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DOI: 10.1055/s-2007-1000388
ADP-Induced Platelet Aggregation and Actin Polymerization
Involvement of GpIIb/IIIa and the Effect of Mg2+Publication History
Publication Date:
06 February 2008 (online)
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Abstract
We have investigated the effects of Mg2+ (added to platelet rich plasma [PRP] as 10mM MgCl2 or MgSO4) on the platelet aggregation and actin polymerization that occurs in response to adenosine diphosphate (ADP). The PRP was prepared from blood containing hirudin as anticoagulant.
Mg2+ added before 1μM ADP completely inhibited aggregation and markedly inhibited actin polymerization. Mg2+ (10mM) added before 10μM ADP converted irreversible aggregation into a reversible response; similarly, apparently irreversible actin polymerization was converted to a reversible response in which polymerization was followed by some actin depolymerization. Mg2+ added after inducing platelet aggregation with 10μM ADP produced parallel disaggregation of platelets and actin depolymerization.
Actin polymerization occurs immediately on adding ADP to PRP (in association with shape change) and further polymerization occurs in association with platelet aggregation. When aggregation (and the actin polymerization associated with this) was prevented by adding M148, a monoclonal antibody directed at the GpIIb/IIIa complex, or simply by avoiding stirring the sample, Mg2+ had no effect on actin polymerization/depolymerization. Thus Mg2+ only affected the changes in actin that were associated with the aggregation response. This was in contrast to iloprost (which acts at the PGI2 receptor to stimulate adenylate cyclase) which induced rapid actin depolymerization when added after ADP stimulation of platelets under circumstances where platelet aggregation was avoided.
These results show that Mg2+ affects actin polymerization as well as platelet aggregation, and that it affects the actin polymerization associated with aggregation but not that associated with shape change (in contrast to iloprost which inhibits both). The results also emphasize the close relationships that exist between aggregation and actin polymerization and between disaggregation and actin depolymerization. It is suggested that Mg2+ may exert its effects by altering the conformation of the GpIIb/IIIa complex such that it is no longer able to fully participate in aggregation and actin polymerization.
Key words:
Platelet aggregation - ADP - actin - magnesium - GPIIb/IIIa