ArticleBiochemical and biophysical research communications2016
Akt isoform-dependent regulation of ATP-Binding cassette A1 expression by apolipoprotein E.
Article in Biochemical and biophysical research communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Metabolism of tissue macrophages in homeostasis and pathology.Cellular & molecular immunology · 2022Review
- ATP-binding cassette transporter A1: A promising therapy target for prostate cancer.Molecular and clinical oncology · 2018Article
- Toward the Language Oscillogenome.Frontiers in psychology · 2018Article
- Emerging roles of calpain proteolytic systems in macrophage cholesterol handling.Cellular and molecular life sciences : CMLS · 2017Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We previously reported that apolipoprotein E (apoE) upregulates ATP-binding cassette transporter A1 (ABCA1) transcription through phosphatidylinositol 3-kinase (PI3K). Here we demonstrate that treatment of murine macrophages with human apoE3 enhanced Akt phosphorylation, and upregulated ABCA1 protein and mRNA expression. Inhibition of PI3K weakened apoE3-induced Akt phosphorylation, and ABCA1 protein and mRNA increase. In contrast, inhibition of Akt only diminished apoE-induced ABCA1 protein but not the mRNA level. Suppression of protein synthesis did not erase the ability of apoE3 to increase ABCA1 protein level. Further, apoE3 increased the resistance of ABCA1 protein to calpain-mediated degradation without affecting calpain activity. Treatment of macrophages with apoE3 selectively enhanced the phosphorylation of Akt1 and Akt2, but not Akt3. Knockdown of Akt1 or Akt2 increased and decreased ABCA1 protein level, respectively; while overexpression of these Akt isoenzymes caused changes in ABCA1 protein level opposite to those induced by knockdown of the corresponding Akt. These data imply that apoE3 guards against calpain-mediated ABCA1 degradation through Akt2.
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Registered trials
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