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Front Cover: Methylglyoxal‐Lysine Dimer, an Advanced Glycation End Product, Induces Inflammation via Interaction with RAGE in Mesangial Cells
Author(s) -
Lee HeeWeon,
Gu Min Ji,
Lee JeeYoung,
Lee Seungju,
Kim Yoonsook,
Ha Sang Keun
Publication year - 2021
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.202170031
Subject(s) - methylglyoxal , glycation , advanced glycation end product , mesangial cell , rage (emotion) , chemistry , reactive oxygen species , lysine , lactoylglutathione lyase , inflammation , biochemistry , receptor , microbiology and biotechnology , immunology , biology , amino acid , enzyme , neuroscience , in vitro
Mol. Nutr. Food Res . 2021, 65 , 2000799 DOI: 10.1002/mnfr.202000799 Methylglyoxal‐lysine dimer, a typical advanced glycation end product, contributes to inflammatory responses during renal disorder. The interaction of Methylglyoxal‐lysine dimer (MOLD) and receptor of advanced glycation end products (RAGE) causes reactive oxygen species (ROS) production and mitochondrial dysfunction in mesangial cells. Further, the NF‐kB and PI3K/AKT signaling pathways triggered by ROS exacerbate the inflammatory responses in MOLD‐induced renal damages. This is reported by Sang Keun Ha and co‐workes in article number 2000799.
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