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Interaction of ceruloplasmin and 5-lipoxygenase

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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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Correspondence to A. V. Sokolov.

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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

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