LPS suppresses expression of asialoglycoprotein-binding protein through TLR4 in thioglycolate-elicited peritoneal macrophages |
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Authors: | Bruce Yong Ma Mio Kaihama Motohiro Nonaka Shogo Oka Nobuko Kawasaki Toshisuke Kawasaki |
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Affiliation: | (1) Research Center for Glycobiotechnology, Ritsumeikan University, Shiga 525-8577, Japan;(2) Department of Biological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan;(3) School of Health Sciences, Faculty of Medicine, Kyoto University, Kyoto 606-8501, Japan |
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Abstract: | Macrophages are known to express various types of endocytosis receptors that mediate the removal of foreign pathogens. Macrophage asialoglycoprotein-binding protein (M-ASGP-BP) is a Gal/GalNAc-specific lectin, which functions as an endocytosis receptor. We found here that LPS is able to down-regulate the mRNA expression of M-ASGP-BP in a time-dependent manner using thioglycolate-elicited rat and mouse peritoneal macrophages. However, LPS does not modulate the mRNA expression of M-ASGP-BP from macrophages of C3H/HeN mice, which have a point mutation of TLR4, the primary LPS receptor. Furthermore, an inhibitor of NF-κB was observed to efficiently block the suppressive effect of LPS on M-ASGP-BP as well as to inhibit the phosphorylated IκB. These results demonstrate that the mRNA expression of M-ASGP-BP is down-regulated by the LPS-mediated TLR4 pathway involving NF-κB activation, suggesting that engagement of M-ASGP-BP by LPS may yield a negative signal that interferes with the LPS-induced positive signals mediated by proinflammatory cytokines. |
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Keywords: | Macrophage asialoglycoprotein-binding protein C-type lectin LPS TLR4 NF-κ B |
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