Activities of enzymes that metabolize platelet-activating factor (1-Alkyl-2-acetyl-sn-glycero-3-phosphocholine) in neutrophils and eosinophils from humans and the effect of a calcium ionophore.
Activities of enzymes that metabolize platelet-activating factor (1-Alkyl-2-acetyl-sn-glycero-3-phosphocholine) in neutrophils and eosinophils from humans and the effect of a calcium ionophore.
复制标题
人类中性粒细胞和嗜酸性粒细胞中血小板激活因子(1-烷基-2-乙酰基-sn-甘油-3-磷酸胆碱)代谢酶的活性以及钙离子载体的作用。
DOI:
10.1016/0006-291x(82)90928-7
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发表时间:
1982
影响因子:
3.1
通讯作者:
Snyder,F
中科院分区:
文献类型:
--
作者:
Lee,TC;Malone,B;Wasserman,SI;Fitzgerald,V;Snyder,F
Enzymatic systems in human blood cells are described for the activation and inactivation of a biologically active phospholipid (1-alkyl-2-acetyl-sn-glycero-3-phosphocholine) with hypotensive, platelet-aggregating, and inflammatory properties. The results document the presence of alkyldihydroxyacetone-phosphate synthase (forms the O-alkyl linkage in lipids), 1-alkyl-2-lyso-sn-glycero-3-phosphocholine: acetyl-CoA acetyltransferase (produces the biologically active molecule), and 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine: acetylhydrolase (destroys the biological activity) in human neutrophils and eosinophils. Both the acetyltransferase and acetylhydrolase activities are increased severalfold after treatment of normal neutrophils with ionophore A23187; however, alkyldihydroxyacetone-phosphate synthase activity is not influenced by the ionophore. Eosinophils isolated from patients with eosinophilia have significantly greater activities of all the enzymes studied than the eosinophils isolated from normal individuals. Our results indicate the acetyltransferase responsible for 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine synthesis may serve an important role in human blood cells that release this biologically active phospholipid. Moreover, the acetyltransferase activity was found to be dramatically influenced by calcium flux.