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Influence of flavonoids on Lck and Fyn tyrosine kinases using ELISA method with comparison of different substrates: Poly Glu:Tyr (4:1) and M3-01 decapeptide

Tyrosine phosphorylation represents unique signalling process in the cell as an answer to different extracellular signals. The enzymes that carry out this modification are protein tyrosine kinases (PTKs) which catalyse transfer of γ-phosphates of ATP on phenole -OH group of tyrosine of protein substrates. The largest subfamily of nonreceptor PTKs is the Src-family. Human Fyn and Lck tyrosine kinases are two of the nonreceptor Src-family tyrosine kinases involved in T-cell signalling transport. Flavonoids are biologically active polyphenole compounds naturally occuring in many plants. This group of compounds has been recognized as inhibitor of Fyn and Lck protein kinases. In conducted experiments, myricetin showed the highest inhibitory effect, with ATP non-competitive mechanism of inhibition. In contrast, competition with ATP has been proved in the example of staurosporine. Inhibitory activity of flavonoids on Fyn and Lck kinases was measured by ELISA (Enzyme-Linked Immunosorbent Assay) method. Affinity of these enzymes on two different substrates, polypeptide polymer PolyGlu:Tyr (4:1) and decapeptide M3-01 was tested. Development of efficient protein kinase inhibitors is important for the treatment of diseases, but also as a tool to investigate the physiological roles of protein kinases.

tyrosine kinases; Lck; Fyn; flavonoids; ELISA

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