Monitoring Cellular Trafficking of Nanoparticle Cargo in Murine Macrophages Through Plasmon Coupling Microscopy

2013 ◽  
Author(s):  
Björn M. Reinhard ◽  
Hongyun Wang ◽  
Linxi Wu
Keyword(s):  
Phenotypic Variability ◽  
Resonance Wavelength ◽  
Plasmon Coupling ◽  
Single Cell Level ◽  
Murine Macrophage ◽  
Macrophage Cell Line ◽  
Macrophage Cell ◽  
Cell Level ◽  
Inhibition Studies ◽  
Endocytosis Mechanisms

A detailed analysis of silver nanoparticle (NP) uptake and trafficking in the murine macrophage cell line J774A.1 through spectral analysis of the resonance wavelength of the metal NP cargo is presented. The NP spectra reveal a strong phenotypic variability in the NP uptake and processing on the single cell level. Cells containing non- or low-agglomerated NPs are found to coexist with cells containing NPs of varying degrees of NP agglomeration, clearly indicated by a spectral red-shift in the resonance wavelength. Pharmacological inhibition studies indicate that the observed differences in the intracellular NP organization result from coexisting actin- and clathrin-dependent endocytosis mechanisms. Correlation with fluorescence macrophage maturity markers shows that differentiated J774A.1 macrophages preferentially contain compact NP agglomerates, whereas monocyte-like macrophages contain non-agglomerated NPs.

Immunomodulatory and cytotoxic effects of various Lactococcus strains on the murine macrophage cell line J774.1

2008 ◽  
Vol 123 (1-2) ◽  
pp. 159-165 ◽  
Author(s):  
Chise Suzuki ◽  
Hiromi Kimoto-Nira ◽  
Miho Kobayashi ◽  
Masaru Nomura ◽  
Keisuke Sasaki ◽  
...  
Keyword(s):  
Cell Line ◽  
Murine Macrophage ◽  
Macrophage Cell Line ◽  
Macrophage Cell ◽  
Cytotoxic Effects ◽  
Murine Macrophage Cell Line

Effects of aflatoxin M1 and aflatoxin M2 on J774A.1 murine macrophage cell line

2010 ◽  
Vol 196 ◽  
pp. S201 ◽  
Author(s):  
R. Russo ◽  
G. Bianco ◽  
S. Marzocco ◽  
A. De Simone ◽  
G. Autore ◽  
...  
Keyword(s):  
Cell Line ◽  
Aflatoxin M1 ◽  
Murine Macrophage ◽  
Macrophage Cell Line ◽  
Macrophage Cell ◽  
Murine Macrophage Cell Line

In vitro differentiation of the murine macrophage cell line BDM-1 into osteoclast-like cells.

Endocrinology ◽  
1995 ◽  
Vol 136 (10) ◽  
pp. 4285-4292 ◽  
Author(s):  
J H Shin ◽  
A Kukita ◽  
K Ohki ◽  
T Katsuki ◽  
O Kohashi
Keyword(s):  
Cell Line ◽  
Murine Macrophage ◽  
In Vitro Differentiation ◽  
Macrophage Cell Line ◽  
Macrophage Cell ◽  
Murine Macrophage Cell Line

Identification of tyrosine 706 in the kinase insert as the major colony-stimulating factor 1 (CSF-1)-stimulated autophosphorylation site in the CSF-1 receptor in a murine macrophage cell line

1990 ◽  
Vol 10 (6) ◽  
pp. 2991-3002
Author(s):  
P van der Geer ◽  
T Hunter
Keyword(s):  
Cell Line ◽  
Murine Macrophage ◽  
Colony Stimulating Factor ◽  
Macrophage Cell Line ◽  
Macrophage Cell ◽  
Major Site ◽  
Murine Macrophage Cell Line ◽  
Stimulating Factor

The receptor for colony-stimulating factor 1 (CSF-1) is a ligand-activated protein-tyrosine kinase. It has been shown previously that the CSF-1 receptor is phosphorylated on serine in vivo and that phosphorylation on tyrosine can be induced by stimulation with CSF-1. We studied the phosphorylation of the CSF-1 receptor by using the BAC1.2F5 murine macrophage cell line, which naturally expresses CSF-1 receptors. Two-dimensional tryptic phosphopeptide mapping showed that the CSF-1 receptor is phosphorylated on several different serine residues in vivo. Stimulation with CSF-1 at 37 degrees C resulted in rapid phosphorylation on tyrosine at one major site and one or two minor sites. We identified the major site as Tyr-706. The identity of Tyr-706 was confirmed by mutagenesis. This residue is located within the kinase insert domain. There was no evidence that Tyr-973 (equivalent to Tyr-969 in the human CSF-1 receptor) was phosphorylated following CSF-1 stimulation. When cells were stimulated with CSF-1 at 4 degrees C, additional phosphotyrosine-containing phosphopeptides were detected and the level of phosphorylation of the individual phosphotyrosine-containing phosphopeptides was substantially increased. In addition, we show that CSF-1 receptors are capable of autophosphorylation at six to eight major sites in vitro.

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