PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1540140-0	1992	Sphingosine enhances platelet aggregation through an increase in phospholipase C activity by a protein kinase C-independent mechanism.	Sphingosine	0-11	LOC100009319	Oryctolagus cuniculus	65-80	
1540140-1	1992	Sphingosine (a potent inhibitor of protein kinase C) at 5-10 microM, which are concentrations lower than those that inhibit this enzyme activity, enhanced the aggregation of rabbit platelets induced by low concentrations of U46619, platelet-activating factor, thrombin and arachidonic acid, whereas H-7 and staurosporine, other protein kinase C inhibitors, failed to do so.	Sphingosine	0-11	prothrombin	Oryctolagus cuniculus	260-268	
1540140-4	1992	Furthermore, the hydrolytic action of exogenously added phospholipase C (from Clostridium perfringens) on platelet membrane phospholipids was dose-dependently enhanced by pretreatment of the platelets with sphingosine.	Phospholipids	124-137	LOC100009319	Oryctolagus cuniculus	56-71	
1540140-4	1992	Furthermore, the hydrolytic action of exogenously added phospholipase C (from Clostridium perfringens) on platelet membrane phospholipids was dose-dependently enhanced by pretreatment of the platelets with sphingosine.	Sphingosine	206-217	LOC100009319	Oryctolagus cuniculus	56-71	
1540140-5	1992	These results imply that sphingosine, at relatively low concentrations, brings about hyperaggregability of the platelets by the agonists employed, probably owing to enhancement of the phospholipase C activity.	Sphingosine	25-36	LOC100009319	Oryctolagus cuniculus	184-199