在受刺激的单核细胞培养物中形成的一种新型β-血小板球蛋白裂解产物可激活人类中性粒细胞。
A novel cleavage product of beta-thromboglobulin formed in cultures of stimulated mononuclear cells activates human neutrophils.
作者信息
Walz A, Baggiolini M
机构信息
Theodor-Kocher-Institut, University of Bern, Switzerland.
出版信息
Biochem Biophys Res Commun. 1989 Mar 31;159(3):969-75. doi: 10.1016/0006-291x(89)92203-1.
A neutrophil-activating peptide, NAP-2, was found to be produced in cultures of human mononuclear cells in the presence of E. coli lipopolysaccharide or phytohaemagglutinin. NAP-2 induced the release of elastase from cytochalasin B-treated human neutrophils. Amino- and carboxy-terminal sequencing and electrophoretic analysis showed that NAP-2 is a single peptide of 70 amino acids (Mr 7,628, IEP 8.7) corresponding to a carboxyterminal fragment of beta-thromboglobulin. NAP-2 is homologous to NAF/NAP-1. When aligned on the basis of their two first cysteines, 13 out of 20 amino-terminal residues are identical. The overall homology between the two peptides is 46%.
一种嗜中性粒细胞激活肽，即NAP-2，被发现是在人单核细胞培养物中，于大肠杆菌脂多糖或植物血凝素存在的情况下产生的。NAP-2诱导了用细胞松弛素B处理过的人嗜中性粒细胞释放弹性蛋白酶。氨基末端和羧基末端测序以及电泳分析表明，NAP-2是一种由70个氨基酸组成的单一肽段（分子量7628，等电点8.7），对应于β-血小板球蛋白的羧基末端片段。NAP-2与NAF/NAP-1同源。当基于它们的前两个半胱氨酸进行比对时，20个氨基末端残基中有13个是相同的。这两种肽之间的总体同源性为46%。
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