| Autor: |
Foretz, Marc, Hébrard, Sophie, Guihard, Soizic, Leclerc, Jocelyne, Cruzeiro, Marcio Do, Hamard, Ghislaine, Niedergang, Florence, Gaudry, Muriel, Viollet, Benoit |
| Předmět: |
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| Zdroj: |
FASEB Journal; Jan2011, Vol. 25 Issue 1, p337-347, 11p |
| Abstrakt: |
AMP-activated protein kinase (AMPK) is an αβY heterotrimer conserved throughout evolution and important for energy sensing in all eukaryote cells. AMPK controls metabolism and various cellular events in response to both hormones and changes in cellular energy status. The γ subunit senses intracellular energy status through the competitive binding of AMP and ATP. We show here that targeted disruption of the mouse AMPK7I gene (Prkagl) causes regenerative hemolytic anemia by increasing the sequestration of abnormal erythrocytes. Prkagl-/- mice displayed splenomegaly and iron accumulation due to compensatory splenic erythropoiesis and erythrophagocytosis. Moreover, AMPKγl- deficient erythrocytes were highly resistant to osmotic hemolysis and poorly deformable in response to increasing shear stress, consistent with greater membrane rigidity. No change in cytoskeletal protein composition was observed; however, the phosphorylation level of addudn, a protein promoting the binding of spectrin to actin, was higher in AMPKγl-deficient erythrocytes. Together, these results demonstrate that AMPRγl subunit is required for the maintenance of erythrocyte membrane elasticity. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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