Evidence map›Paper›PMID 19052261›Full record

ArticleAmerican journal of physiology. Cell physiology2009

Impaired insulin-mediated vasorelaxation in diabetic Goto-Kakizaki rats is caused by impaired Akt phosphorylation.

Jin Hee Lee, Thomas Palaia, Louis Ragolia

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 42 citations in OpenAlex.

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  10. Abnormal myosin phosphatase targeting subunit 1 phosphorylation and actin polymerization contribute to impaired myogenic regulation of cerebral arterial diameter in the type 2 diabetic Goto-Kakizaki rat.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2017
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  20. Effects of type II diabetes on exercising skeletal muscle blood flow in the rat.Journal of applied physiology (Bethesda, Md. : 1985) · 2010
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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

3 authors at 1 institution in 1 country.

Jin Hee LeeVascular Biology Institute, Winthrop Univ. Hospital, 222 Station Plaza North, Rm. 505B, Mineola, NY 11501, USA.
Thomas Palaia
Louis Ragolia
Winthrop-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-067953-04
6 · The paper itself

Abstract

Insulin resistance associated with Type 2 diabetes contributes to impaired vasorelaxation. Previously, we showed the phosphorylation of myosin-bound phosphatase substrate MYPT1, a marker of the vascular smooth muscle cell (VSMC) contraction, was negatively regulated by Akt (protein kinase B) phosphorylation in response to insulin stimulation. In this study we examined the role of Akt phosphorylation on impaired insulin-induced vasodilation in the Goto-Kakizaki (GK) rat model of Type 2 diabetes. GK VSMCs had impaired basal and insulin-induced Akt phosphorylation as well as increases in basal MYPT1 phosphorylation, inducible nitric oxide synthase (iNOS) expression, and nitrite/nitrate production compared with Wistar-Kyoto controls. Both iNOS expression and the inhibition of angiotensin (ANG) II-induced MYPT1 phosphorylation were resistant to the effects of insulin in diabetic GK VSMC. We also measured the isometric tension of intact and denuded GK aorta using a myograph and observed significantly impaired insulin-induced vasodilation. Adenovirus-mediated overexpression of constitutively active Akt in GK VSMC led to significantly improved insulin sensitivity in terms of counteracting ANG II-induced contractile signaling via MYPT1, myosin light chain dephosphorylation, and reduced iNOS expression, S-nitrosylation and survivin expression. We demonstrated for the first time the presence of Akt-independent iNOS expression in the GK diabetic model and that the defective insulin-induced vasodilation observed in the diabetic vasculature can be restored by the overexpression of active Akt, which advocates a novel therapeutic strategy for treating diabetes.

Indexed as

Insulin ResistanceSignal TransductionVasodilationAdenoviridaeAngiotensin IIAnimalsAortaCells, CulturedDiabetes Mellitus, Type 2Disease Models, AnimalGenetic VectorsHumansInsulinMaleMicrotubule-Associated ProteinsMuscle, Smooth, VascularAngiotensin IIBirc5 protein, ratInsulinMicrotubule-Associated ProteinsNitric Oxide Synthase Type IINos2 protein, ratPpp1r12a protein, ratProtein Phosphatase 1Proto-Oncogene Proteins c-aktRecombinant ProteinsSurvivin

Identifiers

PMID19052261
PMCPMC2643848
OpenAlexW2031343973

What OpenQuestion holds

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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.