Phagocytic Index of Malassezia pachydermatis and Malassezia furfur by a Murine Macrophage Cell Line: An In-Vitro Study

2017 ◽  
Vol 156 (1) ◽  
pp. 99
Author(s):  
R.T.F. Moreira ◽  
M.A. Lallo ◽  
E.C. Perez ◽  
J.G. Xavier ◽  
F.T. Konno ◽  
...  
Endocrinology ◽  
1995 ◽  
Vol 136 (10) ◽  
pp. 4285-4292 ◽  
Author(s):  
J H Shin ◽  
A Kukita ◽  
K Ohki ◽  
T Katsuki ◽  
O Kohashi

1990 ◽  
Vol 10 (6) ◽  
pp. 2991-3002
Author(s):  
P van der Geer ◽  
T Hunter

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.


Immunobiology ◽  
1988 ◽  
Vol 178 (3) ◽  
pp. 261-274 ◽  
Author(s):  
Ina S. Klasen ◽  
Johannes P. de Jong ◽  
Jane S.A. Voerman ◽  
Renée M.T. Ladestein ◽  
Pieter J.M. Leenen ◽  
...  

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