scholarly journals Spontaneous lysosomal enzyme secretion by a murine macrophage-like cell line

1980 ◽  
Vol 190 (3) ◽  
pp. 847-850 ◽  
Author(s):  
W Jessup ◽  
R T Dean
Keyword(s):  
Cell Line ◽  
Lysosomal Enzyme ◽  
Peritoneal Macrophages ◽  
Enzyme Secretion ◽  
Murine Macrophage ◽  
Lysosomal Hydrolase

Lysosomal enzyme secretion by the murine macrophage-like cell line, P388D1, was compared with that of normal peritoneal macrophages. Unlike macrophages, lysosomal hydrolase secretion by P388D1 cells occurred spontaneously in vitro and was not further stimulated by the presentation of inflammatory agents such as zymosan and asbestos.

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.

Biological Evaluation of Some Selected Cyclic Imides: Mitochondrial Effects and in vitro Cytotoxicity

2004 ◽  
Vol 59 (9-10) ◽  
pp. 663-672 ◽  
Author(s):  
Silvia Regina Tozado Prado ◽  
Valdir Cechinel-Filho ◽  
Fátima Campos Buzzi ◽  
Rogério Corrêa ◽  
Silvia Maria Correia Suter Cadena ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Cell Viability ◽  
Cell Line ◽  
Biological Activities ◽  
General Structure ◽  
Peritoneal Macrophages ◽  
Biological Evaluation ◽  
Rat Liver Mitochondria ◽  
Cyclic Imides

Abstract Cyclic imides such as succinimides, maleimides, glutarimides, phthalimides and their derivatives contain an imide ring and a general structure -CO-N(R)-CO- that confers hydrophobicity and neutral characteristic. A diversity of biological activities and pharmaceutical uses have been attributed to them, such as antibacterial, antifungal, antinociceptive, anticonvulsant, antitumor. In spite of these activities, much of their action mechanisms at molecular and cellular levels remain to be elucidated. We now show the effects of several related cyclic imides: maleimides (S2, S2.1, S2.2, S3), glutarimides (S4, S5, S6), 4-aminoantipyrine derivatives (L1, F1, AL1, F1.14, F1.2) and sulfonated succinimides (RO1, FA, FE, FD, MC, DMC) on isolated rat liver mitochondria, B16-F10 melanoma cell line, peritoneal macrophages and different bacterial streams. The effects on mitochondrial respiratory parameters, cell viability and antibacterial activity were also evaluated. The results indicated that S3, S5 and S6 caused an increased oxygen consumption in the presence of ADP (state III) or its absence (state IV), while all other compounds decreased those parameters at different degrees of inhibition. All the compounds decreased the respiratory control coefficient (RCC). Loss of cell viability of peritoneal macrophages and the B16- F10 cell line was observed, L1 and S2.1 being more effective. S1, S2, S3, L1 and F1 compounds showed antibacterial activity at experimental concentrations.

scholarly journals Infectivity of amastigotes of Trypanosoma cruzi

1986 ◽  
Vol 28 (4) ◽  
pp. 205-212 ◽  
Author(s):  
Tecia Ulisses de Carvalho ◽  
Wanderley de Souza
Keyword(s):  
Trypanosoma Cruzi ◽  
Guinea Pig ◽  
Cell Line ◽  
Peritoneal Macrophages ◽  
Mouse Peritoneal Macrophages ◽  
Pig Serum

The infectivity amastigotes of Trypanosoma cruzi, isolated from the supernatant of the J774G8 macrophage-like cell line infected with trypomastigotes to normal macrophages in vitro was tested. After a period of 1 h of T. cruzi-macrophage interaction about 2% of the mouse peritoneal macrophages had ingested amastigotes. In contrast 12% of the macrophages had ingested epimastigotes. Treatment of the amastigotes with trypsin did not interfere with their ingestion by macrophages. Once inside the macrophages the amastigotes divided and after some days transformed into trypomastigotes. When i.p. inoculated into mice the amastigotes were highly infective, inducing high levels of parasitaemia and tissue parasitism. As previously described for trypomastigotes, amastigotes were not lysed when incubated in the presence of fresh guinea-pig serum. Contrasting with what has been described for trypomastigotes, the resistance of amastigotes to complement-mediated lysis persisted after treatment with trypsin.

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