ArticleMolecular and cellular biochemistry2012
Characterization of antioxidant and anti-inflammatory activities of bioactive fractions recovered from a glucose-lysine Maillard reaction model system.
Article in Molecular and cellular biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 23 citations in OpenAlex.
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- Glycosylation of Zein Hydrolysate as a Nanocarrier for Lutein Delivery: Preparation and Stability.Frontiers in pharmacology · 2022Article
- Antioxidant and Functional Activities of MRPs Derived from Different Sugar-Amino Acid Combinations and Reaction Conditions.Antioxidants (Basel, Switzerland) · 2021Article
- Oxidative Quality of Dairy Powders: Influencing Factors and Analysis.Foods (Basel, Switzerland) · 2021Review
- Characterization of macrophage stimulating compound in glycated whey protein concentrate.Food science and biotechnology · 2020Article
- The Upregulation of Trophinin-Associated Protein (TROAP) Predicts a Poor Prognosis in Hepatocellular Carcinoma.Journal of Cancer · 2019Article
- Effect of Temperature on Flavor Compounds and Sensory Characteristics of Maillard Reaction Products Derived from Mushroom Hydrolysate.Molecules (Basel, Switzerland) · 2018Article
- Evidence for inhibition of nitric oxide and inducible nitric oxide synthase in Caco-2 and RAW 264.7 cells by a Maillard reaction product [5-(5,6-dihydro-4H-pyridin-3-ylidenemethyl)furan-2-yl]-methanol.Molecular and cellular biochemistry · 2015Article
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2 authors at 1 institution in 1 country.
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Abstract
A glucose-lysine (Glu-Lys) Maillard reaction mixture heated at 121°C for 60 min was processed by ultrafiltration, ethyl acetate extraction, and semi-preparative HPLC to recover a bioactive fraction, termed F3. F3, characterized by spectral analysis to contain three distinct components, inhibited NO and IL-8 by 70 and 61%, respectively, at a concentration of 50 μg/ml in inflamed Caco-2 cells induced by IFN-γ and phorbol 12-myristate 13-acetate (PMA). F3 significantly (P < 0.05) down-regulated several genes involved in nuclear factor kappa B (NF-κB) signaling pathway. These genes included the cytokine receptors, TNFRSF10A and TNFRSF10B; receptor-associated proteins, IRAK2 and TICAM1; the inhibitor κB kinase, IKBKE; the NF-κB inhibitor, NFKBIA; and the NF-κB subunits, REL, RELA, and RELB. F3 also down-regulated the NF-κB responsive genes IL-8, NOS2, and ICAM1, attenuated the gene expression of peroxidases such as DUOX1 and DUOX2, and relieved the down-regulated GCFHR that are involved in the biosynthesis of NO and TROAP, a gene suppressed by NO. The anti-inflammatory activity of F3 was mediated through multiple processes that included regulation of gene expressions involved in NF-κB signaling, the inhibition of IL-8 and iNOS translation, a decrease in NO synthesis and attenuating oxidative stress in inflamed Caco-2 cells. Our results show that MRP components have the potential to suppress inflammation in IFN-γ and PMA-induced Caco-2 cells.
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