## Abstract Protein physical and chemical properties can be altered by polymer interaction. The presence of several high affinity binding sites on human serum albumin (HSA) makes it a possible target for many organic and polymer molecules. This study was designed to examine the interaction of HSA w
Effect of laser welding with human serum albumin on the expression of P-selectin on platelets
β Scribed by Kirman, Irena; Lauto, Antonio; Phillips, Alistar; Hamawy, Adam; Heldman, Eli; Cuomo, Bernardo; Shin, Sandra J.; Soslow, Robert; Felsen, Diane; Poppas, Dix P.
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 222 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0196-8092
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β¦ Synopsis
Background and
Objective: Artery repair by means of laser energy induces activation of platelets with a risk of thrombosis and local inflammatory reactions. The aim of this study was to investigate the effect of human serum albumin, the most common solder in laser surgery, on platelet activation. Study Design/Materials and Methods: Platelet activation was evaluated in canine blood by using two-color flow cytometry with a phycoerythrin-labeled antibody to a common platelet marker, glycoprotein IIb/ IIIa and fluorescein isothiocyanate-labeled antibody to a platelet activation molecule, P-selectin. Human serum albumin was applied in vitro and in vivo, as a solder during laser reconstruction of canine arteries. Results: In vitro, albumin significantly (P < 0.01) reduces the expression of P-selectin on platelets. This is most likely related to the blockage of P-selectin by albumin, which binds to the platelet surface, as confirmed by flow cytometry with fluorescein isothiocyanate-labeled albumin. In vivo, application of albumin solder tended to result in a lower percentage of P-selectin-expressing platelets in laser-repaired arteries compared to suture-repaired arteries. Conclusion: Albumin decreases the percentage of P-selectin-expressing platelets in vitro. Further research may allow the platelet activation inhibiting properties of albumin to be further optimized in vivo. Lasers Surg. Med. 25:438-444, 1999.
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