Glycation of the Major Milk Allergen β‐Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Peruško, Marija; Roest, Manon van; Stanić-Vučinić, Dragana; Simons, Peter J.; Pieters, Raymond; Veličković, Tanja Ćirković; Smit, Joost J.

doi:10.1002/mnfr.201800341

Cited by 51 publications

(60 citation statements)

References 51 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In parallel, the uptake of pyrraline‐Ova in CDs was reduced by SR‐A inhibitors, suggesting that pyrraline specifically interacted with SR‐A (Heilmann et al., 2014). Similarly, the glycated β‐lactoglobulin (major milk allergen) showed higher uptake and faster degradation in DCs, while a higher inflammatory cytokine production was not observed (Perusko et al., 2018).…”

Section: Do Dages Correlate With Food Allergy?mentioning

confidence: 99%

Dietary advanced glycation end‐products: Perspectives linking food processing with health implications

Zhang

2020

Comp Rev Food Sci Food Safe

144

116

View full text Add to dashboard Cite

Dietary advanced glycation end products (dAGEs) are complex and heterogeneous compounds derived from nonenzymatic glycation reactions during industrial processing and home cooking. There is mounting evidence showing that dAGEs are closely associated with various chronic diseases, where the absorbed dAGEs fuel the biological AGEs pool to exhibit noxious effects on human health. Currently, due to the uncertain bioavailability and rapid renal clearance of dAGEs, the relationship between dAGEs and biological AGEs remains debatable. In this review, we provide the most updated information on dAGEs including their generation in processed foods, analytical and characterization techniques, metabolic fates, interaction with AGE receptors, implications on human health and reducing strategies. Available evidence demonstrating a relevance between dAGEs and food allergy is also included. AGEs are ubiquitous in foods and their contents largely depend on the reactivity of carbonyl and amino groups, along with surrounding condition mainly pH and heating procedures. Once being digested and absorbed into the circulation, two separate pathways can be involved in the deleterious effects of dAGEs: an AGE receptor‐dependent way to stimulate cell signals, and an AGE receptor‐independent way to dysregulate proteins via forming complexes. Inhibition of AGEs formation during food processing and reduction in the diet are two potent approaches to restrict health‐hazardous dAGEs. To elucidate the biological role of dAGEs toward human health, the following significant perspectives are raised: molecular size and complexity of dAGEs; interactions between unabsorbed dAGEs and gut microbiota; and roles played by concomitant compounds in the heat‐processed foods.

show abstract

Section: Do Dages Correlate With Food Allergy?mentioning

confidence: 99%

Dietary advanced glycation end‐products: Perspectives linking food processing with health implications

Zhang

2020

Comp Rev Food Sci Food Safe

144

116

View full text Add to dashboard Cite

show abstract

“…However, in this study BLG was heated in solution with glucose for 10 days at 60 437˚C, similar to our wet-heating process. This makes it likely that also in their samples, physicochemical changes such as increased hydrophobicity, rather than glycation, led to a lowered cytokine response [39]. Increased hydrophobicity of our BLG samples did not induce clear immunological responses but rather lowered these.…”

Section: Discussionmentioning

confidence: 83%

“…High-temperature dry-heated BLG, which had a high degree of glycation, bound to all receptors to a higher extent than wet-heated BLG, but its uptake was not significantly reduced when clathrin-dependent uptake was blocked. In another study, the uptake of BLG that had been heated in solution at 60 °C for 10 days with glucose by dendritic cells was reported to be RAGE independent but scavenger receptor dependent [39]. Scavenger receptor A was reported to be involved in the uptake of glycated ovalbumin by macrophages [40], which could thus be a potential target for future discrimination.…”

Section: Discussionmentioning

confidence: 99%

Hydrophobicity drives receptor-mediated uptake of heat-processed proteins by THP-1 macrophages and dendritic cells, but not cytokine responses

Deng

Govers

Teodorowicz

et al. 2020

Preprint

View full text Add to dashboard Cite

AbstractImpact of processing on immunogenicity of food proteins has clearly been demonstrated, but the underlying mechanisms are still unclear. In our previous study, the uptake of the cow’s milk protein β-lactoglobulin (BLG) by THP-1 macrophages varied after applying different processing methods and was positively correlated with hydrophobicity and aggregation. Here we applied the same 3 processing methods: wet heating (60 °C) and low- or high-temperature (50 °C or 130 °C, respectively) dry heating in absence or presence of reducing sugars (i.e. glucose, lactose or galacto-oligosaccharide) to lysozyme and thyroglobulin, which have different pI or molecular weight compared to BLG, respectively. Uptake of the soluble fraction was tested in two types of, genetically homogeneous, antigen-presenting cells (macrophages and dendritic cells derived from THP-1 monocytes). This revealed a strong correlation between the uptake of the different protein samples by macrophages and dendritic cells, and confirmed the key role of hydrophobicity, over aggregation, in determining the uptake. Several uptake routes were shown to contribute to the uptake of BLG by macrophages. However, cytokine responses following exposure of macrophages to BLG samples were not related to the levels of uptake. Heat-treatment-mediated increases in uptake did thus not induce a response in our read-out systems. Together, our results demonstrate that heat-treatment-induced increased hydrophobicity is the prime driving factor in uptake, but not in cytokine production, by THP-1 macrophages.

show abstract

“…However, in this study BLG was heated in solution with glucose for 10 days at 60˚C, similar to our wet-heating process. This makes it likely that also in their samples, physicochemical changes such as increased hydrophobicity, rather than glycation, led to a lowered cytokine response [41]. Increased hydrophobicity of our BLG samples did not induce clear immunological responses but rather lowered these.…”

Section: Plos Onementioning

confidence: 83%

Hydrophobicity drives receptor-mediated uptake of heat-processed proteins by THP-1 macrophages and dendritic cells, but not cytokine responses

et al. 2020

View full text Add to dashboard Cite

Although an impact of processing on immunogenicity of food proteins has clearly been demonstrated, the underlying mechanisms are still unclear. We applied 3 different processing methods: wet heating (60˚C) and low-or high-temperature (50˚C or 130˚C, respectively) dry-heating in absence or presence of reducing sugars, to β-lactoglobulin (BLG), lysozyme and thyroglobulin, which represent dietary proteins with different pI or molecular weight. Uptake of the soluble fraction of the samples was tested in two types of, genetically homogeneous, antigen-presenting cells (macrophages and dendritic cells derived from THP-1 monocytes). This revealed a strong correlation between the uptake of the different protein samples by macrophages and dendritic cells, and confirmed the key role of hydrophobicity, over aggregation, in determining the uptake. Several uptake routes were shown to contribute to the uptake of BLG by macrophages. However, cytokine responses following exposure of macrophages to BLG samples were not related to the levels of uptake. Together, our results demonstrate that heat-treatment-induced increased hydrophobicity is the prime driving factor in uptake, but not in cytokine production, by THP-1 macrophages.

show abstract

Glycation of the Major Milk Allergen β‐Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Cited by 51 publications

References 51 publications

Dietary advanced glycation end‐products: Perspectives linking food processing with health implications

Dietary advanced glycation end‐products: Perspectives linking food processing with health implications

Hydrophobicity drives receptor-mediated uptake of heat-processed proteins by THP-1 macrophages and dendritic cells, but not cytokine responses

Hydrophobicity drives receptor-mediated uptake of heat-processed proteins by THP-1 macrophages and dendritic cells, but not cytokine responses

Contact Info

Product

Resources

About