scholarly journals Upregulation of mouse CD14 expression in Kupffer cells by lipopolysaccharide.

1994 ◽  
Vol 179 (5) ◽  
pp. 1671-1676 ◽  
Author(s):  
K Matsuura ◽  
T Ishida ◽  
M Setoguchi ◽  
Y Higuchi ◽  
S Akizuki ◽  
...  
Keyword(s):  
Cell Line ◽  
Kupffer Cells ◽  
Intraperitoneal Injection ◽  
Specific Binding ◽  
Flow Cytometric Analysis ◽  
Peritoneal Macrophages ◽  
Macrophage Cell ◽  
Inflammatory Monocytes

Western blot analysis showed that a monoclonal antibody against recombinant mouse CD14 (mCD14), designated rmC5-3, specifically reacted with mouse macrophage cell line J774, but not myeloma cell line NS1. Fluorographic and immunocytochemical analysis demonstrated specific binding of rmC5-3 with mouse resident macrophages, inflammatory monocytes and neutrophils, and macrophage cell lines. Immunohistochemical staining using rmC5-3 showed that CD14-positive Kupffer cells (KC) were small in number in the liver in nonstimulated mice. The number of stained KC, which were rich in the midzonal and periportal regions, gradually increased with time after intraperitoneal injection of lipopolysaccharide (LPS), peaked 6 h after injection, and returned to normal by 20 h after injection. Staining intensity over time was proportional to the number of KC. A slight increase in mCD14 expression was observed in peritoneal macrophages 2 h after LPS administration in vivo using flow cytometric analysis. mCD14 mRNA became detectable at 1 h after the intraperitoneal injection of LPS (20 micrograms/mice), and the level dramatically increased with time, peaking at 3 h, and sharply dropped at 6 h. The resident peritoneal macrophages demonstrated a constitutively high mCD14 mRNA expression, which slightly increased 2 h after LPS (100 ng/ml) stimulation in vitro. The level of mCD14 expression in macrophages did not increase after intraperitoneal injection of LPS (20 micrograms/mice).

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.

Comparison of the In Vivo and In Vitro Proliferation of Monoblasts, Promonocytes, and the Macrophage Cell Line J774

1982 ◽  
pp. 175-187 ◽  
Author(s):  
R. van Furth ◽  
Th. J. L. M. Goud ◽  
J. W. M. van der Meer ◽  
A. Blussé van Oud Alblas ◽  
M. M. C. Diesselhoff-den Dulk ◽  
...  
Keyword(s):  
Cell Line ◽  
Macrophage Cell Line ◽  
Macrophage Cell ◽  
In Vitro Proliferation

scholarly journals Clearance and binding of native and defucosylated lactoferrin

1983 ◽  
Vol 212 (2) ◽  
pp. 249-257 ◽  
Author(s):  
M J Imber ◽  
S V Pizzo
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Binding ◽  
Gel Filtration ◽  
Peritoneal Macrophages ◽  
Mononuclear Phagocyte ◽  
Stable Complex

These studies explore the role of carbohydrate recognition systems and the direct involvement of terminal alpha 1-3-linked fucose in the clearance of lactoferrin from the murine circulation and in the specific binding of lactoferrin to receptors on murine peritoneal macrophages. As previously reported, radiolabelled lactoferrin cleared very rapidly (t1/2 less than 1 min) after intravenous injection into mice. However, competing levels of ligands specific for the hepatic galactose receptor (asialo-orosomucoid), the hepatic fucose receptor (fucosyl-bovine serum albumin), and the mononuclear-phagocyte system pathway recognizing mannose, N-acetylglucosamine and fucose (mannosyl-, N-acetylglucosaminyl- and fucosyl-bovine serum albumin) did not block radiolabelled lactoferrin clearance in vivo or binding to mouse peritoneal macrophage monolayers in vitro. Almond emulsin alpha 1-3-fucosidase was used to prepare defucosylated lactoferrin in which 88% of the alpha 1-3-linked fucose was hydrolysed. No difference in clearance or receptor binding was observed between radiolabelled native and defucosylated lactoferrin. Fucoidin, a fucose-rich algal polysaccharide, completely inhibits the clearance in vivo and macrophage binding in vitro of lactoferrin. This effect, however, is probably not the result of competition for binding to the fucose receptor, since gel-filtration studies demonstrated formation of a stable complex between lactoferrin and fucoidin. The present results indicate that the lactoferrin-clearance pathway is distinct from several pathways mediating glycoprotein clearance through recognition of terminal galactose, fucose, N-acetylglucosamine or mannose. Furthermore, alpha 1-3-linked fucose on lactoferrin is not essential for lactoferrin clearance in vivo or specific binding to macrophage receptors in vitro.

Helianthus tuberosus agglutinin directly induces neutrophil migration, which can be modulated/inhibited by resident mast cells

2005 ◽  
Vol 83 (5) ◽  
pp. 659-666 ◽  
Author(s):  
Veruska B.M Alencar ◽  
Gerly A.C Brito ◽  
Nylane M.N Alencar ◽  
Ana M.S Assreuy ◽  
Vicente P.T Pinto ◽  
...  
Keyword(s):  
Cell Population ◽  
Specific Binding ◽  
Neutrophil Migration ◽  
Peritoneal Macrophages ◽  
In Vitro Assays ◽  
Peritoneal Mast Cell ◽  
Helianthus Tuberosus ◽  
Neutrophil Chemotaxis

We investigated the effect of Helianthus tuberosus agglutinin (HTA) on neutrophil migration in vivo and in vitro. The role of resident cells in this effect was analyzed. Peritonitis was induced by injecting stimuli into rat (150–200 g) peritoneal cavities, and in vitro neutrophil chemotaxis was performed using a Boyden microchamber. HTA (80, 200, or 500 µg/mL per cavity) induced significant in vivo neutrophil migration (p < 0.05); in vitro assays showed that this lectin also induced neutrophil chemotaxis, an effect inhibited by the incubation of lectin associated with α-D(+)-mannose, its specific binding sugar. Depletion of the resident-cell population by peritoneal lavage did not alter HTA-induced neutrophil migration (200 µg/mL per cavity). The opposite strategy, increasing peritoneal macrophages by intraperitoneally injecting rats with thioglycollate, did not enhance the neutrophil migration produced by HTA (200 µg/mL per cavity). In addition, injection of supernatant from HTA-stimulated macrophage culture (300 µg/mL) into rat peritoneal cavities did not induce neutrophil migration. However, reduction of the peritoneal mast-cell population potentiated the neutrophil migration (p < 0.05) induced by HTA (200 µg/mL per cavity). Lectin from H. tuberosus has a direct neutrophil chemotatic effect that is modulated by mast cells.Key words: lectins, inflammation, Helianthus tuberosus, neutrophil migration.

Murine Macrophage Cell Line AP284 Presents Antigen to Cloned MT4+, Lyt-2− T Cells in vitro and in vivo

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 ◽  
...  
Keyword(s):  
T Cells ◽  
Cell Line ◽  
Murine Macrophage ◽  
Macrophage Cell Line ◽  
Macrophage Cell ◽  
Murine Macrophage Cell Line

Identification of toxic mineral dusts using mammalian cells

1980 ◽  
Vol 71 (3) ◽  
pp. 181-184 ◽  
Author(s):  
R. Davies ◽  
M. Chamberlain ◽  
R. C. Brown ◽  
D. M. Griffiths
Keyword(s):  
Cell Line ◽  
Mammalian Cells ◽  
Chinese Hamster ◽  
Cell Types ◽  
Peritoneal Macrophages ◽  
Alveolar Type ◽  
Mineral Dusts ◽  
Potential Pathogenicity

ABSTRACTCell culture systems have been developed to assess the potential pathogenicity of mineral dusts. The in vitro cytotoxicities of a variety of dusts towards mouse peritoneal macrophages, Chinese hamster lung cells (V79 cell line) and human alveolar type II cells (A549 cell line) were investigated.Non-pathogenic dusts were found to be inert in vitro. Fibrogenic non-fibrous dusts such as silica were only cytotoxic towards macrophages. Fibrous dusts which are both fibrogenic and carcinogenic in vivo are cytotoxic towards all three cell types, their cytotoxicity being dependent on fibre size. The size range important for the observed biological effect is longer than about 8 μm and thinner than about 1·5 μm.

scholarly journals Role of the Type III Secreted Exoenzymes S, T, and Y in Systemic Spread of Pseudomonas aeruginosa PAO1 In Vivo

2005 ◽  
Vol 73 (3) ◽  
pp. 1706-1713 ◽  
Author(s):  
Russell E. Vance ◽  
Arne Rietsch ◽  
John J. Mekalanos
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cell Line ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Host Cells ◽  
Macrophage Cell ◽  
Type Iii

ABSTRACT Pseudomonas aeruginosa uses a dedicated type III secretion system to deliver toxins directly into the cytoplasm of host cells. While progress has been made in elucidating the function of type III-secreted toxins in vitro, the in vivo functions of the type III-secreted exoenzymes are less well understood, particularly for the sequenced strain PAO1. Therefore, we have systematically deleted the genes for the three known type III effector molecules (exoS, exoT, and exoY) in P. aeruginosa PAO1 and assayed the effect of the deletions, both singly and in combination, on cytotoxicity in vitro and in vivo. We found that the type III secretion system acts differently on different cell types, causing an exoST-dependent rounding of a lung epithelial-like cell line in contrast to causing an exoSTY-independent but translocase (popB)-dependent lysis of a macrophage cell line. We utilized an in vivo competitive infection model to test each of our mutants, examining replication in the lung and spread to secondary sites such as the blood and spleen. Type III mutants inoculated intranasally exhibited only a minor defect in replication and survival in the lung, but popB and exoSTY triple mutants were profoundly defective in their ability to spread systemically. Intravenous injection of the mutants indicated that the type III secretion machinery is required for survival in the blood. Furthermore, our findings suggest that the effector-independent popB-dependent cytotoxicity that we and others have observed in vitro in macrophage cell lines may not be of great importance in vivo.

scholarly journals 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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