Evidence map›Paper›PMID 29920341›Full record

ArticleFree radical biology & medicine2018

High- and low-affinity PEGylated hemoglobin-based oxygen carriers: Differential oxidative stress in a Guinea pig transfusion model.

Esra'a Alomari, Luca Ronda, Stefano Bruno, Gianluca Paredi, Marialaura Marchetti, Stefano Bettati, Davide Olivari, Francesca Fumagalli, Deborah Novelli, Giuseppe Ristagno and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Free radical biology & medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

4 citing papers in PubMed, 14 citations in OpenAlex.

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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

14 authors at 4 institutions in 3 countries.

Esra'a AlomariDepartment of Food and Drug, University of Parma, Parma, Italy.
Luca RondaDepartment of Medicine and Surgery, University of Parma, Parma, Italy; Biopharmanet-TEC, University of Parma, Parma, Italy.
Stefano BrunoDepartment of Food and Drug, University of Parma, Parma, Italy; Biopharmanet-TEC, University of Parma, Parma, Italy. Electronic address: stefano.bruno@unipr.it.
Gianluca ParediDepartment of Food and Drug, University of Parma, Parma, Italy; Interdepartmental Center SITEIA.PARMA, University of Parma, Parma 43121, Italy.
Marialaura MarchettiDepartment of Medicine and Surgery, University of Parma, Parma, Italy; Biopharmanet-TEC, University of Parma, Parma, Italy.
Stefano BettatiDepartment of Medicine and Surgery, University of Parma, Parma, Italy; Biopharmanet-TEC, University of Parma, Parma, Italy; Istituto Nazionale Biostrutture e Biosistemi, Rome, Italy.
Davide OlivariIstituto di Ricerche Farmacologiche 'Mario Negri', Milan, Italy.
Francesca FumagalliIstituto di Ricerche Farmacologiche 'Mario Negri', Milan, Italy.
Deborah NovelliIstituto di Ricerche Farmacologiche 'Mario Negri', Milan, Italy.
Giuseppe RistagnoIstituto di Ricerche Farmacologiche 'Mario Negri', Milan, Italy.
Roberto LatiniIstituto di Ricerche Farmacologiche 'Mario Negri', Milan, Italy.
Chris E CooperSchool of Biological Sciences, University of Essex, Colchester, United Kingdom.
Brandon J ReederSchool of Biological Sciences, University of Essex, Colchester, United Kingdom.
Andrea MozzarelliDepartment of Food and Drug, University of Parma, Parma, Italy; Biopharmanet-TEC, University of Parma, Parma, Italy; Istituto Nazionale Biostrutture e Biosistemi, Rome, Italy; Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Pisa, Italy.
Mario Negri Institute for Pharmacological Research · ITUniversity of Parma · ITIstituto Nazionale Biostrutture e Biosistemi · ITUniversity of Essex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L004232/1Medical Research Council MR/L01310X/1
6 · The paper itself

Abstract

Hemoglobin-based oxygen carriers (HBOCs) are an investigational replacement for blood transfusions and are known to cause oxidative damage to tissues. To investigate the correlation between their oxygen binding properties and these detrimental effects, we investigated two PEGylated HBOCs endowed with different oxygen binding properties - but otherwise chemically identical - in a Guinea pig transfusion model. Plasma samples were analyzed for biochemical markers of inflammation, tissue damage and organ dysfunction; proteins and lipids of heart and kidney extracts were analyzed for markers of oxidative damage. Overall, both HBOCs produced higher oxidative stress in comparison to an auto-transfusion control group. Particularly, tissue 4-hydroxynonenal adducts, tissue malondialdehyde adducts and plasma 8-oxo-2'-deoxyguanosine exhibited significantly higher levels in comparison with the control group. For malondialdehyde adducts, a higher level in the renal tissue was observed for animals treated with the high-affinity HBOC, hinting at a correlation between the HBOCs oxygen binding properties and the oxidative stress they produce. Moreover, we found that the high-affinity HBOC produced greater tissue oxygenation in comparison with the low affinity one, possibly correlating with the higher oxidative stress it induced.

Indexed as

AnimalsBlood SubstitutesGuinea PigsHumansModels, AnimalOxidative StressBlood Substitutes4-hydroxynonenal8-oxo-2'-deoxyguanosineBlood substitutesHemoglobin-based oxygen carriersMalondialdehydeOxidative stressOxygen affinity

Identifiers

PMID29920341
PMCPMC6191936
OpenAlexW2809364991

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.