Cited by 162Fatty Acid Research and HealthLipid metabolism and biosynthesisCholesterol and Lipid Metabolism

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Docosahexaneoic acid (22:6,n-3) regulates rat hepatocyte SREBP-1 nuclear abundance by Erk- and 26S proteasome-dependent pathways

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Botolin, Daniela, Wang, Yun, Christian, Barbara, Jump, Donald B.·2006·Journal of Lipid Research

DOI 10.1194/jlr.m500365-jlr200PMC PMC2764363

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Abstract

Insulin induces and dietary n-3 PUFAs suppress hepatic de novo lipogenesis by controlling sterol-regulatory element binding protein-1 nuclear abundance (nSREBP-1). Our goal was to define the mechanisms involved in this regulatory process. Insulin treatment of rat primary hepatocytes rapidly augments nSREBP-1 and mRNA(SREBP-1c) while suppressing mRNA(Insig-2) but not mRNA(Insig-1). These events are preceded by rapid but transient increases in Akt and Erk phosphorylation. Removal of insulin from hepatocytes leads to a rapid decline in nSREBP-1 [half-time (T1/2) approximately 10 h] that is abrogated by inhibitors of 26S proteasomal degradation. 22:6,n-3, the major n-3 PUFA accumulating in livers of fish oil-fed rats, suppresses hepatocyte levels of nSREBP-1, mRNA(SREBP-1c), and mRNA(Insig-2) but modestly and transiently induces mRNA(Insig-1). More importantly, 22:6,n-3 accelerates the disappearance of hepatocyte nSREBP-1 (T1/2 approximately 4 h) through a 26S proteasome-dependent process. 22:6,n-3 has minimal effects on microsomal SREBP-1 and sterol-regulatory element binding protein cleavage-activating protein or nuclear SREBP-2. 22:6,n-3 transiently inhibits insulin-induced Akt phosphorylation but induces Erk phosphorylation. Inhibitors of Erk phosphorylation, but not overexpressed constitutively active Akt, rapidly attenuate 22:6,n-3 suppression of nSREBP-1. Thus, 22:6,n-3 suppresses hepatocyte nSREBP-1 through 26S proteasome- and Erk-dependent pathways. These studies reveal a novel mechanism for n-3 PUFA regulation of hepatocyte nSREBP-1 and lipid metabolism.

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Authors: Botolin, D., Wang, Y., Christian, B., & Jump, D. B.
Affiliations: Michigan State University (US)
Venue: Journal of Lipid Research
Publisher: Elsevier BV
Published: 2006-01
Volume: 47
Issue: 1
Pages: 181-192
ISSN: 0022-2275 (ISSN-L)
DOI: 10.1194/jlr.m500365-jlr200
PMC: PMC2764363
OpenAlex: W2164098551
Cited by: 162
References: 40
Citations by year: 2026: 2 · 2025: 3 · 2024: 4 · 2023: 6 · 2022: 8 · 2021: 5 · 2020: 4 · 2019: 5 · 2018: 3 · 2017: 7 · 2016: 6 · 2015: 6 · 2014: 5 · 2013: 8 · 2012: 10
FWCI: 11.92
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5357 d)
Locations: Journal of Lipid Research (publishedVersion, cc-by)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: U.S. Department of Agriculture
National Institutes of Health
Cooperative State Research, Education, and Extension Service
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK043220)
Topics: Health Sciences › Nursing › Nutrition and Dietetics › Fatty Acid Research and Health
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
Keywords: docosahexaenoic acid, omega-3 fatty acids, SREBP1, INSIG2, INSIG1, 26S proteasome, ERK1/2 phosphorylation, Akt phosphorylation, insulin signaling, hepatocytes, hepatic de novo lipogenesis, SREBP-1c, SREBP2, lipid metabolism
MeSH terms: Animals, Base Sequence, Cell Nucleus, Dietary Fats, Docosahexaenoic Acids, Insulin, Male, Membrane Proteins, Protease Inhibitors, RNA, Messenger, Rats, Sprague-Dawley, MAP Kinase Signaling System, Hepatocytes, Proteasome Endopeptidase Complex, Intracellular Signaling Peptides and Proteins, Lipid Metabolism, Rats, Sterol Regulatory Element Binding Protein 1, Proteasome Inhibitors

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Docosahexaneoic acid (22:6,n-3) regulates rat hepatocyte SREBP-1 nuclear abundance by Erk- and 26S proteasome-dependent pathways

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