Modulation of platelet-activating factor (PAF) synthesis and release from human polymorphonuclear leukocytes (PMN): role of extracellular albumin.
Modulation of platelet-activating factor (PAF) synthesis and release from human polymorphonuclear leukocytes (PMN): role of extracellular albumin.
复制标题
调节人多形核白细胞(PMN)的血小板激活因子(PAF)合成和释放:细胞外白蛋白的作用。
DOI:
10.1016/0003-9861(85)90555-7
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发表时间:
1985
影响因子:
3.9
通讯作者:
Pinckard,RN
中科院分区:
文献类型:
--
作者:
Ludwig,JC;Hoppens,CL;McManus,LM;Mott,GE;Pinckard,RN
Human neutrophilic polymorphonuclear leukocytes (PMN) stimulated withN′-formyl-methionyl-leucyl-phenylalanine (FMLP) in the presence of cytochalasin B but in the absence of human serum albumin (HSA) synthesized only small amounts of platelet-activating factor (PAF) that attained maximum levels within 60–120 s after stimulation; in addition, no release of PAF occurred. However, in the presence of 2.5 mg HSA/ml, there was a threefold increase in PAF synthesis, 30–40% of which was released within 5 min after FMLP stimulation. In the presence of 50 mg HSA/ml there was at least a fourfold increase in PAF synthesis and release, with maximal synthesis occurring 10–20 min after stimulation. Thus, the presence of HSA during PMN stimulation not only induced an albumin dose-dependent increase in PAF release but significantly augmented the synthesis of PAF. In contrast to PAF synthesis and release, the presence or absence of HSA had no effect upon lysosomal enzyme secretion from FMLP-stimulated PMN, which was maximal within 30–60 s after stimulation. These results demonstrate that HSA plays an essential rolein vitroin the synthesis and release of PAF from human PMN, and support the hypothesis that there is a cyclic PAF synthesis-release coupling mechanism in the stimulated human PMN.