Phosphorylation of the lymphoid cell kinase p56lck is stimulated by micromolar concentrations of Zn2+
- 9 April 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 281 (1-2) , 278-282
- https://doi.org/10.1016/0014-5793(91)80411-u
Abstract
In particulate fraction from LSTRA lymphoma cells, tyrosine phosphorylation of the lymphoid specific tyrosine kinase p56lck is elicited by Zn2+ in the absence of other divalent cations. Zn2+ alone also induces autophosphorylation of immunoprecipitated p56lck. The effect of Zn2+ is dose dependent; it is detected at concentrations of Zn2+ as low as 5 μM and reaches a maximum at 100 μM Zn2+. Among other divalent cations tested. Mn2+, and Co2+ to a lesser extent, were also effective. Zn2+ also stimulated p56lck phosphorylation in the presence of Mg2+ ions at physiological concentration, whereas orthovanadate had no effect. These results suggest that Zn2+ activates the autophosphorylation of p56lck; this fact could be related with the stimulating effect of Zn2+ in the activation of T lymphocytes.Keywords
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