Abstract：
:Activation of AMP-activated protein kinase (AMPK) upon energy depletion stimulates energy production and limits energy utilization. Erythrocytes lacking AMPK are susceptible to suicidal cell death (eryptosis). A hallmark of eryptosis is cell membrane scrambling with phosphatidylserine exposure at the erythrocyte surface, which can be identified from annexin V-binding. AMPKα1-deficient mice (ampk(-/-)) suffer from anemia due to accelerated clearance of erythrocytes from circulating blood. To determine the link between AMPK and the eryptotic phenotype, we performed a global proteome analysis of erythrocytes from ampk(-/-) mice and wild-type mice using high-accuracy mass spectrometry and label-free quantitation and measured changes of expression levels of 812 proteins. Notably, the p21-activated kinase 2 (PAK2), previously implicated in apoptosis, was detected as downregulated in erythrocytes of ampk(-/-) mice, pointing to its potential role in eryptosis. To validate this, we showed that specific inactivation of PAK2 with the inhibitor IPA3 in human and murine ampk(+/+) erythrocytes increases the binding of annexin V and augments the stimulating effect of glucose deprivation on annexin V-binding. Inhibition of PAK2 failed to significantly modify annexin V-binding in ampk(-/-) erythrocytes, showing that AMPK and PAK2 exert similar phenotypes upon inactivation in erythrocytes. This study presents the first large-scale analysis of protein expression in erythrocytes from AMPKα1-deficient mice and reveals a role of PAK2 kinase in eryptosis.
journal_name
J Proteome Resjournal_title
Journal of proteome researchauthors
Zelenak C,Föller M,Velic A,Krug K,Qadri SM,Viollet B,Lang F,Macek Bdoi
10.1021/pr101004jsubject
Has Abstractpub_date
2011-04-01 00:00:00pages
1690-7issue
4eissn
1535-3893issn
1535-3907journal_volume
10pub_type
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