Evidence map›Paper›PMID 23717309›Full record

ArticleFrontiers in immunology2013

Role of arginase in vessel wall remodeling.

William Durante

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

43 citing papers in PubMed, 87 citations in OpenAlex.

  1. Trial
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  9. Albumin Is a Component of the Esterase Status of Human Blood Plasma.International journal of molecular sciences · 2023
    Article
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  11. Article
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  13. Article
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  15. Aging of Vascular System Is a Complex Process: The Cornerstone Mechanisms.International journal of molecular sciences · 2022
    Review
  16. 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

1 author at 1 institution in 1 country.

William DuranteDepartment of Medical Pharmacology and Physiology, University of Missouri-Columbia Columbia, MO, USA.
University of Missouri · US

Funding

CARBON MONOXIDE AND VASCULAR SMOOTH MUSCLE CELL FUNCTIONR01HL059976 · NHLBI · UNIVERSITY OF MISSOURI-COLUMBIA · PI DURANTE, WILLIAM · 1999 to 2013
$3.3M
ARGINASE AND ARTERIAL INJURYR01HL074966 · NHLBI · UNIVERSITY OF MISSOURI-COLUMBIA · PI DURANTE, WILLIAM · 2005 to 2009
$1.6M
NHLBI NIH HHS R01 HL059976NHLBI NIH HHS R01 HL074966
6 · The paper itself

Abstract

Arginase metabolizes the semi-essential amino acid l-arginine to l-ornithine and urea. There are two distinct isoforms of arginase, arginase I and II, which are encoded by separate genes and display differences in tissue distribution, subcellular localization, and molecular regulation. Blood vessels express both arginase I and II but their distribution appears to be cell-, vessel-, and species-specific. Both isoforms of arginase are induced by numerous pathologic stimuli and contribute to vascular cell dysfunction and vessel wall remodeling in several diseases. Clinical and experimental studies have documented increases in the expression and/or activity of arginase I or II in blood vessels following arterial injury and in pulmonary and arterial hypertension, aging, and atherosclerosis. Significantly, pharmacological inhibition or genetic ablation of arginase in animals ameliorates abnormalities in vascular cells and normalizes blood vessel architecture and function in all of these pathological states. The detrimental effect of arginase in vascular remodeling is attributable to its ability to stimulate vascular smooth muscle cell and endothelial cell proliferation, and collagen deposition by promoting the synthesis of polyamines and l-proline, respectively. In addition, arginase adversely impacts arterial remodeling by directing macrophages toward an inflammatory phenotype. Moreover, the proliferative, fibrotic, and inflammatory actions of arginase in the vasculature are further amplified by its capacity to inhibit nitric oxide (NO) synthesis by competing with NO synthase for substrate, l-arginine. Pharmacologic or molecular approaches targeting specific isoforms of arginase represent a promising strategy in treating obstructive fibroproliferative vascular disease.

Indexed as

arginaseendothelial dysfunctionnitric oxidesmooth muscle cell proliferationvascular remodeling

Identifiers

PMID23717309
PMCPMC3651990
OpenAlexW1999416757

What OpenQuestion holds

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LicenceCC BY
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.