重组人HBP/CAP37/天青杀素的特性，一种增强脂多糖诱导单核细胞释放细胞因子的多效性炎症介质。

Characterization of recombinant human HBP/CAP37/azurocidin, a pleiotropic mediator of inflammation-enhancing LPS-induced cytokine release from monocytes.

作者信息

Rasmussen P B, Bjørn S, Hastrup S, Nielsen P F, Norris K, Thim L, Wiberg F C, Flodgaard H

机构信息

Health Care Discovery, Novo Nordisk, Bagsvaerd, Denmark.

出版信息

FEBS Lett. 1996 Jul 15;390(1):109-12. doi: 10.1016/0014-5793(96)00639-4.

DOI:10.1016/0014-5793(96)00639-4

PMID:8706818

Abstract

Neutrophil-derived heparin-binding protein (HBP) is a strong chemoattractant for monocytes. We report here for the first time the expression of recombinant HBP. A baculovirus containing the human HBP cDNA mediated in insect cells the secretion of a 7-residue N-terminally extended HBP form (pro-HBP). Deletion of the pro-peptide-encoding cDNA sequence resulted in correctly processed HBP at the N-terminus. Electrospray mass spectrum analysis of recombinant HBP yielded a molecular weight of 27.237 +/- 3 amu. Consistent with this mass is a HBP form of 225 amino acids (mature part +3 amino acid C-terminal extension). The biological activity of recombinant HBP was confirmed by its chemotactic action towards monocytes. Furthermore, we have shown that recombinant HBP stimulates in a dose-dependent manner the lipopolysaccharide (LPS)-induced cytokine release from human monocytes.

摘要

中性粒细胞衍生的肝素结合蛋白（HBP）是一种对单核细胞具有强大趋化作用的物质。我们在此首次报告重组HBP的表达情况。一种含有人类HBP cDNA的杆状病毒在昆虫细胞中介导分泌出一种N端延伸了7个残基的HBP形式（前体HBP）。缺失编码前肽的cDNA序列导致在N端正确加工出HBP。重组HBP的电喷雾质谱分析得出分子量为27.237±3原子质量单位。与该质量相符的是一种由225个氨基酸组成的HBP形式（成熟部分+3个氨基酸的C端延伸）。重组HBP的生物活性通过其对单核细胞的趋化作用得到证实。此外，我们还表明重组HBP以剂量依赖的方式刺激人单核细胞释放脂多糖（LPS）诱导的细胞因子。