Escherichia coli Maltose-Binding Protein Induces M1 Polarity of RAW264.7 Macrophage Cells via a TLR2- and TLR4-Dependent Manner

Autor: Fang Wang, Wan Wang, Weihua Ni, Guomu Liu, Hongyan Yuan, Guixiang Tai
Jazyk: angličtina
Rok vydání: 2015
Předmět:
Cell Survival
MAP Kinase Signaling System
toll-like receptor 4
Nitric Oxide Synthase Type II
Nitric Oxide
p38 Mitogen-Activated Protein Kinases
Catalysis
Article
lcsh:Chemistry
Inorganic Chemistry
Maltose-binding protein
Mice
Immune system
toll-like receptor 2
Animals
Physical and Theoretical Chemistry
lcsh:QH301-705.5
Molecular Biology
Spectroscopy
Maltodextrin transport
biology
Escherichia coli Proteins
Macrophages
Organic Chemistry
Histocompatibility Antigens Class I
NF-kappa B
Cell Polarity
General Medicine
Molecular biology
Computer Science Applications
Up-Regulation
Nitric oxide synthase
TLR2
RAW 264.7 Cells
lcsh:Biology (General)
lcsh:QD1-999
maltose-binding protein
Periplasmic Binding Proteins
biology.protein
classically activated macrophages
Phosphorylation
Cytokines
Pinocytosis
Inflammation Mediators
Cell activation
CD80
Biomarkers
Zdroj: International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 16, Iss 5, Pp 9896-9909 (2015)
Volume 16
Issue 5
Pages 9896-9909
ISSN: 1422-0067
Popis: Maltose-binding protein (MBP) is a critical player of the maltose/maltodextrin transport system in Escherichia coli. Our previous studies have revealed that MBP nonspecifically induces T helper type 1 (Th1) cell activation and activates peritoneal macrophages obtained from mouse. In the present study, we reported a direct stimulatory effect of MBP on RAW264.7 cells, a murine macrophage cell line. When stimulated with MBP, the production of nitric oxide (NO), IL-1β, IL-6 and IL-12p70, and the expressions of CD80, MHC class II and inducible nitric oxide synthase (iNOS) were all increased in RAW264.7 cells, indicating the activation and polarization of RAW264.7 cells into M1 macrophages induced by MBP. Further study showed that MBP stimulation upregulated the expression of TLR2 and TLR4 on RAW264.7 cells, which was accompanied by subsequent phosphorylation of IκB-α and p38 MAPK. Pretreatment with anti-TLR2 or anti-TLR4 antibodies largely inhibited the phosphorylation of IκB-α and p38 MAPK, and greatly reduced MBP-induced NO and IL-12p70 production, suggesting that the MBP-induced macrophage activation and polarization were mediated by TLR2 and TLR4 signaling pathways. The observed results were independent of lipopolysaccharide contamination. Our study provides a new insight into a mechanism by which MBP enhances immune responses and warrants the potential application of MBP as an immune adjuvant in immune therapies.
Databáze: OpenAIRE