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

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 p...

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Bibliographic Details
Published in:FEBS letters 1987-07, Vol.219 (1), p.169-175
Main Authors: Rothhut, Bernard, Comera, Christine, Prieur, Benoît, Errasfa, Mourad, Minassian, Garo, Russo-Marie, Françoise
Format: Article
Language:English
Subjects:
Amino Acids - blood
Analytical, structural and metabolic biochemistry
Animals
Annexins
Antibodies, Monoclonal
Arachidonic Acid
Arachidonic Acids - blood
Biological and medical sciences
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Glycoproteins - blood
Glycoproteins - isolation & purification
Glycoproteins - pharmacology
Humans
Hydrolases
Immunochemistry
In Vitro Techniques
Lipocortin
Mice
Monocyte
Monocytes - enzymology
Phospholipase A2
Phospholipases - antagonists & inhibitors
Phospholipases A - antagonists & inhibitors
Phospholipases A2
Phospholipid
T-Lymphocytes - enzymology
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(87)81211-5