Evidence map›Paper›PMID 22203676›Full record

ArticleThe Journal of biological chemistry2012

Amidoxime reductase system containing cytochrome b5 type B (CYB5B) and MOSC2 is of importance for lipid synthesis in adipocyte mitochondria.

Etienne P A Neve, Asa Nordling, Tommy B Andersson, Ulf Hellman, Ulf Diczfalusy, Inger Johansson, Magnus Ingelman-Sundberg

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 64 citations in OpenAlex.

  1. miR-375 protects against acetaminophen-induced acute liver failure by orchestrating pharmacogene expression.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
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  4. The History of mARC.Molecules (Basel, Switzerland) · 2023
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  5. Hepatocyte mARC1 promotes fatty liver disease.JHEP reports : innovation in hepatology · 2023
    Article
  6. Active Site Structures of theInorganic chemistry · 2023
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  11. Article
  12. Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Review
  14. Article
  15. Article
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  19. Article
  20. Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    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

7 authors at 3 institutions in 2 countries.

Etienne P A NeveSection of Pharmacogenetics, Department of Physiology and Pharmacology, Karolinska Institutet, SE-17177 Stockholm.
Asa Nordling
Tommy B Andersson
Ulf Hellman
Ulf Diczfalusy
Inger Johansson
Magnus Ingelman-Sundberg
Karolinska Institutet · SEAstraZeneca (Australia) · AULudwig Cancer Research · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reduction of hydroxylamines and amidoximes is important for drug activation and detoxification of aromatic and heterocyclic amines. Such a reductase system was previously found to be of high activity in adipose tissue and liver, and furthermore, in vitro studies using recombinant truncated and purified enzymes suggested the participation of cytochrome b(5) reductase (CYB5R), cytochrome b(5) (CYB5), and molybdenum cofactor sulfurase C-terminal containing 1 and 2 (MOSC1 and -2). Here, we show that purified rat liver outer mitochondrial membrane contains high amidoxime reductase activity and that MOSC2 is exclusively localized to these membranes. Moreover, using the same membrane fraction, we could show direct binding of a radiolabeled benzamidoxime substrate to MOSC2. Following differentiation of murine 3T3-L1 cells into mature adipocytes, the MOSC2 levels as well as the amidoxime reductase activity were increased, indicating that the enzyme is highly regulated under lipogenic conditions. siRNA-mediated down-regulation of MOSC2 and the mitochondrial form of cytochrome b(5) type B (CYB5B) significantly inhibited the reductase activity in the differentiated adipocytes, whereas down-regulation of MOSC1, cytochrome b(5) type A (CYB5A), CYB5R1, CYB5R2, or CYB5R3 had no effect. Down-regulation of MOSC2 caused impaired lipid synthesis. These results demonstrate for the first time the direct involvement of MOSC2 and CYB5B in the amidoxime reductase activity in an intact cell system. We postulate the presence of a novel reductive enzyme system of importance for lipid synthesis that is exclusively localized to the outer mitochondrial membrane and is composed of CYB5B, MOSC2, and a third unknown component (a CYB5B reductase).

Indexed as

3T3-L1 CellsAdipocytesAdipogenesisAnimalsCarrier ProteinsCell DifferentiationCell FractionationCytochromes b5FemaleHeme-Binding ProteinsHemeproteinsInactivation, MetabolicLipidsMiceMitochondria, LiverMitochondrial MembranesCarrier ProteinsCYB5B protein, mouseCyb5 protein, ratCytochromes b5Heme-Binding ProteinsHemeproteinsLipidsMitochondrial ProteinsMtarc2 protein, mouseMtarc2 protein, ratOxidoreductasesRNA, Small InterferingXenobiotics

Identifiers

PMID22203676
PMCPMC3307252
OpenAlexW2078243445

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.