Evidence map›Paper›PMID 22447946›Full record

ArticleAmerican journal of physiology. Heart and circulatory physiology2012

TGF-β and Smad3 modulate PI3K/Akt signaling pathway in vascular smooth muscle cells.

Pasithorn A Suwanabol, Stephen M Seedial, Fan Zhang, Xudong Shi, Yi Si, Bo Liu, K Craig Kent

Erratum issuedAbstract read
In one paragraph

Article in American journal of physiology. Heart and circulatory physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

53 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
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  5. Observational
  6. Systemic sclerosis, main culprits and involved signaling pathways.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025
    Review
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  10. International journal of molecular sciences · 2025
    Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Pasithorn A SuwanabolDivision of Vascular Surgery, Department of Surgery, University of Wisconsin, Madison, 53592-7375, USA.
Stephen M Seedial
Fan Zhang
Xudong Shi
Yi Si
Bo Liu
K Craig Kent
University of Wisconsin–Madison · US

Funding

RESEARCH TRAINING IN HEMATOLOGYT32HL007899 · NHLBI · UNIVERSITY OF WISCONSIN-MADISON · PI Jane Ellen Churpek · 1998 to 2026
$8.2M
TGF-Beta in Intimal Hyperplasia after Vascular BypassR01HL068673 · NHLBI · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI KENT, K CRAIG · 2002 to 2017
$4.9M
Howard Hughes Medical InstituteNHLBI NIH HHS R01 HL068673NHLBI NIH HHS R01-HL-068673NHLBI NIH HHS T32 HL007899NHLBI NIH HHS T32-HL-07899
6 · The paper itself

Abstract

Transforming growth factor-β (TGF-β) is upregulated at the time of arterial injury; however, the mechanism through which TGF-β enhances the development of intimal hyperplasia is not clear. Recent studies from our laboratory suggest that in the presence of elevated levels of Smad3, TGF-β stimulates smooth muscle cell (SMC) proliferation. This is a novel phenomenon in that TGF-β has traditionally been known as a potent inhibitor of cellular proliferation. In these studies we explore the signaling pathways through which TGF-β mediates its proliferative effect in vascular SMCs. We found that TGF-β phosphorylates and activates Akt in a time-dependent manner, and this effect is significantly enhanced by overexpression of Smad3. Furthermore, both chemical and molecular inhibition of Smad3 can reverse the effect of TGF-β on Akt. Although we found numerous signaling pathways that might function as intermediates between Smad3 and Akt, p38 appeared the most promising. Overexpression of Smad3 enhanced p38 phosphorylation and inhibition of p38 with a chemical inhibitor or a small interfering RNA blocked TGF-β-induced Akt phosphorylation. Moreover, TGF-β/Smad3 enhancement of SMC proliferation was blocked by inhibition of p38. Phosphorylation of Akt by TGF-β/Smad3 was not dependent on gene expression or protein synthesis, and immunoprecipitation studies revealed a physical association among p38, Akt, and Smad3 suggesting that activation requires a direct protein-protein interaction. Our findings were confirmed in vivo where overexpression of Smad3 in a rat carotid injury model led to enhancement of p-p38, p-Akt, as well as SMC proliferation. Furthermore, inhibition of p38 in vivo led to decreased Akt phosphorylation and SMC proliferation. In summary, our studies reveal a novel pathway whereby TGF-β/Smad3 stimulates SMC proliferation through p38 and Akt. These findings provide a potential mechanism for the substantial effect of TGF-β on intimal hyperplasia and suggest new targets for chemical or molecular prevention of vascular restenosis.

Indexed as

Cell ProliferationAnimalsCarotid Artery InjuriesCells, CulturedIn Vitro TechniquesMaleModels, AnimalMuscle, Smooth, Vascularp38 Mitogen-Activated Protein KinasesPhosphatidylinositol 3-KinasesPhosphorylationProto-Oncogene Proteins c-aktRatsRats, Sprague-DawleyRNA, Small InterferingSignal Transductionp38 Mitogen-Activated Protein KinasesPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktRNA, Small InterferingSmad3 ProteinTransforming Growth Factor beta

Identifiers

PMID22447946
PMCPMC3378292
OpenAlexW1993976160

What OpenQuestion holds

Textmetadata
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.