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

FEBS Letters

Bjørn, Søren¹  Thim, Lars¹  Norris, Kjeld¹  Flodgaard, Hans¹  Hastrup, Sven¹  Nielsen, Per F.¹  Rasmussen, Poul B.¹  Wiberg, Finn C.¹ 

[1] Health Care Discovery, Novo Nordisk, Novo Allé, DK-2880 Bagsvaerd, Denmark

关键词: HBP/CAP37/azurocidin;    Baculovirus;    N-terminal processing;    Mass spectrometry;    Lipopolysaccharide;    Cytokine;   

DOI  :  10.1016/0014-5793(96)00639-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown