Evidence map›Paper›PMID 26025205›Full record

ReviewVascular pharmacology2015

The critical role of Akt in cardiovascular function.

Prasanna Abeyrathna, Yunchao Su

Open access · greenAbstract readReview
In one paragraph

Review in Vascular pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 210 papers.

0numbers the graph read from it
0cells of the map it votes in
210citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

210 citing papers in PubMed, 425 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Cytochrome P450 1a (CYP1A)-Knockout Javanese Medaka Fish Exhibit Diabetic Traits and Reduced Reproductive Capacity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Study on the Role and Mechanism ofJournal of cardiovascular development and disease · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

150 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Prasanna AbeyrathnaDepartment of Pharmacology & Toxicology, Medical College of Georgia, Georgia Regents University, Augusta, GA 30912, USA.
Yunchao SuDepartment of Pharmacology & Toxicology, Medical College of Georgia, Georgia Regents University, Augusta, GA 30912, USA. Electronic address: ysu@gru.edu.
Augusta University · US

Funding

eNOS-actin Interaction and Oxygen in Lung EndotheliumR01HL088261 · NHLBI · UNIVERSITY OF FLORIDA · PI SU, YUNCHAO · 2008 to 2012
$1.8M
Calpain Activates Intracellular TGF-beta1 in Pulmonary HypertensionR03HL115078 · NHLBI · AUGUSTA UNIVERSITY · PI SU, YUNCHAO · 2012 to 2013
$146k
Airway and Lung Vascular Remodeling in COPDI01BX002035 · VA · CHARLIE NORWOOD VA MEDICAL CENTER · PI SU, YUNCHAO · 2015 to 2018
–
BLRD VA I01 BX002035NHLBI NIH HHS HL088261NHLBI NIH HHS HL115078NHLBI NIH HHS R01 HL088261NHLBI NIH HHS R03 HL115078
6 · The paper itself

Abstract

Akt kinase, a member of AGC kinases, is important in many cellular functions including proliferation, migration, cell growth and metabolism. There are three known Akt isoforms which play critical and diverse roles in the cardiovascular system. Akt activity is regulated by its upstream regulatory pathways at transcriptional and post-translational levels. Beta-catenin/Tcf-4, GLI1 and Stat-3 are some of few known transcriptional regulators of AKT gene. Threonine 308 and serine 473 are the two critical phosphorylation sites of Akt1. Translocation of Akt to the cell membrane facilitates PDK1 phosphorylation of the threonine site. The serine site is phosphorylated by mTORC2. Ack1, Src, PTK6, TBK1, IKBKE and IKKε are some of the non-canonical pathways which affect the Akt activity. Protein-protein interactions of Akt to actin and Hsp90 increase the Akt activity while Akt binding to other proteins such as CTMP and TRB3 reduces the Akt activity. The action of Akt on its downstream targets determines its function in cardiovascular processes such as cell survival, growth, proliferation, angiogenesis, vasorelaxation, and cell metabolism. Akt promotes cell survival via caspase-9, YAP, Bcl-2, and Bcl-x activities. Inhibition of FoxO proteins by Akt also increases cell survival by transcriptional mechanisms. Akt stimulates cell growth and proliferation through mTORC1. Akt also increases VEGF secretion and mediates eNOS phosphorylation, vasorelaxation and angiogenesis. Akt can increase cellular metabolism through its downstream targets GSK3 and GLUT4. The alterations of Akt signaling play an important role in many cardiovascular pathological processes such as atherosclerosis, cardiac hypertrophy, and vascular remodeling. Several Akt inhibitors have been developed and tested as anti-tumor agents. They could be potential novel therapeutics for the cardiovascular diseases.

Indexed as

AnimalsCardiovascular DiseasesCardiovascular SystemCell ProliferationCell SurvivalHumansProto-Oncogene Proteins c-aktSignal TransductionProto-Oncogene Proteins c-aktAktSignal transductionVascular remodeling

Identifiers

PMID26025205
PMCPMC4659756
OpenAlexW438790120

What OpenQuestion holds

Textmetadata
LicenceTDM
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.