Morphology, ultrastructure and function of glycosylation-modified chilled blood platelets.
- Author:
Yong GUO
1
;
Ying HAN
;
Guo-Bo QUAN
;
Min-Xia LIU
;
An LIU
Author Information
1. Beijing Institute of Transfusion Medicine, Beijing 100850, China.
- Publication Type:Journal Article
- MeSH:
Blood Platelets;
drug effects;
physiology;
ultrastructure;
Blood Preservation;
methods;
Cryopreservation;
methods;
Galactose;
pharmacology;
Glycosylation;
Humans
- From:
Journal of Experimental Hematology
2008;16(2):411-415
- CountryChina
- Language:Chinese
-
Abstract:
The glycosylation of platelets may prolong their life-span when being transfused after preservation under 4 degrees C, therefore this study was aimed to investigate the effect of glycosylation on morphology, ultrastructure, function and membrane glycoprotein of platelets. The experiments were divided into 3 groups: group preserved in room temperature (RT group), group preserved in 4 degrees C (4T group) and group UDP-Gal glycosylated and preserved in 4 degrees C (U+4T group). The binding rate of RCA I lectin and expression of platelet surface markers CD62P, CD42b were determined by flow cytometry. Morphology and ultrastructure of platelets were observed by light microscopy, scanning electron microscopy (SEM) and transmission electron microscopy (TEM). Platelets aggregation was detected by aggregometer. The results showed that the binding rate of RCAI in U+4T group significantly higher than that in RT group (p<0.01), no obvious changes was found in ultrastructure of glycosylated platelets, as compared with fresh platelets. Some morphologic changes, such as pseudopodium could be observed in 4T group. The aggregation rate of platelets in U+4T group reached to 50% of RT group. The expression levels of CD42b and CD62P, and the binding rate of annexin V in U+4T group were not significantly different from that in RT group. It is concluded that UDP-Gal can effectively cause galactosylation of platelets, and the platelets modified with UDP-Gal remain normal morphology, ultrastructure and function.
