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• W2210816877 abstract "Insulin-like growth factor binding protein-1 (IGFBP-1), secreted by fetal liver, is a key regulator of IGF-I bioavailability and fetal growth. IGFBP-1 phosphorylation decreases IGF-I bioavailability and diminishes its growth-promoting effects. Growth-restricted fetuses have decreased levels of circulating essential amino acids. We recently showed that IGFBP-1 hyperphosphorylation (pSer101/119/169) in response to leucine deprivation is regulated via activation of the amino acid response (AAR) in HepG2 cells. Here we investigated nutrient-sensitive protein kinases CK2/PKC/PKA in mediating IGFBP-1 phosphorylation in leucine deprivation. We demonstrated that leucine deprivation stimulated CK2 activity (enzymatic assay) and induced IGFBP-1 phosphorylation (immunoblotting/MRM-MS). Inhibition (pharmacological/siRNA) of CK2/PKC, but not PKA, prevented IGFBP-1 hyperphosphorylation in leucine deprivation. PKC inhibition also prevented leucine deprivation-stimulated CK2 activity. Functionally, leucine deprivation decreased IGF-I-induced-IGF-1R autophosphorylation when CK2/PKC were not inhibited. Our data strongly support that PKC promotes leucine deprivation-induced IGFBP-1 hyperphosphorylation via CK2 activation, mechanistically linking decreased amino acid availability and reduced fetal growth." @default.
• W2210816877 created "2016-06-24" @default.
• W2210816877 creator A5026773122 @default.
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• W2210816877 date "2016-04-01" @default.
• W2210816877 modified "2023-10-13" @default.
• W2210816877 title "Increased IGFBP-1 phosphorylation in response to leucine deprivation is mediated by CK2 and PKC" @default.
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• W2210816877 doi "https://doi.org/10.1016/j.mce.2015.12.006" @default.
• W2210816877 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4811673" @default.
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• W2210816877 hasPublicationYear "2016" @default.
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