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.
Highlights
In the past 30 years the consumption of ultra-processed foods has almost tripled from11% to 32% of daily energy intake, with this increased consumption of ultra-processed food being associated with a higher risk of increased mortality from numerous kinds of noncommunicable diseases [1]
This review provides a comprehensive summary of the literature focusing on dietary advanced glycation end-products (AGEs) and how they exert their immunomodulatory effects via specific receptors on cells of the immune system
The evidence reviewed above shows that dietary AGEs (dAGEs) may act as molecules that can modulate innate and adaptative immunity, and contribute to low-grade inflammation, food allergies and non-communicable diseases. dAGEs may influence the activation of the immune system in two different manners—firstly, via the interaction with receptor for advanced glycation end products (RAGE) which does not lead to the internalization of the ligand [72] but does activate pro-inflammatory pathways as described for endogenous AGEs [113]
Summary
In the past 30 years the consumption of ultra-processed foods has almost tripled from. 11% to 32% of daily energy intake, with this increased consumption of ultra-processed food being associated with a higher risk of increased mortality from numerous kinds of noncommunicable diseases [1] This diet pattern, mainly associated with Western countries, has a led to increased exposure to advanced glycation end-products (AGEs). The MR occurs when proteins are heated in the presence of reducing sugars, e.g., during the thermal processing of food, plus it is often used in the food industry since it generates taste, color, and aroma It causes a number of modifications on the level of the protein structure [5]. The type of AGE produced highly depends on the type of sugar used in the reaction and on the processing conditions, such as temperature, time of heating, pH, and water activity, plus AGEs are bound to proteins with high contents of lysine and arginine units [25]. The MR has been described to have an effect on the digestibility, immunogenicity and allergenicity of food proteins; monitoring its impact on health and its use in the food industry is of great importance for the general public [16,26]
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.