We are analyzing https://link.springer.com/article/10.1007/s00125-011-2311-5.

Title:
Metformin activates AMP-activated protein kinase in primary human hepatocytes by decreasing cellular energy status | Diabetologia
Description:
Aim/hypothesis The glucose-lowering drug metformin has been shown to activate hepatic AMP-activated protein kinase (AMPK), a master kinase regulating cellular energy homeostasis. However, the underlying mechanisms remain controversial and have never been investigated in primary human hepatocytes. Methods Hepatocytes isolated from rat, mouse and human livers were treated with various concentrations of metformin. Isoform-specific AMPKα abundance and activity, as well as intracellular adenine nucleotide levels and mitochondrial oxygen consumption rates were determined at different time points. Results Metformin dose- and time-dependently increased AMPK activity in rat and human hepatocytes, an effect associated with a significant rise in cellular AMP:ATP ratio. Surprisingly, we found that AMPKα2 activity was undetectable in human compared with rat hepatocytes, while AMPKα1 activities were comparable. Accordingly, metformin only increased AMPKα1 activity in human hepatocytes, although both AMPKα isoforms were activated in rat hepatocytes. Analysis of mRNA expression and protein levels confirmed that only AMPKα1 is present in human hepatocytes; it also showed that the distribution of β and γ regulatory subunits differed between species. Finally, we demonstrated that the increase in AMP:ATP ratio in hepatocytes from liver-specific Ampkα1/2 (also known as Prkaa1/2) knockout mice and humans is due to a similar and specific inhibition of the mitochondrial respiratory-chain complex 1 by metformin. Conclusions/interpretation Activation of hepatic AMPK by metformin results from a decrease in cellular energy status owing to metformin’s AMPK-independent inhibition of the mitochondrial respiratory-chain complex 1. The unique profile of AMPK subunits found in human hepatocytes should be considered when developing new pharmacological agents to target the kinase.
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Keywords {🔍}

metformin, ampk, hepatocytes, article, google, scholar, pubmed, mmoll, cas, human, mitochondrial, complex, kinase, ampkα, protein, activity, activation, fig, hepatic, rat, ratio, ampatp, drug, mice, subunits, primary, effect, inhibition, respiratorychain, ampactivated, cellular, energy, results, cell, liver, diabetes, amp, phosphorylation, concentrations, expression, liverspecific, cells, effects, levels, subunit, μmoll, wildtype, guigas, shown, isolated,

Topics {✒️}

5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside conserved serine/threonine-protein kinase serine/threonine-protein kinase lkb1 amp-activated/snf1 protein kinases 5′-monophosphate-activated protein kinase quantitative real-time pcr amp-activated protein kinase intensive blood-glucose control high-performance liquid chromatography article download pdf exhibits cardio-protective features ampk-independent mechanism involving ser79-acetyl-coa carboxylase anti-diabetic drugs rosiglitazone ser/thr protein kinases adenine nucleotide-independent mechanism apparent species-specific difference amp-insensitive γ2 mutant effective anti-hyperglycaemic action ice-cold hclo4-edta hepatic lkb1/ampk axis putative amp-independent mechanism improve insulin action high-fat diet [49] pancreatic beta-cells ampk-null hepatocytes isolated primary antibodies cross-reacting isoform-specific ampkα activities tissue-specific localisation pattern rt quantitative pcr isoform-specific ampkα abundance ice-cold buffer glucose-lowering drug metformin metabolic research unit cellular energy status subtle species-specific differences privacy choices/manage cookies ampk-mediated as160 phosphorylation specific protein phosphatases inhibit respiratory complex electronic supplementary material hepatic glucose production dose-dependent effect persisted gamma-subunit isoforms krebs/bicarbonate medium α2-ampk catalytic subunits mitochondrial respiratory chain respiratory-chain complex 1 respiratory-chain complex 2 respiratory chain complex

Questions {❓}

Ben Sahra I, Le Marchand-Brustel Y, Tanti JF, Bost F (2010) Metformin in cancer therapy: a new perspective for an old antidiabetic drug?
Brunmair B, Staniek K, Gras F et al (2004) Thiazolidinediones, like metformin, inhibit respiratory complex I: a common mechanism contributing to their antidiabetic actions?

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         description:The glucose-lowering drug metformin has been shown to activate hepatic AMP-activated protein kinase (AMPK), a master kinase regulating cellular energy homeostasis. However, the underlying mechanisms remain controversial and have never been investigated in primary human hepatocytes. Hepatocytes isolated from rat, mouse and human livers were treated with various concentrations of metformin. Isoform-specific AMPKα abundance and activity, as well as intracellular adenine nucleotide levels and mitochondrial oxygen consumption rates were determined at different time points. Metformin dose- and time-dependently increased AMPK activity in rat and human hepatocytes, an effect associated with a significant rise in cellular AMP:ATP ratio. Surprisingly, we found that AMPKα2 activity was undetectable in human compared with rat hepatocytes, while AMPKα1 activities were comparable. Accordingly, metformin only increased AMPKα1 activity in human hepatocytes, although both AMPKα isoforms were activated in rat hepatocytes. Analysis of mRNA expression and protein levels confirmed that only AMPKα1 is present in human hepatocytes; it also showed that the distribution of β and γ regulatory subunits differed between species. Finally, we demonstrated that the increase in AMP:ATP ratio in hepatocytes from liver-specific Ampkα1/2 (also known as Prkaa1/2) knockout mice and humans is due to a similar and specific inhibition of the mitochondrial respiratory-chain complex 1 by metformin. Activation of hepatic AMPK by metformin results from a decrease in cellular energy status owing to metformin’s AMPK-independent inhibition of the mitochondrial respiratory-chain complex 1. The unique profile of AMPK subunits found in human hepatocytes should be considered when developing new pharmacological agents to target the kinase.
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