clearing these complexes from circulation.
Area of Science:
- Biochemistry
- Immunology
- Cell Biology
Background:
- S-protein is an abundant plasma protein, now identified as vitronectin and serum spreading factor.
- It possesses multiple binding sites for key biological molecules including complement complexes, thrombin-antithrombin III, heparin, and cell receptors.
Purpose of the Study:
- To investigate the structural and sequence homology of S-protein with hemopexin.
- To elucidate the primary function of S-protein in the circulatory system.
Main Methods:
- Structural and sequence homology analysis between S-protein and hemopexin.
Main Results:
- A significant structural and sequence homology was identified between S-protein and hemopexin.
- This homology suggests a shared functional role between the two proteins.
Conclusions:
- The primary function of S-protein is likely that of a scavenging molecule.
- S-protein plays a crucial role in clearing spent complement and coagulation complexes from the circulation, maintaining homeostasis.
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