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A Rapid and Specific Microplate Assay for the Determination of Intra- and Extracellular Ascorbate in Cultured Cells
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L-ascorbic acid: A true substrate for HIF prolyl hydroxylase?

Andrey I Osipyants1, Andrey A Poloznikov1, Natalya A Smirnova1

  • 1Dmitry Rogachev National Medical Research Center of Pediatric Hematology, Oncology and Immunology, 117997, Moscow, Russian Federation.

Biochimie
|January 1, 2018
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Summary
This summary is machine-generated.

L-Ascorbate (L-Asc) acts as a co-substrate for HIF prolyl hydroxylase (PHD) enzymes, not just a reducing agent. This finding impacts understanding of hypoxia-inducible factor (HIF) regulation.

Keywords:
AdaptaquinCatalytic cycleHIF PHD inhibitorHIF1 ODD-Luciferase reporter assayJumonji demethylaseTET enzyme

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Signaling

Background:

  • Hypoxia-inducible factors (HIFs) are crucial regulators of cellular response to low oxygen.
  • HIF prolyl hydroxylase (PHD) enzymes regulate HIF stability by hydroxylation.
  • Ascorbate's role as a cofactor or simple reducing agent in enzymatic processes is debated.

Purpose of the Study:

  • To investigate the precise mechanism by which L-Ascorbate (L-Asc) influences HIF prolyl hydroxylase (PHD) activity.
  • To differentiate the role of L-Asc from its isomer D-isoascorbate (D-Asc) and N-acetylcysteine (NAC) in regulating HIF signaling.

Main Methods:

  • Utilized a HIF1 ODD-luc reporter assay to measure PHD activity.
  • Tested the suppressive effects of L-Asc, D-Asc, and N-acetylcysteine (NAC) on reporter activation induced by various PHD inhibitors.
  • Performed molecular docking of L-Asc and D-Asc into the HIF PHD2 crystal structure.

Main Results:

  • L-Ascorbate, but not D-isoascorbate or N-acetylcysteine, suppressed HIF1 ODD-luc reporter activation.
  • Suppression efficiency by L-Asc varied depending on the type of HIF PHD inhibitor used.
  • Molecular docking suggested L-Asc may interfere with the alpha-ketoglutarate binding site, unlike D-Asc.

Conclusions:

  • L-Ascorbate functions as a co-substrate for HIF prolyl hydroxylases, competing for the alpha-ketoglutarate binding site.
  • L-Ascorbate's role is specific and not merely that of a general reducing agent.
  • Findings align with L-Ascorbate's proposed co-substrate role in other dioxygenase enzymes like TET and jumonji demethylases.