Evidence map›Paper›PMID 16855220›Full record

ArticleAmerican journal of physiology. Cell physiology2006

AKT phosphorylation is essential for insulin-induced relaxation of rat vascular smooth muscle cells.

Jin Hee Lee, Louis Ragolia

Abstract read
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In one paragraph

Article in American journal of physiology. Cell physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 60 citations in OpenAlex.

  1. Observational
  2. Article
  3. Review
  4. Insulin resistance, CaFrontiers in physiology · 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

2 authors at 2 institutions in 1 country.

Jin Hee LeeVascular Biology Institute, Winthrop-University Hospital, Mineola, NY 11501, USA.
Louis Ragolia
Stony Brook University · USWinthrop-University Hospital · US

Funding

Control of Vascular Smooth Muscle Function by InsulinR01HL067953 · NHLBI · WINTHROP-UNIVERSITY HOSPITAL · PI RAGOLIA, LOUIS · 2003 to 2006
$1.0M
NHLBI NIH HHS 5 R01 HL-067953-03NHLBI NIH HHS R01 HL067953
6 · The paper itself

Abstract

Insulin resistance, a major factor in the development of type 2 diabetes, is known to be associated with defects in blood vessel relaxation. The role of Akt on insulin-induced relaxation of vascular smooth muscle cell (VSMC) was investigated using siRNA targeting Akt (siAKTc) and adenovirus constructing myristilated Akt to either suppress endogenous Akt or overexpress constitutively active Akt, respectively. siAKTc decreased both basal and insulin-induced phosphorylations of Akt and glycogen synthase kinase 3beta, abolishing insulin-induced nitric oxide synthase (iNOS) expression. cGMP-dependent kinase 1alpha (cGK1alpha) and myosin-bound phosphatase (MBP) activities, both downstream of iNOS, were also decreased. siAKTc treatment resulted in increased insulin and ANG II-stimulated phosphorylation of contractile apparatus, such as MBP substrate (MYPT1) and myosin light chain (MLC20), accompanied by increased Rho-associated kinase alpha (ROKalpha) activity, demonstrating the requirement of Akt for insulin-induced vasorelaxation. Corroborating these results, constitutively active Akt upregulated the signaling molecules involved in insulin-induced relaxation such as iNOS, cGK1alpha, and MBP activity, even in the absence of insulin stimulation. On the contrary, the contractile response involving the phosphorylation of MYPT1 and MLC20, and increased ROKalpha activity stimulated by ANG II were all abolished by overexpressing active Akt. In conclusion, we demonstrated here that insulin-induced VSMC relaxation is dependent on Akt activation via iNOS, cGK1alpha, and MBP activation, as well as the decreased phosphorylations of MYPT1 and MLC20 and decreased ROKalpha activity.

Indexed as

Muscle, Smooth, VascularAngiotensin IIAnimalsCarrier ProteinsCells, CulturedGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHumansInsulinIntracellular Signaling Peptides and ProteinsMaleMyocytes, Smooth MuscleMyosin Light ChainsNitric Oxide Synthase Type IIPhosphoprotein PhosphatasesPhosphorylationAngiotensin IICarrier ProteinsGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGSK3B protein, humanGsk3b protein, ratInsulinIntracellular Signaling Peptides and ProteinsMyosin Light ChainsNitric Oxide Synthase Type IIPhosphoprotein PhosphatasesPpp1r12a protein, ratProtein Phosphatase 1Protein Serine-Threonine KinasesProto-Oncogene Proteins c-aktrho-Associated KinasesRNA, Small Interfering

Identifiers

PMID16855220
PMCPMC1636679
OpenAlexW2063407911

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.