Role of kinases and G-proteins on arachidonate release induced by zymosan in mouse peritoneal macrophages

1996 ◽  
Vol 28 (4) ◽  
pp. 465-472 ◽  
Author(s):  
Sergio Lloret ◽  
Juan J. Moreno
Keyword(s):  
G Proteins ◽  
Peritoneal Macrophages ◽  
Arachidonate Release ◽  
Mouse Peritoneal Macrophages

scholarly journals A Critical Role of Activin A in Maturation of Mouse Peritoneal Macrophages in vitro and in vivo

2009 ◽  
Vol 6 (5) ◽  
pp. 387-392 ◽  
Author(s):  
Yinan Wang ◽  
Xueling Cui ◽  
Guixiang Tai ◽  
Jingyan Ge ◽  
Nan Li ◽  
...  
Keyword(s):  
Critical Role ◽  
Peritoneal Macrophages ◽  
Activin A ◽  
Mouse Peritoneal Macrophages

scholarly journals Studies on the mechanism of phagocytosis. I. Requirements for circumferential attachment of particle-bound ligands to specific receptors on the macrophage plasma membrane.

1975 ◽  
Vol 142 (5) ◽  
pp. 1263-1282 ◽  
Author(s):  
F M Griffin ◽  
J A Griffin ◽  
J E Leider ◽  
S C Silverstein
Keyword(s):  
Plasma Membrane ◽  
Sheep Erythrocyte ◽  
Peritoneal Macrophages ◽  
Membrane Receptors ◽  
Macrophage Receptors ◽  
Specific Receptors ◽  
Particle Ingestion ◽  
Plasma Membrane Receptors ◽  
Mouse Peritoneal Macrophages

These experiments were designed to evaluate the role of macrophage plasma membrane receptors for the third component of complement (C) and for the Fc portion of IgG in the ingestion phase of phagocytosis. Sheep erythrocyte (E) were coated with anti-E IgG [E(IgG)]; these E(IgG) were then attached to cultivated monolayers of mouse peritoneal macrophages under conditions which reversibly inhibit ingestion of E(IgG). The E(IgG)-macrophage complexes were further incubated under similar conditions with an antimacrophage IgG fraction which blocks Fc receptor-mediated ingestion but has no effect upon ingestion mediated by other phagocytic receptors. When these cultures were subsequently incubated under conditions optimal for particle ingestion, phagocytosis of the IgG-coated erythrocytes did not occur; the erythrocytes remained bound to the Fc receptors of the macrophage plasma membrane. To determine whether ligands must cover the entire surface of an attached particle to permit ingestion of that particle, C-coated E [E(IgM)C] were bound to the C receptors of thioglycollate-induced (activated) macrophages at 4 degrees C. E(IgM)C-macrophage complexes were then trypsinized at 4 degrees C, a procedure which resulted in cleavage of erythrocyte-bound C3b molecules to a form of C3 not recognized by the macrophage receptors for C3b. Under the conditions used, trypsin did not affect the attachment of E(IgM)C to the macrophage surface or the macrophage receptors for C3b. When these trypsin treated E(IgM)C-macrophage complexes were incubated at 37 degrees C, the bound E(IgM)C were not ingested; the erythrocytes remained attached to the macrophage plasma membrane via the macrophage's C receptors. These results indicate that attachment of a particle to specific receptors on the macrophage plasma membrane is not sufficient to trigger ingestion of that particle. Rather, ingestion requires the sequential, circumferential interaction of particle-bound ligands with specific plasma membrane receptors not involved in the initial attachment process.

A potential role of the NOD genetic background in mouse peritoneal macrophages for the development of primary effusion lymphoma

2016 ◽  
Vol 42 ◽  
pp. 37-42 ◽  
Author(s):  
Hiroki Goto ◽  
Ryusho Kariya ◽  
Kouki Matsuda ◽  
Eriko Kudo ◽  
Harutaka Katano ◽  
...  
Keyword(s):  
Genetic Background ◽  
Potential Role ◽  
Primary Effusion Lymphoma ◽  
Peritoneal Macrophages ◽  
Mouse Peritoneal Macrophages

scholarly journals Histone H2B as a functionally important plasminogen receptor on macrophages

Blood ◽  
2007 ◽  
Vol 110 (10) ◽  
pp. 3763-3772 ◽  
Author(s):  
Riku Das ◽  
Tim Burke ◽  
Edward F. Plow
Keyword(s):  
Binding Capacity ◽  
Peritoneal Macrophages ◽  
Blood Monocytes ◽  
Histone H2b ◽  
Cell Recruitment ◽  
Annexin 2 ◽  
Enhanced Expression ◽  
And Function ◽  
Mouse Peritoneal Macrophages

AbstractPlasminogen (Plg) facilitates inflammatory cell recruitment, a function that depends upon its binding to Plg receptors (Plg-Rs). However, the Plg-Rs that are critical for cell migration are not well defined. Three previously characterized Plg-Rs (α-enolase, annexin 2, and p11) and a recently identified Plg-R (histone H2B [H2B]) were assessed for their contribution to Plg binding and function on macrophages. Two murine macrophage cell lines (RAW 264.7 and J774A.1) and mouse peritoneal macrophages induced by thioglycollate were analyzed. All 4 Plg-Rs were present on the surface of these cells and showed enhanced expression on the thioglycollate-induced macrophages compared with peripheral blood monocytes. Using blocking Fab fragments to each Plg-R, H2B supported approximately 50% of the Plg binding capacity, whereas the other Plg-Rs contributed less than 25%. Anti-H2B Fab also demonstrated a major role of this Plg-R in plasmin generation and matrix invasion. When mice were treated intravenously with anti-H2B Fab, peritoneal macrophage recruitment in response to thioglycollate was reduced by approximately 45% at 24, 48, and 72 hours, with no effect on blood monocyte levels. Taken together, these data suggest that multiple Plg-Rs do contribute to Plg binding to macrophages, and among these, H2B plays a very prominent and functionally important role.

scholarly journals Role of prostaglandin E2 in peptidoglycan mediated iNOS expression in mouse peritoneal macrophages in vitro

FEBS Letters ◽  
2010 ◽  
Vol 584 (19) ◽  
pp. 4227-4232 ◽  
Author(s):  
Yogesh Dahiya ◽  
Rajeev Kumar Pandey ◽  
Kunal H. Bhatt ◽  
Ajit Sodhi
Keyword(s):  
Prostaglandin E2 ◽  
Peritoneal Macrophages ◽  
Inos Expression ◽  
Mouse Peritoneal Macrophages

scholarly journals Role of Methionine Sulfoxide Reductases A and B of Enterococcus faecalis in Oxidative Stress and Virulence

2010 ◽  
Vol 78 (9) ◽  
pp. 3889-3897 ◽  
Author(s):  
Chen Zhao ◽  
Axel Hartke ◽  
Marilena La Sorda ◽  
Brunella Posteraro ◽  
Jean-Marie Laplace ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Enterococcus Faecalis ◽  
Galleria Mellonella ◽  
Methionine Sulfoxide ◽  
Peritoneal Macrophages ◽  
Infection Model ◽  
Repair Enzymes ◽  
Methionine Sulfoxide Reductases ◽  
Mouse Peritoneal Macrophages

ABSTRACT Methionine sulfoxide reductases A and B are antioxidant repair enzymes that reduce the S- and R-diastereomers of methionine sulfoxides back to methionine, respectively. Enterococcus faecalis, an important nosocomial pathogen, has one msrA gene and one msrB gene situated in different parts of the chromosome. Promoters have been mapped and mutants have been constructed in two E. faecalis strains (strains JH2-2 and V583) and characterized. For both backgrounds, the mutants are more sensitive than the wild-type parents to exposure to H2O2, and in combination the mutations seem to be additive. The virulence of the mutants has been analyzed in four different models. Survival of the mutants inside mouse peritoneal macrophages stimulated with recombinant gamma interferon plus lipopolysaccharide but not in naïve phagocytes is significantly affected. The msrA mutant is attenuated in the Galleria mellonella insect model. Deficiency in either Msr enzyme reduced the level of virulence in a systemic and urinary tract infection model. Virulence was reconstituted in the complemented strains. The combined results show that Msr repair enzymes are important for the oxidative stress response, macrophage survival, and persistent infection with E. faecalis.

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