Cardiology Medical News about zinc-induced cardioprotection;molecular mechanism underlying Akt activation

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The molecular mechanism underlying Akt activation in zinc-induced cardioprotection
Heart And Circulatory Physiology, 06/16/09

Lee SR et al. – Exogenous zinc activates Akt via the selective insulin-like growth factor-1 RTK (IGF-1RTK) and prevents themitochondrial permeability transition pore (mPTP) opening in cardiac cells. Inactivation of serine/threonine (Ser/Thr) protein phosphatases may also contribute to zinc-induced Akt activation.

Methods

Study of the mechanism by which zinc activates Akt

Results

Treatment of H9c2 cells with ZnCl2 (10 microM) for 20 min enhanced Akt phosphorylation (Ser473), indicating that zinc can rapidly activate Akt
Zinc did not alter either PTEN (phosphatase and tensin homolog on chromosome ten) phosphorylation and total PTEN protein levels or PTEN oxidation, implying that PTEN may not play a role in zinc action
Zinc-induced Akt phosphorylation was blocked by both the non-selective receptor tyrosine kinase (RTK) inhibitor genistein and IGF-1RTK inhibitor AG1024, indicating that zinc activates Akt via IGF-1RTK
AG1024 also abolished zinc-induced phosphorylation of protein tyrosine and serine/threonine
Zinc markedly enhanced phosphorylation of IGF-1R, reversed by genistein and AG1024
On confocal imaging study, AG1024 abolished preventive effect of zinc on oxidant-induced mPTP opening, confirming that IGF-1RTK plays a role in zinc-induced cardioprotection
Zinc decreased activity of protein phosphatase 2A (PP2A), a major protein Ser/Thr phosphatase, implying that protein Ser/Thr phosphatases may also play a role in the action of zinc on Akt activity

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