We are analyzing https://link.springer.com/article/10.1007/s10522-008-9187-x.

Title:
Age-associated impairment of Akt phosphorylation in primary rat hepatocytes is remediated by alpha-lipoic acid through PI3 kinase, PTEN, and PP2A | Biogerontology
Description:
Akt is a highly regulated serine/threonine kinase involved in stress response and cell survival. Stress response pathways must cope with increasing chronic stress susceptibility with age. We found an age-related lesion in Akt activity via loss of phosphorylation on Ser473. In hepatocytes from old rats, basal phospho-Ser473 Akt is 30% lower when compared to young, but basal phospho-Thr308 Akt is unchanged. (R)-α-lipoic acid (LA), a dithiol compound with antioxidant properties, is effective against age-related increases in oxidative stress and has been used to improve glucose utilization through insulin receptor (IR) pathway-mediated Akt phosphorylation. Treatment with physiologically relevant doses of LA (50 μM) provided a 30% increase in phospho-Ser473. Furthermore, two phosphatases that antagonize Akt, PTEN and PP2A, were both partially inhibited by LA. Thus, LA may be a nutritive agent that can remediate loss of function in the Akt pathway and aid in the survival of liver cells.
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28 years and 1 months (reg. 1997-05-29).

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Keywords {🔍}

article, pubmed, cas, google, scholar, akt, acid, kinase, alphalipoic, hagen, insulin, protein, phosphorylation, stress, receptor, aging, usa, cell, biol, dois, phosphatase, chem, privacy, cookies, content, pten, shay, loss, oxidative, pathway, access, ageing, sci, signaling, publish, research, search, petersen, tory, agerelated, antioxidant, proc, natl, acad, doipnas, biochem, lifespan, nature, smith, function,

Topics {✒️}

igf-ii-overexpressing rhabdomyosarcoma cells des igf-i-mediated activation month download article/chapter ceramide-activated phosphatase 2a 3-phosphoinositide-dependent protein kinase dna-dependent protein kinase alpha-lipoic acid-reduction pathway-mediated akt phosphorylation phosphoinositide 3-kinase/akt pathway carboxyl-terminal autoinhibitory domain basal phospho-thr308 akt pi3k/akt signaling pathway protein phosphatase 2a basal phospho-ser473 akt alpha-lipoic acid alpha-lipoic acid article biogerontology aims full article pdf akt/pkb signaling regulates akt phosphorylation oxidative stress tolerance ames dwarf mice α-lipoic acid privacy choices/manage cookies stress signaling pathways akt kinase activities vascular endothelial dysfunction activates protein kinase protein kinase cascades insulin-sensitive pathway insulin-signaling network insulin receptor substrate stress response pathways oregon state university pi3 kinase increased insulin sensitivity improves insulin sensitivity primary rat hepatocytes growth hormone production p38 mapk signaling european economic area oxidative stress physiologically relevant doses 3t3-l1 adipocytes directly binding activator stimulus-specific fashion reactive oxygen species shenvi sv health r01 2ag17141 akt/pkb

Questions {❓}

Konrad D (2005) Utilization of the insulin-signaling network in the metabolic actions of alpha-lipoic acid-reduction or oxidation?
Petersen Shay K, Moreau RF, Smith EJ, Hagen TM (2008) Is alpha-lipoic acid a scavenger of reactive oxygen species in vivo?

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      description:Akt is a highly regulated serine/threonine kinase involved in stress response and cell survival. Stress response pathways must cope with increasing chronic stress susceptibility with age. We found an age-related lesion in Akt activity via loss of phosphorylation on Ser473. In hepatocytes from old rats, basal phospho-Ser473 Akt is 30% lower when compared to young, but basal phospho-Thr308 Akt is unchanged. (R)-α-lipoic acid (LA), a dithiol compound with antioxidant properties, is effective against age-related increases in oxidative stress and has been used to improve glucose utilization through insulin receptor (IR) pathway-mediated Akt phosphorylation. Treatment with physiologically relevant doses of LA (50 μM) provided a 30% increase in phospho-Ser473. Furthermore, two phosphatases that antagonize Akt, PTEN and PP2A, were both partially inhibited by LA. Thus, LA may be a nutritive agent that can remediate loss of function in the Akt pathway and aid in the survival of liver cells.
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         Developmental Biology
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