| pubmed-article:6412754 | pubmed:abstractText | Four amines, galactosamine, mannosamine, histamine and arginine were studied for their effects on platelet aggregation, platelet morphological changes, platelet protein phosphorylation and platelet secretion. Galactosamine inhibited platelet aggregation in response to arachidonic acid and ionophore A23187 but did not inhibit changes in platelet morphology, or in platelet protein phosphorylation in response to these agents and only partially inhibited platelet secretion. The results suggest that galactosamine can be used as a selective inhibitor of platelet-platelet attachment without having a significant effect on intracellular processes. Mannosamine was similar to galactosamine except that it partially suppressed phosphorylation of myosin light chain. Histamine was similar to mannosamine except that some platelet damage was seen in platelets exposed to histamine and arachidonic acid or ionophore A23187. Arginine was non-selective: it suppressed platelet aggregation, secretion and phosphorylation of myosin light chain and a 40 kDa protein (40P) in response to arachidonic acid and ionophore A23187. Arginine was also potent in suppressing platelet morphological changes. When the same four amines were evaluated for their effects on thrombin-induced aggregation; secretion was inhibited concomitantly with inhibition of aggregation. Inhibition of myosin light chain and 40P phosphorylation was evident with galactosamine, suggesting that when thrombin is used as the agonist, galactosamine is not a specific inhibitor of platelet-platelet attachment. These amines therefore have various effects on platelet responses. Under some conditions and with arachidonic acid or ionophore A23187 as agonist, one of them, galactosamine, can be used as a selective inhibitor of platelet-platelet attachment. | lld:pubmed |
