Evidence map›Paper›PMID 25659933›Full record

ArticleFree radical biology & medicine2015

Novel insights in mammalian catalase heme maturation: effect of NO and thioredoxin-1.

Ritu Chakravarti, Karishma Gupta, Alana Majors, Lisa Ruple, Mark Aronica, Dennis J Stuehr

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In one paragraph

Article in Free radical biology & medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Targeting catalase in cancer.Redox biology · 2024
    Review
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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

6 authors at 2 institutions in 1 country.

Ritu ChakravartiDepartment of Pathobiology, Lerner Research Institute, 9500 Euclid Avenue, Cleveland Clinic, Cleveland, OH 44195, USA.
Karishma GuptaSchool of Medicine, Case Western Reserve University, Cleveland, OH 44195, USA.
Alana MajorsDepartment of Pathobiology, Lerner Research Institute, 9500 Euclid Avenue, Cleveland Clinic, Cleveland, OH 44195, USA.
Lisa RupleDepartment of Pathobiology, Lerner Research Institute, 9500 Euclid Avenue, Cleveland Clinic, Cleveland, OH 44195, USA.
Mark AronicaDepartment of Pathobiology, Lerner Research Institute, 9500 Euclid Avenue, Cleveland Clinic, Cleveland, OH 44195, USA.
Dennis J StuehrDepartment of Pathobiology, Lerner Research Institute, 9500 Euclid Avenue, Cleveland Clinic, Cleveland, OH 44195, USA. Electronic address: stuehrd@ccf.org.
Cleveland Clinic Lerner College of Medicine · USCase Western Reserve University · US

Funding

Structural Determinants Of Ceruloplasmin Inflammatory ActivityP01HL076491 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI PLOW, EDWARD FRANKLIN · 2004 to 2019
$27.3M
Targeting pathological hyaluronan matricesP01HL103453 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI REIZES, OFER · 2011 to 2020
$26.8M
New mechanism and regulation of intracellular heme delivery in mammalsR01GM097041 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI STUEHR, DENNIS J · 2011 to 2014
$1.2M
NHLBI NIH HHS HL076491NHLBI NIH HHS P01 HL076491NHLBI NIH HHS P01 HL103453NIGMS NIH HHS GM097041NIGMS NIH HHS R01 GM097041
6 · The paper itself

Abstract

Catalase is a tetrameric heme-containing enzyme with essential antioxidant functions in biology. Multiple factors including nitric oxide (NO) have been shown to attenuate its activity. However, the possible impact of NO in relation to the maturation of active catalase, including its heme acquisition and tetramer formation, has not been investigated. We found that NO attenuates heme insertion into catalase in both short-term and long-term incubations. The NO inhibition in catalase heme incorporation was associated with defective oligomerization of catalase, such that inactive catalase monomers and dimers accumulated in place of the mature tetrameric enzyme. We also found that GAPDH plays a key role in mediating these NO effects on the structure and activity of catalase. Moreover, the NO sensitivity of catalase maturation could be altered up or down by manipulating the cellular expression level or activity of thioredoxin-1, a known protein-SNO denitrosylase enzyme. In a mouse model of allergic inflammatory asthma, we found that lungs from allergen-challenged mice contained a greater percentage of dimeric catalase relative to tetrameric catalase in the unchallenged control, suggesting that the mechanisms described here are in play in the allergic asthma model. Together, our study shows how maturation of active catalase can be influenced by NO, S-nitrosylated GAPDH, and thioredoxin-1, and how maturation may become compromised in inflammatory conditions such as asthma.

Indexed as

AnimalsAntioxidantsAsthmaCatalaseCell LineDisease Models, AnimalGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)HEK293 CellsHemeHumansLungMiceMice, Inbred BALB CMyocytes, Smooth MuscleNitric OxideOvalbuminAntioxidantsCatalaseGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)HemeNitric OxideOvalbuminThioredoxinsAsthmaCatalaseHemeNitric oxideOligomerizationS-nitrosylated GAPDHThioredoxin-1

Identifiers

PMID25659933
PMCPMC5030845
OpenAlexW2113593409

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Registered trials

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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.