Hydrophobicity and aggregation, but not glycation, are key determinants for uptake of thermally processed β-lactoglobulin by THP-1 macrophages

Deng, Ying; Govers, Coen; Bastiaan‐Net, Shanna; Hulst, Nina van der; Hettinga, Kasper; Wichers, Harry J.

doi:10.1016/j.foodres.2019.01.038

Cited by 21 publications

(55 citation statements)

References 53 publications

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“…Besides this solution without saccharides, D-glucose (glu), D-lactose (lac), and galacto-oligosaccharide (GOS; Royal FrieslandCampina, Wageningen, the Netherlands) were added to reach a final 1:4 molar ratio of total free amino groups to saccharide reducing ends. Identical heating methods, being high-temperature dry-heating (H), wet-heating (W) and low-temperature dryheating (L), sample preparation and naming were applied to the proteins as indicated in a previous study [3]. Fluorescein isothiocyanate isomer I (FITC) labelling was performed as described previously [3].…”

Section: Sample Preparation and Fluorescent Labellingmentioning

confidence: 99%

“…Identical heating methods, being high-temperature dry-heating (H), wet-heating (W) and low-temperature dryheating (L), sample preparation and naming were applied to the proteins as indicated in a previous study [3]. Fluorescein isothiocyanate isomer I (FITC) labelling was performed as described previously [3].…”

Section: Sample Preparation and Fluorescent Labellingmentioning

confidence: 99%

“…The analysis of solubility (protein mass remaining in solution), loss of amino group (OPA method), AGE formation (fluorescent measurement), exposure of hydrophobicity region (ANS method), surface charge (zeta-potential measurement), secondary structure (circular dichroism measurement) and aggregation (size exclusion chromatography) were performed using the protocols as described previously [3].…”

Section: Physicochemical Analysismentioning

confidence: 99%

“…Uptake experiments were performed as described previously [3]. No significant difference of absolute uptake value has been found for native BLG, thyroglobulin or lysozyme in macrophages or dendritic cells ( S1 Fig).…”

Section: Uptake and Blocking Of Different Uptake Routesmentioning

confidence: 99%

“…In an earlier study on β-lactoglobulin (BLG), the major whey protein of milk [3], we observed that heat processing under different conditions altered the physicochemical properties and its uptake by THP-1 macrophages. In particular, heating in solution at 60 °C for 3 days introduced changes in hydrophobicity and molecular weight, which were shown to be the key determinants for uptake.…”

Section: Introductionmentioning

confidence: 99%

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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

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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.

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Section: Sample Preparation and Fluorescent Labellingmentioning

confidence: 99%

Section: Sample Preparation and Fluorescent Labellingmentioning

confidence: 99%

Section: Physicochemical Analysismentioning

confidence: 99%

Section: Uptake and Blocking Of Different Uptake Routesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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

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Enhanced Uptake of Processed Bovine β‐Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity

Teodorowicz

Zenker

Ewaz

et al. 2021

Molecular Nutrition Food Res

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Scope: -lactoglobulin (BLG) is a major cow milk allergen encountered by the immune system of infants fed with milk-based formulas. To determine the effect of processing on immunogenicity of BLG, this article characterized how heated and glycated BLG are recognized and internalized by APCs. Also, the effect of heat-induced structural changes as well as gastrointestinal digestion on immunogenicity of BLG is evaluated. Methods and results: The binding and uptake of BLG from raw cow milk and heated either alone (BLG-H) or with lactose/glucose (BLG-Lac and BLG-Glu) to the receptors present on APCs are analyzed by ELISA and cell-binding assays. Heated and glycated BLG is internalized via galectin-3 (Gal-3)and scavenger receptors (CD36 and SR-AI) while binding to the receptor for advanced glycation end products (R AGE) does not cause internalization. Receptor affinity of BLG is dependent on increased hydrophobicity, -sheet exposure and aggregation. Digested glycated BLG maintained binding to sRAGE and Gal-3 but not to CD36 and SR-AI, and is detected on the surface of APCs. This suggests a mechanism via which digested glycated BLG may trigger innate (via RAGE) and adaptive immunity (via Gal-3). Conclusions: This study defines structural characteristics of heated and glycated BLG determining its interaction with APCs via specific receptors thus revealing enhanced immunogenicity of glycated versus heated BLG.

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Revealing the Potential of Theaflavin to Reduce Egg Allergenicity at the Molecular Level: A Study of the Binding Affinity of Theaflavin to Egg White Lysozyme

Li,

et al. 2023

Food Bioprocess Technol

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Hydrophobicity and aggregation, but not glycation, are key determinants for uptake of thermally processed β-lactoglobulin by THP-1 macrophages

Cited by 21 publications

References 53 publications

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

Enhanced Uptake of Processed Bovine β‐Lactoglobulin by Antigen Presenting Cells: Identification of Receptors and Implications for Allergenicity

Revealing the Potential of Theaflavin to Reduce Egg Allergenicity at the Molecular Level: A Study of the Binding Affinity of Theaflavin to Egg White Lysozyme

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