Abstract
The interaction between ceruloplasmin (CP), the multicopper oxidase of human plasma, and 5-lipoxygenase (5-LO), the key enzyme of leukotriene synthesis, is shown for the first time. By Western-blotting and mass spectrometry of tryptic fragments, it is shown that 5-LO from protein extract of human leukocytes binds with immobilized CP. Dose-dependent influence of intact CP on leukotrienes synthesis is found: CP reduced leukotrienes synthesis in leukocytes in a dose above 50 μg/ml (normal CP concentration in plasma is about 300–400 μg/ml). Proteolyzed CP and apo-form of CP is unable to inhibit activity of 5-LO. CP increased activity of 5-LO at low doses (5–10 μg/ml). On the whole, the influence of CP on phagocytosis index of leukocytes coordinates with influence on activity of 5-LO: the index increased in the range of 2–10 μg/ml CP and decreased at doses of CP above 40 μg/ml. The dual role of CP in regulation of cellular response of leukocytes is discussed.
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Abbreviations
- CP:
-
ceruloplasmin
- LF:
-
lactoferrin
- 5-LO:
-
5-lipoxygenase
- MPO:
-
myeloperoxidase
- OZ:
-
opsonized zymosan
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Published in Russian in Biokhimiya, 2010, Vol. 75, No. 12, pp. 1687–1694.
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Sokolov, A.V., Golenkina, E.A., Kostevich, V.A. et al. Interaction of ceruloplasmin and 5-lipoxygenase. Biochemistry Moscow 75, 1464–1469 (2010). https://doi.org/10.1134/S0006297910120072
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DOI: https://doi.org/10.1134/S0006297910120072