Purification and characterization of a 32‐kDa phospholipase A2 inhibitory protein (lipocortin) from human peripheral blood mononuclear cells

FEBS Letters

Russo-Marie, Françoise¹  Prieur, Benoît¹  Errasfa, Mourad¹  Minassian, Garo¹  Comera, Christine¹  Rothhut, Bernard¹ 

[1] Unité des Venins, Unité associée Institut Pasteur/INSERM U 285, 25 rue du Dr Roux, 75015 Paris, France

关键词: Lipocortin;    Phospholipase A2;    Monocyte;    Phospholipid;   

DOI  :  10.1016/0014-5793(87)81211-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A 32-kDa protein was isolated from human monocytes after calcium precipitation and chromatography. The protein activity was assessed by the inhibition of soluble phospholipase A₂, (PLA₂). This in vitro inhibitory effect on phospholipases A₂ was found only with negatively charged phospholipids. The protein was also able to inhibit cellular PLA₂, in mouse thymocytes. The biochemical properties and amino acid composition strongly suggest that the protein shares similarities with endonexin. Using a neutralizing monoclonal antibody against rat lipocortin, we found a cross-reactivity with the 32-kDa protein. According to the biochemical and immunological properties, we propose to relate this PLA₂, inhibitory protein from human monocytes to lipocortin.

【 授权许可】

Unknown