Evidence map›Paper›PMID 17531997›Full record

ArticleAtherosclerosis2008

Structure-function properties of the apoE-dependent COX-2 pathway in vascular smooth muscle cells.

Kamilah Ali, Sissel Lund-Katz, John Lawson, Michael C Phillips, Daniel J Rader

Abstract read
In one paragraph

Article in Atherosclerosis, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
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  4. TNF-α-Induced cPLAFrontiers in pharmacology · 2016
    Article
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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

5 authors at 3 institutions in 1 country.

Kamilah AliInstitute for Translational Medicine and Therapeutics, Department of Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA, United States.
Sissel Lund-KatzDivision of Gastroenterology, Hepatology, and Nutrition, The Children's Hospital of Philadelphia, University of Pennsylvania School of Medicine, Philadelphia, PA, United States.
John LawsonInstitute for Translational Medicine and Therapeutics, Department of Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA, United States.
Michael C PhillipsDivision of Gastroenterology, Hepatology, and Nutrition, The Children's Hospital of Philadelphia, University of Pennsylvania School of Medicine, Philadelphia, PA, United States.
Daniel J RaderInstitute for Translational Medicine and Therapeutics, Department of Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA, United States. Electronic address: rader@mail.med.upenn.edu.
University of Pennsylvania · USChildren's Hospital of Philadelphia · USPhiladelphia University · US

Funding

STUDIES OF PLATELET ADHERENCE TO OSTEOPONTINP01HL062250 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI FITZGERALD, GARRET A · 1999 to 2013
$28.4M
STRUCTURAL BASIS OF THE INTERACTIONS OF APOLIPOPROTEIN ER01HL056083 · NHLBI · MCP HAHNEMANN UNIVERSITY · PI LUND-KATZ, SISSEL · 1997 to 2013
$5.0M
PHYSIOLOGY AND BIOCHEMISTRY OF ARTERIOSCLEROSIST32HL007443 · NHLBI · MCP HAHNEMANN UNIVERSITY · PI PHILLIPS, MICHAEL C. · 1985 to 2004
$1.0M
NHLBI NIH HHS HL07443NHLBI NIH HHS HL56083NHLBI NIH HHS P01 HL062250NHLBI NIH HHS P01-HL62250NHLBI NIH HHS R01 HL056083NHLBI NIH HHS T32 HL007443
6 · The paper itself

Abstract

Apolipoprotein (apoE) E is a multifunctional protein that plays a critical role in atherogenesis, in part by regulating the intimal proliferation of vascular smooth muscle cells. Recently, a novel cyclooxygenase (COX)-2 pathway was shown to contribute to the anti-proliferative action of human apoE3 in vascular smooth muscle cells (VSMC). Here, we provide insight into the structure-function properties by which apoE mediates these effects. ApoE3 is most effective in promoting COX-2 expression as a lipid-free protein and is less active after lipidation. Alterations in the stability of the helix bundle N-terminal domain of apoE that contains the binding site for the low density lipoprotein (LDL) receptor and heparin do not affect the up-regulation of the COX-2 pathway. In addition, the apoE2, 3, and 4 isoforms are all capable of up-regulating the COX-2 pathway. Finally, the effect of apoE on COX-2 was found to be independent of expression on the VSMC surface of the LDL receptor and heparan sulfate proteoglycans (HSPG). In summary, our data indicates that apoE, particularly in the lipid-free state, can up-regulate COX-2 in murine vascular smooth muscle cells apparently independently of binding to the LDLR, LRP or HSPG.

Indexed as

AnimalsApolipoprotein E3Cyclooxygenase 2Heparan Sulfate ProteoglycansMiceMice, KnockoutMuscle, Smooth, VascularMyocytes, Smooth MuscleSignal TransductionStructure-Activity RelationshipUp-RegulationApolipoprotein E3Cyclooxygenase 2Heparan Sulfate ProteoglycansPtgs2 protein, mouse

Identifiers

PMID17531997
PMCPMC3328805
OpenAlexW2001219970

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.