Evidence map›Paper›PMID 29846135›Full record

ArticleMolecular biology of the cell2018

Knockdown of a disintegrin A metalloprotease 12 (ADAM12) during adipogenesis reduces cell numbers, delays differentiation, and increases lipid accumulation in 3T3-L1 cells.

Chantal A Coles, Jovana Maksimovic, Jenny Wadeson, Fahri T Fahri, Tracie Webster, Carolina Leyton, Matthew B McDonagh, Jason D White

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

9 citing papers in PubMed, 16 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.

Chantal A ColesMurdoch Children's Research Institute, Royal Children's Hospital, Parkville 3052, Australia.
Jovana MaksimovicMurdoch Children's Research Institute, Royal Children's Hospital, Parkville 3052, Australia.
Jenny WadesonDiscovery Technologies, Department of Environment and Primary -Industries, Victoria Centre for AgriBioscience, La Trobe University, Melbourne 3083, Australia.
Fahri T FahriDepartment of Primary Industries, New South Wales Food Authority, Sydney, New South Wales 2001, Australia.
Tracie WebsterDiscovery Technologies, Department of Environment and Primary -Industries, Victoria Centre for AgriBioscience, La Trobe University, Melbourne 3083, Australia.
Carolina LeytonDiscovery Technologies, Department of Environment and Primary -Industries, Victoria Centre for AgriBioscience, La Trobe University, Melbourne 3083, Australia.
Matthew B McDonaghDiscovery Technologies, Department of Environment and Primary -Industries, Victoria Centre for AgriBioscience, La Trobe University, Melbourne 3083, Australia.
Jason D WhiteMurdoch Children's Research Institute, Royal Children's Hospital, Parkville 3052, Australia.
La Trobe University · AURoyal Children's Hospital · AUNew South Wales Department of Primary Industries · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mouse models have shown that a disintegrin A metalloprotease 12 (ADAM12) is implicated during adipogenesis; the molecular pathways are not well understood. Stealth RNA interference was used to knock down ADAM12 in 3T3-L1 cells. Using gene profiling and metabolic enzymatic markers, we have identified signaling pathways ADAM12 impacts upon during proliferation, differentiation, and maturation of adipocytes. ADAM12 reduced cell numbers in proliferating preadipocytes, delayed differentiation of preadipocytes to adipocytes, and increased lipid accumulation in mature adipocytes. The pathway most affected by ADAM12 knockdown was regulation of insulin-like growth factor (IGF) activity by insulin-like growth factor binding proteins (IGFBPs); ADAM12 is known to cleave IGFBP3 and IGFBP5. The IGF/mTOR signaling pathway was down-regulated, supporting a role for ADAM12 in the IGFBP/IGF/mTOR-growth pathway. PPARγ signaling was also down-regulated by ADAM12 knockdown. Gene ontology (GO) analysis revealed that the extracellular matrix was the cellular compartment most impacted. Filtering for matrisome genes, connective tissue growth factor ( Ctgf) was up-regulated. CTGF and IGBP3 can interact with PPARγ to hinder its regulation. Increased expression of these molecules could have influenced PPARγ signaling reducing differentiation and an imbalance of lipids. We believe ADAM12 regulates cell proliferation of preadipocytes through IGFBP/IGF/mTOR signaling and delays differentiation through altered PPAR signaling to cause an imbalance of lipids within mature adipocytes.

Indexed as

AdipogenesisCell DifferentiationGene Knockdown TechniquesLipid Metabolism3T3-L1 CellsADAM12 ProteinAdipocytesAnimalsBiomarkersCell CountCell ShapeCluster AnalysisGene Expression ProfilingGene Expression RegulationGene OntologyMiceADAM12 ProteinBiomarkers

Identifiers

PMID29846135
PMCPMC6085825
OpenAlexW2885717234

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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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.