Evidence map›Paper›PMID 35057553›Full record

ReviewNutrients2022

Receptor Mediated Effects of Advanced Glycation End Products (AGEs) on Innate and Adaptative Immunity: Relevance for Food Allergy.

Daniela Briceno Noriega, Hannah E Zenker, Cresci-Anne Croes, Arifa Ewaz, Janneke Ruinemans-Koerts, Huub F J Savelkoul, R J Joost van Neerven, Malgorzata Teodorowicz

Open access · goldAbstract readReview
In one paragraph

Review in Nutrients, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 49 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

8 authors at 3 institutions in 2 countries.

Daniela Briceno NoriegaCell Biology and Immunology, Wageningen University and Research Centre, De Elst 1, 6708 WD Wageningen, The Netherlands.ORCID 0000-0002-4909-2976
Hannah E ZenkerFood Chemistry, Department of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg (FAU), 91054 Erlangen, Germany.ORCID 0000-0002-0396-4425
Cresci-Anne CroesCell Biology and Immunology, Wageningen University and Research Centre, De Elst 1, 6708 WD Wageningen, The Netherlands.ORCID 0000-0002-9837-9922
Arifa EwazCell Biology and Immunology, Wageningen University and Research Centre, De Elst 1, 6708 WD Wageningen, The Netherlands.
Janneke Ruinemans-KoertsCell Biology and Immunology, Wageningen University and Research Centre, De Elst 1, 6708 WD Wageningen, The Netherlands.
Huub F J SavelkoulCell Biology and Immunology, Wageningen University and Research Centre, De Elst 1, 6708 WD Wageningen, The Netherlands.ORCID 0000-0001-6236-7092
R J Joost van NeervenCell Biology and Immunology, Wageningen University and Research Centre, De Elst 1, 6708 WD Wageningen, The Netherlands.ORCID 0000-0002-3991-5297
Malgorzata TeodorowiczCell Biology and Immunology, Wageningen University and Research Centre, De Elst 1, 6708 WD Wageningen, The Netherlands.
Wageningen University & Research · NLFriedrich-Alexander-Universität Erlangen-Nürnberg · DERijnstate Hospital · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As of late, evidence has been emerging that the Maillard reaction (MR, also referred to as glycation) affects the structure and function of food proteins. MR induces the conformational and chemical modification of food proteins, not only on the level of IgG/IgE recognition, but also by increasing the interaction and recognition of these modified proteins by antigen-presenting cells (APCs). This affects their biological properties, including digestibility, bioavailability, immunogenicity, and ultimately their allergenicity. APCs possess various receptors that recognize glycation structures, which include receptor for advanced glycation end products (RAGE), scavenger receptors (SRs), galectin-3 and CD36. Through these receptors, glycation structures may influence the recognition, uptake and antigen-processing of food allergens by dendritic cells (DCs) and monocytes. This may lead to enhanced cytokine production and maturation of DCs, and may also induce adaptive immune responses to the antigens/allergens as a result of antigen uptake, processing and presentation to T cells. Here, we aim to review the current literature on the immunogenicity of AGEs originating from food (exogenous or dietary AGEs) in relation to AGEs that are formed within the body (endogenous AGEs), their interactions with receptors present on immune cells, and their effects on the activation of the innate as well as the adaptive immune system. Finally, we review the clinical relevance of AGEs in food allergies.

Indexed as

Adaptive ImmunityImmunity, InnateAllergensAntigen PresentationAntigen-Presenting CellsDendritic CellsDietFoodFood HypersensitivityGlycation End Products, AdvancedHumansMaillard ReactionReceptor for Advanced Glycation End ProductsT-LymphocytesAllergensGlycation End Products, AdvancedReceptor for Advanced Glycation End Productsadaptative immunityadvanced glycation end products (AGEs)AGE receptorsdAGEs(food) allergyglycationimmunogenicityinnate immunityRAGE

Identifiers

PMID35057553
PMCPMC8778532
OpenAlexW4205695139

What OpenQuestion holds

Textmetadata
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.