Abstract

Human serum albumin modified with 1–2 methylglyoxal residues per molecule of protein (MG min-HSA) stimulated the synthesis and secretion of interleukin 1β (IL-1β) from human monocytic THP-1 cells in vitro. It was a more potent inducer of IL-1β synthesis than human serum albumin highly-modified with glucose-derived advanced glycation endproducts (AGE-HSA). With 20 μM ligand, IL-1β synthesis was (pg/10 6 cells): MG min-HSA 484.5 ± 50.3; AGE-HSA 30.6 ± 2.0 ( n = 3). IL-1β synthesis increased markedly with MG min-HSA concentrations > 5 μM. IL-1β synthesis and secretion from monocytes in response to methylglyoxal-modifed proteins in vivo may contribute to the development of macro- and micro-angiopathy, particularly in diabetes mellitus.

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