Lanthanum induces extracellular signal-regulated kinase phosphorylation through different mechanisms in HeLa cells and NIH 3T3 cells.
Lanthanum ion (La3+) was generally regarded as calcium antagonist and was used as calcium channel blocker. However, its potential biological effects on cells were poorly understood. In the present work, it was found that La3+ could induce rapid extracellular signal-regulated kinase (ERK) phosphorylation in both HeLa cells and NIH 3T3 cells, but different mechanisms were involved. At a concentration of 30 microM or higher, La3+ enters the cells and activates ERK through a mechanism involving calmodulin activation inside the cells, which is similar to the action of intracellular Ca2+. However, at lower concentration, free La3+ promoted ERK phosphorylation in NIH 3T3 cells outside the cells through an unknown La3+ sensing mechanism, while Ca2+ exerted much weaker effect. The present results suggested that the biological effects of La3+ on cells maybe involve mechanisms beyond calcium antagonist.
Hu
Jian
J
Department of Chemical Biology, School of Pharmaceutical Sciences, Peking University Health Science Center, Beijing, 100083, P.R.China.
Yu
Siwang
S
Yang
Xiaoda
X
Wang
Kui
K
Qian
Zhongming
Z
D000818:Animals; D002147:Calmodulin / Q000187:drug effects / Q000378:metabolism; D002462:Cell Membrane / Q000187:drug effects; D002478:Cells, Cultured; D048049:Extracellular Signal-Regulated MAP Kinases / Q000187:drug effects* / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D007811:Lanthanum / Q000494:pharmacology*; D051379:Mice; D041681:NIH 3T3 Cells; D010766:Phosphorylation / Q000187:drug effects
D002147:Calmodulin; D007811:Lanthanum; D048049:Extracellular Signal-Regulated MAP Kinases