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Expression of 5'-AMP-activated protein kinase with starvation in murine thymocytes
Rintarou Okoshi1, Kazumasa Ohta, Ayako Ishikawa
1Department of Biochemistry, Tokyo Dental College, Mihama-ku, Chiba, Japan. rkrr_o2002@yahoo.co.jp
Abstract:
The 5'-AMP-activated protein kinase (AMPK) is a key enzyme in the protection of cells during energy crisis. AMPK is a heterotrimer consisting of a catalytic α (α1, 2) subunit and two regulatory subunits, β (β1, 2) and γ (γ1-3). To elucidate the role of AMPK in thymocytes with starvation, we investigated the expression of AMPK in murine thymocytes. The main isoforms expressed were α2, β1, and γ1, of which expression increased time-dependently with starvation, together with an increase in the amount of the active form of AMPK, phospho-AMPKα. In cultured thymocytes, expression of AMPK was induced by dexamethasone, but not by a low glucose concentration in medium. Increased expression was inhibited by glucocorticoid receptor antagonist RU486. Phosphorylation of AMPKα showed an increase with low glucose concentration, but not with dexamethasone. These results suggest that increased expression of AMPK in starved mouse thymocytes is induced by an increase in glucocorticoids and that activation is induced by hypoglycemia.
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