CPEB4 Increases Expression of PFKFB3 to Induce Glycolysis and Activate Mouse and Human Hepatic Stellate Cells, Promoting Liver Fibrosis.


Journal

Gastroenterology
ISSN: 1528-0012
Titre abrégé: Gastroenterology
Pays: United States
ID NLM: 0374630

Informations de publication

Date de publication:
07 2020
Historique:
received: 15 07 2019
revised: 27 02 2020
accepted: 02 03 2020
pubmed: 15 3 2020
medline: 1 4 2021
entrez: 15 3 2020
Statut: ppublish

Résumé

We investigated mechanisms of hepatic stellate cell (HSC) activation, which contributes to liver fibrogenesis. We aimed to determine whether activated HSCs increase glycolysis, which is regulated by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), and whether this pathway might serve as a therapeutic target. We performed studies with primary mouse HSCs, human LX2 HSCs, human cirrhotic liver tissues, rats and mice with liver fibrosis (due to bile duct ligation [BDL] or administration of carbon tetrachloride), and CPEB4-knockout mice. Glycolysis was inhibited in cells and mice by administration of a small molecule antagonist of PFKFB3 (3-[3-pyridinyl]-1-[4-pyridinyl]-2-propen-1-one [3PO]). Cells were transfected with small interfering RNAs that knock down PFKFB3 or CPEB4. Up-regulation of PFKFB3 protein and increased glycolysis were early and sustained events during HSC activation and accompanied by increased expression of markers of fibrogenesis; incubation of HSCs with 3PO or knockdown of PFKFB3 reduced their activation and proliferation. Mice with liver fibrosis after BDL had increased hepatic PFKFB3; injection of 3PO immediately after the surgery prevented HSC activation and reduced the severity of liver fibrosis compared with mice given vehicle. Levels of PFKFB3 protein were increased in fibrotic liver tissues from patients compared with non-fibrotic liver. Up-regulation of PFKFB3 in activated HSCs did not occur via increased transcription, but instead via binding of CPEB4 to cytoplasmic polyadenylation elements within the 3'-untranslated regions of PFKFB3 messenger RNA. Knockdown of CPEB4 in LX2 HSCs prevented PFKFB3 overexpression and cell activation. Livers from CPEB4-knockout had decreased PFKFB3 and fibrosis after BDL or administration of carbon tetrachloride compared with wild-type mice. Fibrotic liver tissues from patients and rodents (mice and rats) have increased levels of PFKFB3 and glycolysis, which are essential for activation of HSCs. Increased expression of PFKFB3 is mediated by binding of CPEB4 to its untranslated messenger RNA. Inhibition or knockdown of CPEB4 or PFKFB3 prevents HSC activation and fibrogenesis in livers of mice.

Sections du résumé

BACKGROUND & AIMS
We investigated mechanisms of hepatic stellate cell (HSC) activation, which contributes to liver fibrogenesis. We aimed to determine whether activated HSCs increase glycolysis, which is regulated by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3), and whether this pathway might serve as a therapeutic target.
METHODS
We performed studies with primary mouse HSCs, human LX2 HSCs, human cirrhotic liver tissues, rats and mice with liver fibrosis (due to bile duct ligation [BDL] or administration of carbon tetrachloride), and CPEB4-knockout mice. Glycolysis was inhibited in cells and mice by administration of a small molecule antagonist of PFKFB3 (3-[3-pyridinyl]-1-[4-pyridinyl]-2-propen-1-one [3PO]). Cells were transfected with small interfering RNAs that knock down PFKFB3 or CPEB4.
RESULTS
Up-regulation of PFKFB3 protein and increased glycolysis were early and sustained events during HSC activation and accompanied by increased expression of markers of fibrogenesis; incubation of HSCs with 3PO or knockdown of PFKFB3 reduced their activation and proliferation. Mice with liver fibrosis after BDL had increased hepatic PFKFB3; injection of 3PO immediately after the surgery prevented HSC activation and reduced the severity of liver fibrosis compared with mice given vehicle. Levels of PFKFB3 protein were increased in fibrotic liver tissues from patients compared with non-fibrotic liver. Up-regulation of PFKFB3 in activated HSCs did not occur via increased transcription, but instead via binding of CPEB4 to cytoplasmic polyadenylation elements within the 3'-untranslated regions of PFKFB3 messenger RNA. Knockdown of CPEB4 in LX2 HSCs prevented PFKFB3 overexpression and cell activation. Livers from CPEB4-knockout had decreased PFKFB3 and fibrosis after BDL or administration of carbon tetrachloride compared with wild-type mice.
CONCLUSIONS
Fibrotic liver tissues from patients and rodents (mice and rats) have increased levels of PFKFB3 and glycolysis, which are essential for activation of HSCs. Increased expression of PFKFB3 is mediated by binding of CPEB4 to its untranslated messenger RNA. Inhibition or knockdown of CPEB4 or PFKFB3 prevents HSC activation and fibrogenesis in livers of mice.

Identifiants

pubmed: 32169429
pii: S0016-5085(20)30328-0
doi: 10.1053/j.gastro.2020.03.008
pii:
doi:

Substances chimiques

CPEB4 protein, human 0
Cpeb4 protein, mouse 0
RNA-Binding Proteins 0
Carbon Tetrachloride CL2T97X0V0
PFKFB3 protein, human EC 2.7.1.105
PFKFB3 protein, mouse EC 2.7.1.105
Phosphofructokinase-2 EC 2.7.1.105

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

273-288

Subventions

Organisme : Worldwide Cancer Research
ID : 20-0284
Pays : United Kingdom

Informations de copyright

Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.

Auteurs

Marc Mejias (M)

Angiogenesis in Liver Disease Research Group, August Pi i Sunyer Biomedical Research Institute, Hospital Clinic, University of Barcelona, Barcelona, Spain; Biomedical Research Networking Center on Hepatic and Digestive Disease, Institute of Health Carlos III, Spain.

Javier Gallego (J)

Angiogenesis in Liver Disease Research Group, August Pi i Sunyer Biomedical Research Institute, Hospital Clinic, University of Barcelona, Barcelona, Spain; Biomedical Research Networking Center on Hepatic and Digestive Disease, Institute of Health Carlos III, Spain.

Salvador Naranjo-Suarez (S)

Angiogenesis in Liver Disease Research Group, August Pi i Sunyer Biomedical Research Institute, Hospital Clinic, University of Barcelona, Barcelona, Spain.

Marta Ramirez (M)

Angiogenesis in Liver Disease Research Group, August Pi i Sunyer Biomedical Research Institute, Hospital Clinic, University of Barcelona, Barcelona, Spain.

Nuria Pell (N)

Angiogenesis in Liver Disease Research Group, August Pi i Sunyer Biomedical Research Institute, Hospital Clinic, University of Barcelona, Barcelona, Spain.

Anna Manzano (A)

Department of Physiological Sciences, University of Barcelona, Bellvitge Biomedical Research Institute, Barcelona, Spain.

Clara Suñer (C)

Institute for Research in Biomedicine, The Barcelona Institute of Science and Technology, Barcelona, Spain.

Ramon Bartrons (R)

Department of Physiological Sciences, University of Barcelona, Bellvitge Biomedical Research Institute, Barcelona, Spain.

Raul Mendez (R)

Institute for Research in Biomedicine, The Barcelona Institute of Science and Technology, Barcelona, Spain; Institució Catalana de Recerca i Estudis Avançats, Barcelona, Spain.

Mercedes Fernandez (M)

Angiogenesis in Liver Disease Research Group, August Pi i Sunyer Biomedical Research Institute, Hospital Clinic, University of Barcelona, Barcelona, Spain; Biomedical Research Networking Center on Hepatic and Digestive Disease, Institute of Health Carlos III, Spain. Electronic address: mercefernandez@ub.edu.

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Classifications MeSH