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Study · In vitro (cells) · 2014

6 results

Scavenger receptor CD36 mediates inhibition of cholesterol synthesis via activation of the PPARγ/PGC-1α pathway and Insig1/2 expression in hepatocytes.

Rodrigue-Way A, Caron V, Bilodeau S, Keil S, Hassan M, Lévy E, Mitchell GA, Tremblay A

FASEB journal : official publication of the Federation of American Societies for Experimental Biology26 Dec 2013Cited by 35 (Europe PMC)

PMID24371122 (opens in a new tab)DOI10.1096/fj.13-240168 (opens in a new tab)PepBankPUB-24371122
Publisher pagePubMedAsk about this study
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study6

6 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cells)Mechanism

    In HepG2 cells, the CD36 ligand hexarelin rapidly increased phosphorylation of HMG-CoA reductase at Ser-872, inactivating the enzyme.

    In plain wordsIn lab-grown liver cells, hexarelin quickly switched off the main cholesterol-making enzyme HMG-CoA reductase.

    Peptide
    Hexarelin
    Outcome
    IncreaseHMG-CoA reductase Ser-872 phosphorylation
    Study

    humann: not reported in source

    HepG2 hepatocyte cells
    Outcome group
    Receptor activity and mechanism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Using the CD36 ligand hexarelin, we found a rapid phosphorylation of HMG-CoA reductase Ser-872 in treated cells, resulting in inactivation of the rate-limiting enzyme in sterol synthesis.
    1 context sentence
    Summary · context
    Here, we describe the cellular mechanism by which CD36 activation induces cholesterol depletion in HepG2 cells.
  2. 02LabIn vitro (cells)Mechanism

    In HepG2 cells, hexarelin enhanced ubiquitin-proteasome degradation of HMG-CoA reductase.

    In plain wordsIn lab-grown liver cells, hexarelin increased the breakdown of the cholesterol-making enzyme HMG-CoA reductase.

    Peptide
    Hexarelin
    Outcome
    IncreaseHMG-CoA reductase degradation
    Study

    humann: not reported in source

    HepG2 hepatocyte cells
    Outcome group
    Receptor activity and mechanism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Degradation of HMG-CoA reductase by the ubiquitin-proteasome pathway was also enhanced by hexarelin, through an increased recruitment of the anchor proteins insulin-induced gene (Insig)-1 and Insig-2.
    1 context sentence
    Summary · context
    Here, we describe the cellular mechanism by which CD36 activation induces cholesterol depletion in HepG2 cells.
  3. 03LabIn vitro (cells)Mechanism

    In HepG2 cells, hexarelin increased recruitment of the anchor proteins Insig-1 and Insig-2 to HMG-CoA reductase.

    In plain wordsIn lab-grown liver cells, hexarelin increased the binding of Insig-1 and Insig-2 proteins to the cholesterol-making enzyme.

    Peptide
    Hexarelin
    Outcome
    IncreaseInsig-1 and Insig-2 recruitment
    Study

    humann: not reported in source

    HepG2 hepatocyte cells
    Outcome group
    Receptor activity and mechanism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Degradation of HMG-CoA reductase by the ubiquitin-proteasome pathway was also enhanced by hexarelin, through an increased recruitment of the anchor proteins insulin-induced gene (Insig)-1 and Insig-2.
    1 context sentence
    Summary · context
    Here, we describe the cellular mechanism by which CD36 activation induces cholesterol depletion in HepG2 cells.
  4. 04LabIn vitro (cells)Mechanism

    In HepG2 cells with CD36 activation by hexarelin, SREBP-2 controlled cholesterol synthesis genes remained unresponsive to sterol depletion.

    In plain wordsIn lab-grown liver cells, cholesterol-making genes did not respond to low sterol levels after hexarelin acted on CD36.

    Peptide
    Hexarelin
    Outcome
    No significant changeSREBP-2 target gene response to sterol depletion
    Study

    humann: not reported in source

    HepG2 hepatocyte cells
    Outcome group
    Receptor activity and mechanism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Genes encoding key enzymes involved in cholesterol synthesis and under the control of transcription factor sterol regulatory element-binding protein (SREBP)-2 remained unresponsive to sterol depletion, due to retention of the SREBP-2 escort protein Scap by Insig-1/2.
    2 context sentences
    Summary · context
    Using the CD36 ligand hexarelin, we found a rapid phosphorylation of HMG-CoA reductase Ser-872 in treated cells, resulting in inactivation of the rate-limiting enzyme in sterol synthesis.
    Summary · context
    Here, we describe the cellular mechanism by which CD36 activation induces cholesterol depletion in HepG2 cells.
  5. 05LabIn vitro (cells)Mechanism

    In HepG2 cells, CD36 activation by hexarelin increased Insig1 and Insig2 gene expression through PPARγ activation.

    In plain wordsIn lab-grown liver cells, hexarelin acting on CD36 raised the expression of Insig1 and Insig2 genes.

    Peptide
    Hexarelin
    Outcome
    IncreaseInsig1 and Insig2 gene expression
    Study

    humann: not reported in source

    HepG2 hepatocyte cells
    Outcome group
    Receptor activity and mechanism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Insig1 and Insig2 gene expression was also increased through activation of nuclear receptor peroxisome-proliferator activating receptor γ (PPARγ) by CD36, which lifted the inhibitory effect of PPARγ1 Ser-84 phosphorylation.
    2 context sentences
    Summary · context
    Using the CD36 ligand hexarelin, we found a rapid phosphorylation of HMG-CoA reductase Ser-872 in treated cells, resulting in inactivation of the rate-limiting enzyme in sterol synthesis.
    Summary · context
    Here, we describe the cellular mechanism by which CD36 activation induces cholesterol depletion in HepG2 cells.
  6. 06LabIn vitro (cells)Mechanism

    In HepG2 cells, CD36 activation by hexarelin promoted PGC-1α recruitment to AMPKα and PGC-1α transcriptional activation.

    In plain wordsIn lab-grown liver cells, hexarelin acting on CD36 turned on the PGC-1α gene regulator.

    Peptide
    Hexarelin
    Outcome
    IncreasePGC-1α transcriptional activation
    Study

    humann: not reported in source

    HepG2 hepatocyte cells
    Outcome group
    Receptor activity and mechanism · Liver
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Recruitment of coactivator peroxisome proliferator-activated receptor-γ coactivator 1α (PGC1α) to activated AMPKα was also promoted, resulting in PGC-1α transcriptional activation through Sirt1-mediated deacetylation, increased recruitment of PPARγ, and up-regulation of Insig-1/2, revealing a regula…
    2 context sentences
    Summary · context
    Using the CD36 ligand hexarelin, we found a rapid phosphorylation of HMG-CoA reductase Ser-872 in treated cells, resulting in inactivation of the rate-limiting enzyme in sterol synthesis.
    Summary · context
    Here, we describe the cellular mechanism by which CD36 activation induces cholesterol depletion in HepG2 cells.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    13 Oct 2026, 21:44 UTC

    Study results updated

  2. Version 1

    13 Oct 2026, 16:31 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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