Evidence map›Paper›PMID 22829653›Full record

ArticleJournal of lipid research2012

The acyl-CoA binding protein is required for normal epidermal barrier function in mice.

Maria Bloksgaard, Signe Bek, Ann-Britt Marcher, Ditte Neess, Jonathan Brewer, Hans Kristian Hannibal-Bach, Torben Helledie, Christina Fenger, Marianne Due, Zane Berzina and 9 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 35 citations in OpenAlex.

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  12. Acyl-CoA metabolism and partitioning.Annual review of nutrition · 2014
    Review
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

19 authors at 3 institutions in 2 countries.

Maria BloksgaardDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark; MEMPHYS-Center for Biomembrane Physics, University of Southern Denmark, DK-5230 Odense, Denmark.
Signe BekDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark.
Ann-Britt MarcherDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark.
Ditte NeessDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark.
Jonathan BrewerDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark; MEMPHYS-Center for Biomembrane Physics, University of Southern Denmark, DK-5230 Odense, Denmark.
Hans Kristian Hannibal-BachDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark.
Torben HelledieDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark.
Christina FengerInstitute of Molecular Medicine, University of Southern Denmark, DK-5230 Odense, Denmark.
Marianne DueDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark.
Zane BerzinaDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark.
Reinhard NeubertInstitut für Pharmazie, Martin-Luther-Universität Halle-Wittenberg, Halle, Germany.
John ChemnitzInstitute of Molecular Medicine, University of Southern Denmark, DK-5230 Odense, Denmark.
Bente FinsenInstitute of Molecular Medicine, University of Southern Denmark, DK-5230 Odense, Denmark.
Anders ClemmensenDepartment of Dermatology, Odense University Hospital, Odense, Denmark; and.
Johannes WilbertzDepartment of Dermatology, Karolinska Center of Transgene Technologies, Stockholm, Sweden.
Henrik SaxtorphLaboratory Animal Science and Comparative Medicine, University of Southern Denmark, DK-5230 Odense, Denmark and.
Jens KnudsenDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark.
Luis BagatolliDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark; MEMPHYS-Center for Biomembrane Physics, University of Southern Denmark, DK-5230 Odense, Denmark; Danish Molecular Biomedical Imaging Center (DaMBIC), University of Southern Denmark, DK-5230 Odense, Denmark. Electronic address: bagatolli@memphys.sdu.dk.
Susanne MandrupDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark. Electronic address: s.mandrup@bmb.sdu.dk.
University of Southern Denmark · DKMartin Luther University Halle-Wittenberg · DEOdense University Hospital · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The acyl-CoA binding protein (ACBP) is a 10 kDa intracellular protein expressed in all eukaryotic species. Mice with targeted disruption of Acbp (ACBP(-/-) mice) are viable and fertile but present a visible skin and fur phenotype characterized by greasy fur and development of alopecia and scaling with age. Morphology and development of skin and appendages are normal in ACBP(-/-) mice; however, the stratum corneum display altered biophysical properties with reduced proton activity and decreased water content. Mass spectrometry analyses of lipids from epidermis and stratum corneum of ACBP(+/+) and ACBP(-/-) mice showed very similar composition, except for a significant and specific decrease in the very long chain free fatty acids (VLC-FFA) in stratum corneum of ACBP(-/-) mice. This finding indicates that ACBP is critically involved in the processes that lead to production of stratum corneum VLC-FFAs via complex phospholipids in the lamellar bodies. Importantly, we show that ACBP(-/-) mice display a ∼50% increased transepidermal water loss compared with ACBP(+/+) mice. Furthermore, skin and fur sebum monoalkyl diacylglycerol (MADAG) levels are significantly increased, suggesting that ACBP limits MADAG synthesis in sebaceous glands. In summary, our study shows that ACBP is required for production of VLC-FFA for stratum corneum and for maintaining normal epidermal barrier function.

Indexed as

AnimalsCholesterolDiazepam Binding InhibitorEpidermisLipid MetabolismLipidsMass SpectrometryMiceMice, Inbred StrainsPhenotypeSebaceous GlandsSkinCholesterolDiazepam Binding InhibitorLipids

Identifiers

PMID22829653
PMCPMC3435549
OpenAlexW2165464486

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.