Title : Energy depletion of bovine mammary epithelial cells activates AMPK and suppresses protein synthesis through inhibition of mTORC1 signaling.

Pub. Date : 2013 Mar

PMID : 22972179






4 Functional Relationships(s)
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1 The objective of this study was to examine the effect of AMP-activated protein kinase (AMPK) activation by 2-deoxyglucose on protein synthesis and the mammalian target of rapamycin complex 1 (mTORC1) signaling pathway in bovine mammary epithelial cells. Deoxyglucose protein kinase AMP-activated catalytic subunit alpha 2 Homo sapiens
2 The objective of this study was to examine the effect of AMP-activated protein kinase (AMPK) activation by 2-deoxyglucose on protein synthesis and the mammalian target of rapamycin complex 1 (mTORC1) signaling pathway in bovine mammary epithelial cells. Deoxyglucose protein kinase AMP-activated catalytic subunit alpha 2 Homo sapiens
3 Phosphorylation of AMPK at Thr172 increased by 1.4-fold within 5 min, and remained elevated throughout a 30-min time course, in response to 2-deoxyglucose. Deoxyglucose protein kinase AMP-activated catalytic subunit alpha 2 Homo sapiens
4 2-Deoxyglucose increased phosphorylation of tuberous sclerosis complex 2 (TSC2) on AMPK consensus sites but did not change the amount of TSC1 bound to TSC2. Deoxyglucose protein kinase AMP-activated catalytic subunit alpha 2 Homo sapiens