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