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Abstract
Interleukin (IL)-6 secretion from macrophage cells is known to be induced by toll-like
receptor (TLR) 9 ligands, CpG (microbial DNA sequences containing unmethylated CpG
dinucleotides). We have found, using macrophage-like J774.1 cells, that this induction
was dramatically suppressed by a disaccharide derived from chondroitin sulfate A (Di-4S),
but not by chondroitin sulfate A (CS-A) itself. The suppression of IL-6 secretion
by Di-4S occurred at protein and mRNA expression levels. Di-4S inhibited the degradation
of interleukin-1 receptor-associated kinase 1 (IRAK1) in the signaling pathway mediated
by myeloid differentiation primary response gene (88) (MyD88) when stimulated by TLR9
activation. In addition to suppressing IRAK1 activation, interference with CpG-TLR9
interaction by Di-4S is also suggested to be one of the mechanisms. Oligosaccharides
derived from chondroitin sulfates would be effective suppressing agents for the TLR9-mediated
inflammation reaction.