Evidence map›Paper›PMID 31530151›Full record

ArticleCell cycle (Georgetown, Tex.)2019

Involvement of CaMKII in regulating the release of diplotene-arrested mouse oocytes by pAkt1 (Ser473).

Lingling Liu, Hanwen Li, Ben Labbe, Yang Wang, Shitao Mao, Yu Cao, Mingjing Zhao, Shuo Liu, Hang Yu, Xin Deng

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

Article in Cell cycle (Georgetown, Tex.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

1 citing paper in PubMed, 11 citations in OpenAlex.

  1. 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

10 authors at 3 institutions in 2 countries.

Lingling LiuCentral Laboratory of the Fourth Affiliated Hospital, CMU , Shenyang , PR China.
Hanwen LiDepartment of Anorectum, the Fourth Affiliated Hospital, China Medical University (CMU) , Shenyang , PR China.
Ben LabbeDepartment of Microbiology and Immunology, Indiana University School of Medicine , Indianapolis, IN , USA.
Yang WangDepartment of Physiology, China Medical University (CMU) , Shenyang , PR China.
Shitao MaoDepartment of Pneumology, the Fourth Affiliated Hospital, CMU , Shenyang , PR China.
Yu CaoDepartment of Physiology, China Medical University (CMU) , Shenyang , PR China.
Mingjing ZhaoDepartment of Pneumology, the Fourth Affiliated Hospital, CMU , Shenyang , PR China.
Shuo LiuDepartment of Pneumology, the Fourth Affiliated Hospital, CMU , Shenyang , PR China.
Hang YuDepartment of Biophysics, China Medical University (CMU) , Shenyang , China.
Xin DengCentral Laboratory of the Fourth Affiliated Hospital, CMU , Shenyang , PR China.ORCID https://orcid.org/0000-0001-7846-7389
Fourth Affiliated Hospital of China Medical University · CNChina Medical University · CNIndiana University School of Medicine

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcium (Ca2+)/calmodulin-dependent protein kinase II (CaMKII) had been reported to play a role in the process of fertilization. However, the role of CaMKII in the release of diplotene-arrested oocytes is poorly understood. In this study, we explored the potential effect of CaMKII on Akt1 and the relationship among CaMKII, Akt1 and phosphatidylinositol (3,4,5)-trisphosphate (PIP3) during the meiotic resumption of mouse oocytes. We found that inhibition of CaMKII aggravated diplotene arrest. We detected the expression and distribution of pCaMKII (Thr286), pAkt1 (Ser473), Cdc25B and pCdc2 (Tyr15) when oocytes were treated with KN-93, SH-6, LY294002 or PIP3, respectively. Our data showed that down-regulated CaMKII by KN-93 decreased the levels of pAkt1 (Ser473) and rearranged the distribution of pAkt1 (Ser473). Meanwhile, down-regulated pAkt1 (Ser473) by SH-6 also decreased the levels of pCaMKII (Thr286), Cdc25B and pCdc2 (Tyr15) significantly and rearranged the distributions of pCaMKII (Thr286). Furthermore, our data showed that exogenous PIP3 up-regulated GVBD rates significantly and increased the levels of pCaMKII (Thr286) and pAkt1 (Ser473). On the contrary, down-regulation of PIP3 by LY294002 decreased GVBD rates and the levels of pCaMKII (Thr286) and pAkt1 (Ser473), respectively. Our results showed that Akt1 and CaMKII regulated each other, and PIP3 may be involved in these regulations during the release of mouse oocytes from diplotene arrest.

Indexed as

AnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2cdc25 PhosphatasesCDC2 Protein KinaseFemaleMeiotic Prophase IMiceOocytesPhosphatidylinositol PhosphatesProto-Oncogene Proteins c-aktAkt1 protein, mouseCalcium-Calmodulin-Dependent Protein Kinase Type 2Cdc25b protein, mousecdc25 PhosphatasesCDC2 Protein KinaseCdk1 protein, mousephosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol PhosphatesProto-Oncogene Proteins c-aktCalcium (Ca2+)/calmodulin-dependent protein kinase II (CaMKII)diplotene arrestmouse oocyteprotein kinase B alpha (PKBα/Akt1)

Identifiers

PMID31530151
PMCPMC6791694
OpenAlexW2973856035

What OpenQuestion holds

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Registered trials

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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.