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Purification and characterization of a 32‐kDa phospholipase A 2 inhibitory protein (lipocortin) from human peripheral blood mononuclear cells
Author(s) -
Rothhut Bernard,
Comera Christine,
Prieur Benoît,
Errasfa Mourad,
Minassian Garo,
Russo-Marie Françoise
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81211-5
Subject(s) - phospholipase a2 , peripheral blood mononuclear cell , monoclonal antibody , annexin , biochemistry , in vitro , annexin a1 , microbiology and biotechnology , phospholipase , chemistry , antibody , immunoprecipitation , inhibitory postsynaptic potential , protein a/g , biology , enzyme , recombinant dna , immunology , endocrinology , fusion protein , gene
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 A 2 , (PLA 2 ). This in vitro inhibitory effect on phospholipases A 2 was found only with negatively charged phospholipids. The protein was also able to inhibit cellular PLA 2 , 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 PLA 2 , inhibitory protein from human monocytes to lipocortin.