PHOSPHORYLATION OF THE LYMPHOID-CELL KINASE P56LCK IS STIMULATED BY MICROMOLAR CONCENTRATIONS OF ZN-2+
PHOSPHORYLATION OF THE LYMPHOID-CELL KINASE P56LCK IS STIMULATED BY MICROMOLAR CONCENTRATIONS OF ZN-2+
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DOI:
10.1016/0014-5793(91)80411-u
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发表时间:
1991-04-09
期刊:
影响因子:
3.5
通讯作者:
GACON, G
中科院分区:
文献类型:
--
作者:
PERNELLE, JJ;CREUZET, C;GACON, G
In particulate fractions 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-mu-M and reaches a maximum at 100-mu-M 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.