Bult H, Herman A G
Agents Actions Suppl. 1979(4):147-55.
Large concentrations of endotoxin lipopolysaccharides (LPS) E. coli O127:B8 and E. coli O26:B6 were needed for induction of platelet aggregation in citrated platelet rich plasma (PRP) from normal guinea-pigs. When guinea-pigs were actively immunized with LPS E. coli O127:B8 their PRP became more sensitive to the aggregatory effects of this type of LPS. The increase in sensitivity was rather selective since the responses to ADP and LPS E. coli O26:B6 remained unchanged. In endotoxin-stimulated PRP from normal guinea-pigs thromboxane A2 (TXA2) was not detectable by bioassay. Thus biosynthesis of TXA2 seemed to be of little importance in endotoxin-induced platelet responses in normal citrate PRP. LPS E. coli O127:B8, but not LPS E. coli O26:B6, was a potent inducer of the biosynthesis of TXA2 in sensitized PRP. Under those conditions endotoxin-induced aggregation seemed to be dependent on the endogenous biosynthesis of TXA2 by the platelets.
在来自正常豚鼠的枸橼酸化富血小板血浆（PRP）中，需要高浓度的大肠杆菌O127:B8和大肠杆菌O26:B6内毒素脂多糖（LPS）来诱导血小板聚集。当豚鼠用大肠杆菌O127:B8 LPS进行主动免疫时，它们的PRP对这种类型LPS的聚集作用变得更加敏感。敏感性的增加具有相当的选择性，因为对ADP和大肠杆菌O26:B6 LPS的反应保持不变。在来自正常豚鼠的内毒素刺激的PRP中，通过生物测定法无法检测到血栓素A2（TXA2）。因此，TXA2的生物合成在内毒素诱导的正常枸橼酸PRP血小板反应中似乎不太重要。大肠杆菌O127:B8 LPS，而不是大肠杆菌O26:B6 LPS，是致敏PRP中TXA2生物合成的有效诱导剂。在这些条件下，内毒素诱导的聚集似乎依赖于血小板内源性TXA2的生物合成。
