The Soluble Form of the Cellular Prion Protein Enhances Phagocytic Activity and Cytokine Production by Human Monocytes Via Activation of ERK and NF-kappaB
Immune Network
;
: 148-156, 2013.
Article
in English
| WPRIM
| ID: wpr-77566
ABSTRACT
The PrP(C) is expressed in many types of immune cells including monocytes and macrophages, however, its function in immune regulation remains to be elucidated. In the present study, we examined a role for PrP(C) in regulation of monocyte function. Specifically, the effect of a soluble form of PrP(C) was studied in human monocytes. A recombinant fusion protein of soluble human PrP(C) fused with the Fc portion of human IgG1 (designated as soluble PrP(C)-Fc) bound to the cell surface of monocytes, induced differentiation to macrophage-like cells, and enhanced adherence and phagocytic activity. In addition, soluble PrP(C)-Fc stimulated monocytes to produce pro-inflammatory cytokines such as TNF-alpha, IL-1beta, and IL-6. Both ERK and NF-kappaB signaling pathways were activated in soluble PrP(C)-treated monocytes, and inhibitors of either pathway abrogated monocyte adherence and cytokine production. Taken together, we conclude that soluble PrP(C)-Fc enhanced adherence, phagocytosis, and cytokine production of monocytes via activation of the ERK and NF-kappaB signaling pathways.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Phagocytosis
/
Immunoglobulin G
/
Monocytes
/
Cytokines
/
NF-kappa B
/
Interleukin-6
/
Tumor Necrosis Factor-alpha
/
Macrophages
Limits:
Humans
Language:
English
Journal:
Immune Network
Year:
2013
Type:
Article
Similar
MEDLINE
...
LILACS
LIS