Evidence map›Paper›PMID 28487951›Full record

ArticleMolecular medicine reports2017

Berberine activates AMPK to suppress proteolytic processing, nuclear translocation and target DNA binding of SREBP-1c in 3T3-L1 adipocytes.

Jaewoong Jang, Yoonju Jung, Seong Jun Seo, Seok-Min Kim, Yae Jie Shim, Soo Hyun Cho, Sang-In Chung, Yoosik Yoon

Open access · hybridAbstract read
In one paragraph

Article in Molecular medicine reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.4field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 43 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Jaewoong JangDepartment of Microbiology, Chung‑Ang University College of Medicine, Dongjak‑gu, Seoul 156‑756, Republic of Korea.
Yoonju JungDepartment of Microbiology, Chung‑Ang University College of Medicine, Dongjak‑gu, Seoul 156‑756, Republic of Korea.
Seong Jun SeoDepartment of Dermatology, Chung‑Ang University College of Medicine, Dongjak‑gu, Seoul 156‑756, Republic of Korea.
Seok-Min KimSchool of Mechanical Engineering, Chung‑Ang University, Dongjak‑gu, Seoul 156‑756, Republic of Korea.
Yae Jie ShimCollege of General Studies, Sangmyung University, Jongno‑gu, Seoul 110‑743, Republic of Korea.
Soo Hyun ChoDepartment of Family Medicine, College of Medicine, Chung‑Ang University Hospital, Dongjak‑gu, Seoul 156‑755, Republic of Korea.
Sang-In ChungDepartment of Microbiology, Chung‑Ang University College of Medicine, Dongjak‑gu, Seoul 156‑756, Republic of Korea.
Yoosik YoonDepartment of Microbiology, Chung‑Ang University College of Medicine, Dongjak‑gu, Seoul 156‑756, Republic of Korea.
Chung-Ang University · KRChung-Ang University Hospital · KRSangmyung University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AMP-activated protein kinase (AMPK) and sterol regulatory element binding protein (SREBP)‑1c are major therapeutic targets in the treatment of metabolic diseases. In the present study, the fat‑reducing mechanisms of berberine (BBR), a natural isoquinoline, was investigated by examining the AMPK‑mediated modulation of SREBP‑1c in 3T3‑L1 adipocytes. BBR activated AMPK in a dose‑ and time‑dependent manner, and increased the phosphorylation of the 125‑kDa precursor form of SREBP‑1c, which suppressed its proteolytic processing into the mature 68‑kDa form and its subsequent nuclear translocation. The binding of nuclear SREBP‑1c to its E‑box motif‑containing target DNA sequence was decreased following treatment with BBR, which led to a decrease in the expression of lipogenic genes and subsequently reduced intracellular fat accumulation. Transfection with AMPKα1 siRNA, and not control siRNA, inhibited BBR‑induced phosphorylation of the 125‑kDa SREBP‑1c, which confirmed that AMPK was responsible for phosphorylating SREBP‑1c. AMPKα1 siRNA transfection rescued the proteolytic processing, nuclear translocation and target DNA binding of SREBP‑1c that had been suppressed by BBR. In addition, BBR‑induced suppression of lipogenic gene expression and intracellular fat accumulation were rescued by AMPKα1 siRNA transfection. In conclusion, the results of the present study demonstrate that BBR activates AMPK to induce phosphorylation of SREBP‑1c, thereby suppressing proteolytic processing, nuclear translocation and target DNA binding of SREBP‑1c, which leads to a reduction in lipogenic gene expression and intracellular fat accumulation. The results of the present study indicate that BBR may be a potential candidate for the development of drugs to treat obesity.

Indexed as

3T3-L1 CellsActive Transport, Cell NucleusAdipocytesAdipogenesisAMP-Activated Protein KinasesAnimalsBerberineDNA-Binding ProteinsDose-Response Relationship, DrugGene Expression RegulationGene Knockdown TechniquesLipogenesisMiceModels, BiologicalProteolysisSterol Regulatory Element Binding Protein 1AMP-Activated Protein KinasesBerberineDNA-Binding ProteinsSterol Regulatory Element Binding Protein 1

Identifiers

PMID28487951
PMCPMC5436149
OpenAlexW2609430170

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.