Summary
This reviews summarizes our evidence suggesting that the plasma protein environment influences platelet aggregation potential and metabolic activity.
Cationic proteins are capable of restoring the aggregation potential of washed human platelets. The aggregation restoring effect of gamma globulin is inhibited by more anionic proteins in subfractions of Cohn fraction IV and fractions V and VI. Artificial enhancement of the net negative charge of plasma proteins through acylation produces derivatives capable of inhibiting platelet aggregation in platelet rich plasma.
The oxygen consumption of washed human platelets is lower than in platelet rich plasma while the lactate production is identical. Autologous plasma, albumin or IgG immunoglobulin restores the oxygen consumption of washed platelets to values comparable to those obtained for platelet rich plasma, while the lactate production is unaffected. Fibrinogen or IgA myeloma protein increases the lactate production, but not the oxygen consumption. Cyclic AMP levels are considerably lower in washed platelets than in platelet rich plasma. Gamma globulin and albumin causes a further decrease, which is progressive with time. Fibrinogen causes no change in platelet cyclic AMP content.
It is suggested that these observations may in part be explained by the equilibrium between anionic and cationic proteins in the platelet microenvironment.
This hypothesis appears applicable in certain clinical situations.
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Hansen, M.S., Bang, N.U. Plasma protein regulation of platelet function and metabolism. Mol Cell Biochem 24, 143–158 (1979). https://doi.org/10.1007/BF00220733
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DOI: https://doi.org/10.1007/BF00220733