Evidence map›Paper›PMID 26801741›Full record

ArticleJournal of molecular and cellular cardiology2016

Polymerase delta-interacting protein 2 regulates collagen accumulation via activation of the Akt/mTOR pathway in vascular smooth muscle cells.

Masakazu Fujii, Angélica Amanso, Thalita B Abrahão, Bernard Lassègue, Kathy K Griendling

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular and cellular cardiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

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  11. Polymerase δ-interacting Protein 2: A Multifunctional Protein.Journal of cardiovascular pharmacology · 2017
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Masakazu FujiiDivision of Cardiology, Department of Medicine, Emory University, Atlanta, GA, United States.
Angélica AmansoDivision of Cardiology, Department of Medicine, Emory University, Atlanta, GA, United States.
Thalita B AbrahãoDivision of Cardiology, Department of Medicine, Emory University, Atlanta, GA, United States.
Bernard LassègueDivision of Cardiology, Department of Medicine, Emory University, Atlanta, GA, United States.
Kathy K GriendlingDivision of Cardiology, Department of Medicine, Emory University, Atlanta, GA, United States. Electronic address: kgriend@emory.edu.
Emory University · US

Funding

T cell triggering events and hypertensionP01HL095070 · NHLBI · EMORY UNIVERSITY · PI JO, HANJOONG · 2009 to 2019
$20.5M
NOX4 and vascular smooth muscle differentiationR37HL038206 · NHLBI · EMORY UNIVERSITY · PI GRIENDLING, KATHY K · 2006 to 2015
$3.8M
VASCULAR SMOOTH MUSCLE PHOSPHOLIPASE DR01HL038206 · NHLBI · EMORY UNIVERSITY · PI GRIENDLING, KATHY K · 1993 to 2005
$2.1M
DIACYLGLYCEROL SIGNALING IN VASCULAR SMOOTH MUSCLER29HL038206 · NHLBI · EMORY UNIVERSITY · PI GRIENDLING, KATHY K · 1987 to 1991
–
NHLBI NIH HHS HL095070NHLBI NIH HHS HL38206NHLBI NIH HHS P01 HL095070NHLBI NIH HHS R01 HL038206NHLBI NIH HHS R37 HL038206
6 · The paper itself

Abstract

objectivesPolymerase delta interacting protein 2 (Poldip2) has previously been implicated in migration, proliferation and extracellular matrix (ECM) production in vascular smooth muscle cells. To better understand the role of Poldip2 in ECM regulation, we investigated the mechanism responsible for collagen I accumulation in Poldip2(+/-) mouse aortic smooth muscle cells (MASMs). APPROACH AND

resultsProtein degradation and protein synthesis pathways were investigated. Depletion of Poldip2 had no effect on proteasome activity, but caused a partial reduction in autophagic flux. However, the rate of collagen I degradation was increased in Poldip2(+/-) vs. Poldip2(+/+) MASMs. Conversely, activation of the PI3K/Akt/mTOR signaling pathway, involved in regulation of protein synthesis, was significantly elevated in Poldip2(+/-) MASMs as was β1-integrin expression. Suppressing mTOR signaling using Akt inhibitor or rapamycin and reducing β1-integrin expression using siRNA prevented the increase in collagen I production. While collagen I and fibronectin were increased in Poldip2(+/-) MASMs, overall protein synthesis was not different from that in Poldip2(+/)(+)MASMs, suggesting selectivity of Poldip2 for ECM proteins.

conclusionsPoldip2(+/-) MASMs exhibit higher β1-integrin expression and activity of the PI3K/Akt/mTOR signaling pathway, leading to increased ECM protein synthesis. These findings have important implications for vascular diseases in which ECM accumulation plays a role.

Indexed as

AnimalsAortaCell ProliferationCollagen Type IExtracellular MatrixFibronectinsIntegrin beta ChainsMiceMitochondrial ProteinsMuscle, Smooth, VascularMyocytes, Smooth MuscleNuclear ProteinsPhosphatidylinositol 3-KinasesProteasome Endopeptidase ComplexProtein BiosynthesisProteolysisCollagen Type IFibronectinsIntegrin beta ChainsMitochondrial Proteinsmitogenin 1 protein, mouseMTOR protein, humanNuclear ProteinsPhosphatidylinositol 3-KinasesProteasome Endopeptidase ComplexProto-Oncogene Proteins c-aktTOR Serine-Threonine KinasesExtracellular matrixmTORPoldip2Vascular smooth muscle

Identifiers

PMID26801741
PMCPMC4825175
OpenAlexW2276467918

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.