Evidence map›Paper›PMID 21979951›Full record

ArticleThe Journal of biological chemistry2011

Akt2 kinase suppresses glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-mediated apoptosis in ovarian cancer cells via phosphorylating GAPDH at threonine 237 and decreasing its nuclear translocation.

Qiaojia Huang, Fenghua Lan, Zhiyong Zheng, Feilai Xie, Junyong Han, Lihong Dong, Yanchuan Xie, Feng Zheng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
3.3field-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

55 citing papers in PubMed, 100 citations in OpenAlex.

  1. The moonlighting functions of glycolytic enzymes in tumorigenesis.Cellular oncology (Dordrecht, Netherlands) · 2026
    Review
  2. Stress-induced nuclear GAPDH: Scientific update and clinical application.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
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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 1 institution in 1 country.

Qiaojia HuangDepartment of Experimental Medicine, Fuzhou General Hospital (Dongfang Hospital), 156 North Xi-er Huan Road, Fuzhou City, Fujian Province 350025, China. Electronic address: huangqj100@126.com.
Fenghua LanDepartment of Experimental Medicine, Fuzhou General Hospital (Dongfang Hospital), 156 North Xi-er Huan Road, Fuzhou City, Fujian Province 350025, China.
Zhiyong ZhengDepartment of Pathology, Fuzhou General Hospital (Dongfang Hospital), 156 North Xi-er Huan Road, Fuzhou City, Fujian Province 350025, China.
Feilai XieDepartment of Pathology, Fuzhou General Hospital (Dongfang Hospital), 156 North Xi-er Huan Road, Fuzhou City, Fujian Province 350025, China.
Junyong HanDepartment of Experimental Medicine, Fuzhou General Hospital (Dongfang Hospital), 156 North Xi-er Huan Road, Fuzhou City, Fujian Province 350025, China.
Lihong DongDepartment of Experimental Medicine, Fuzhou General Hospital (Dongfang Hospital), 156 North Xi-er Huan Road, Fuzhou City, Fujian Province 350025, China.
Yanchuan XieDepartment of Experimental Medicine, Fuzhou General Hospital (Dongfang Hospital), 156 North Xi-er Huan Road, Fuzhou City, Fujian Province 350025, China.
Feng ZhengDepartment of Nephrology, Fuzhou General Hospital (Dongfang Hospital), 156 North Xi-er Huan Road, Fuzhou City, Fujian Province 350025, China.
Fuzhou General Hospital of Nanjing Military Command · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase B (Akt) plays important roles in regulation of cell growth and survival, but while many aspects of its mechanism of action are known, there are potentially additional regulatory events that remain to be discovered. Here we detected a 36-kDa protein that was co-immunoprecipitated with protein kinase Bβ (Akt2) in OVCAR-3 ovarian cancer cells. The protein was identified to be glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by MALDI-TOF/TOF MS, and the interaction of Akt2 and GAPDH was verified by reverse immunoprecipitation. Our further study showed that Akt2 may suppress GAPDH-mediated apoptosis in ovarian cancer cells. Overexpression of GAPDH increased ovarian cancer cell apoptosis induced by H(2)O(2), which was inhibited by Akt2 overexpression and restored by the PI3K/Akt inhibitor wortmannin or Akt2 siRNA. Akt2 phosphorylated Thr-237 of GAPDH and decreased its nuclear translocation, an essential step for GAPDH-mediated apoptosis. The interaction between Akt2 and GAPDH may be important in ovarian cancer as immunohistochemical analysis of 10 normal and 30 cancerous ovarian tissues revealed that decreased nuclear expression of GAPDH correlated with activation (phosphorylation) of Akt2. In conclusion, our study suggests that activated Akt2 may increase ovarian cancer cell survival via inhibition of GAPDH-induced apoptosis. This effect of Akt2 is partly mediated by its phosphorylation of GAPDH at Thr-237, which results in the inhibition of GAPDH nuclear translocation.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceApoptosisCell Line, TumorCell SurvivalCytoplasmFemaleGlyceraldehyde-3-Phosphate DehydrogenasesHumansModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedOvarian NeoplasmsPhosphorylationProto-Oncogene Proteins c-aktRNA InterferenceGlyceraldehyde-3-Phosphate DehydrogenasesProto-Oncogene Proteins c-akt

Identifiers

PMID21979951
PMCPMC3234938
OpenAlexW2051124098

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.