Evidence map›Paper›PMID 32200954›Full record

ArticleBiomedical journal2020

Defects in CISD-1, a mitochondrial iron-sulfur protein, lower glucose level and ATP production in Caenorhabditis elegans.

Kuei-Ching Hsiung, Kuan-Yu Liu, Ting-Fen Tsai, Sawako Yoshina, Shohei Mitani, Bertrand Chin-Ming Tan, Szecheng J Lo

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomedical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 41% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structure and biological evaluation ofAdvances in redox research · 2022
    Article
  7. Article
  8. Article
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.

Kuei-Ching HsiungDepartment and Institute of Biomedical Sciences, College of Medicine, Chang Gung University, Taoyuan, Taiwan.
Kuan-Yu LiuDepartment and Institute of Biomedical Sciences, College of Medicine, Chang Gung University, Taoyuan, Taiwan.
Ting-Fen TsaiNational Yang Ming University, Department of Life Science, Taipei, Taiwan.
Sawako YoshinaDepartment of Physiology, Tokyo Women's Medical University, School of Medicine and CREST, Japan Science and Technology, Tokyo, Japan.
Shohei MitaniDepartment of Physiology, Tokyo Women's Medical University, School of Medicine and CREST, Japan Science and Technology, Tokyo, Japan.
Bertrand Chin-Ming TanDepartment and Institute of Biomedical Sciences, College of Medicine, Chang Gung University, Taoyuan, Taiwan; Molecular Medicine Research Center, Chang Gung University, Taoyuan, Taiwan; Department of Neurosurgery, Chang Gung Memorial Hospital at Linkou, Taoyuan, Taiwan. Electronic address: btan@mail.cgu.edu.tw.
Szecheng J LoDepartment and Institute of Biomedical Sciences, College of Medicine, Chang Gung University, Taoyuan, Taiwan. Electronic address: losj@mail.cgu.edu.tw.
Chang Gung University · TWTokyo Women's Medical University · JPNational Yang Ming Chiao Tung University · TW

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Ann E. Rougvie · 2012 to 2026
$7.5M
NIH HHS P40 OD010440
6 · The paper itself

Abstract

backgroundCDGSH iron sulfur domain-containing protein 1 (CISD-1) belongs to the CISD protein family that is evolutionary conserved across different species. In mammals, CISD-1 protein has been implicated in diseases such as cancers and diabetes. As a tractable model organism to study disease-associated proteins, we employed Caenorhabditis elegans in this study with an aim to establish a model for interrogating the functional relevance of CISD-1 in human metabolic conditions.

methodsWe first bioinformatically identified the human Cisd-1 homologue in worms. We then employed N2 wild-type and cisd-1(tm4993) mutant to investigate the consequences of CISD-1 loss-of-function on: 1) the expression pattern of CISD-1, 2) mitochondrial morphology pattern, 3) mitochondrial function and bioenergetics, and 4) the effects of anti-diabetes drugs.

resultsWe first identified C. elegans W02B12.15 gene as the human Cisd-1 homologous gene, and pinpointed the localization of CISD-1 to the outer membrane of mitochondria. As compared with the N2 wild-type worm, cisd-1(tm4993) mutant exhibited a higher proportion of hyperfused form of mitochondria. This structural abnormality was associated with the generation of higher levels of ROS and mitochondrial superoxide but lower ATP. These physiological changes in mutants did not result in discernable effects on animal motility and lifespan. Moreover, the amount of glucose in N2 wild-type worms treated with troglitazone and pioglitazone, derivatives of TZD, was reduced to a comparable level as in the mutant animals.

conclusionsBy focusing on the Cisd-1 gene, our study established a C. elegans genetic system suitable for modeling human diabetes-related diseases.

Indexed as

Adenosine TriphosphateAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsEnergy MetabolismGlucoseIron-Sulfur ProteinsLongevityMitochondriaMitochondrial ProteinsAdenosine TriphosphateCaenorhabditis elegans ProteinsCISD1 protein, humanGlucoseIron-Sulfur ProteinsMitochondrial ProteinsC. elegansDiabetesGlucose consumptionIron-sulfur containing proteinLifespanROS

Identifiers

PMID32200954
PMCPMC7090286
OpenAlexW3007886688

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.