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Altered expression of platelet surface glycoproteins during storage
Author(s) -
Dhar Animesh,
Ganguly Pankaj
Publication year - 1988
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1988.tb02436.x
Subject(s) - wheat germ agglutinin , platelet , glycoprotein , concanavalin a , lectin , thrombin , chemistry , glycoconjugate , biochemistry , agglutinin , peanut agglutinin , wheat germ , microbiology and biotechnology , biology , immunology , in vitro
Human blood platelets were stored in autologous plasma at 4°C or 22°C and their surface changes were probed with three lectins—wheat germ agglutinin, lentil lectin and concanavalin A. Platelets stored at either temperature for different times showed increased sensitivity to lectins. Lectins which were nonagglutinating to fresh platelets readily agglutinated stored platelets. The platelets stored for 24 h or longer lost their ability to respond to thrombin but demonstrated enhanced aggregation with wheat germ agglutinin. Surface labelling experiments revealed progressive loss of a glycoprotein of M r 150 000 (GPIb) together with the appearance of components with M r 69 000, 60 000 and 25 000 respectively. New high molecular weight glycoproteins were detected only in stored platelets. These findings illustrate the usefulness of lectins for the detection of altered expression of surface glycoconjugates which may be a factor in storage related dysfunction of platelets.