scholarly journals Characterization of deoxyribonuclease activities derived from control and inflammation-associated mouse peritoneal macrophages

1984 ◽  
Vol 220 (2) ◽  
pp. 561-568
Author(s):  
G E Brown ◽  
T P Karpetsky ◽  
K Rictor ◽  
A Rahman
Keyword(s):  
Peritoneal Cavity ◽  
Peripheral Blood ◽  
Peritoneal Macrophages ◽  
Apparent Size ◽  
Blood Components ◽  
Cell Type ◽  
Specific Subset ◽  
Mouse Peritoneal Macrophages ◽  
Increased Activity

Native DNAase (deoxyribonuclease) activities derived from mouse peritoneal cavity and peripheral blood components were separated, detected, and characterized by electrophoresis into polyacrylamide gels containing DNA, followed by incubation of the gels, and staining of the substrate to reveal only the DNAase activities. Resident peritoneal macrophages contained 12 DNAase-II-like activities that were characteristic of that cell type, whereas lymphocytes and granulocytes each contained five DNAases. Induction of inflammation by peritoneal injection of thioglycollate resulted in changes in macrophage DNAase expression, including: increased total DNAase activity, a decrease in the number of activities from 12 to 11, increased activity of a specific subset of the enzymes, and a change in the apparent size of a specific subset of the enzymes. Electrophoretic and enzymic properties and sensitivity to endo-beta-N-acetylglucosaminidase H indicated that the macrophage activities probably represented charge variants of one or two parent peptide chains.

scholarly journals Identification and characterization of a phospholipase C activity in resident mouse peritoneal macrophages. Inhibition of the enzyme by phenothiazines

1981 ◽  
Vol 197 (2) ◽  
pp. 523-526 ◽  
Author(s):  
Paul D. Wightman ◽  
Mary Ellen Dahlgren ◽  
James C. Hall ◽  
Philip Davies ◽  
Robert J. Bonney
Keyword(s):  
Phospholipase C ◽  
High Activity ◽  
Peritoneal Macrophages ◽  
Ph Optimum ◽  
Reaction Velocity ◽  
Neutral Ph ◽  
Maximum Reaction ◽  
Mouse Peritoneal Macrophages ◽  
Identification And Characterization

Resident mouse peritoneal macrophages contain a phospholipase C of high activity that is specific for phosphatidylinositol. The activity has a neutral pH optimum, is Ca2+-dependent and has a maximum reaction velocity of 525nmol/h per mg of protein. Certain phenothiazines are potent inhibitors of this activity.

scholarly journals Phagolysosome formation in normal and colchicine-treated macrophages.

1975 ◽  
Vol 142 (4) ◽  
pp. 903-913 ◽  
Author(s):  
E L Pesanti ◽  
S G Axline
Keyword(s):  
Acid Phosphatase ◽  
Lysosomal Enzyme ◽  
Peritoneal Macrophages ◽  
Cell Type ◽  
Inert Particles ◽  
Time Periods ◽  
Mouse Peritoneal Macrophages ◽  
Over Time

Intracellular lysosomal fusion has been evaluated in cultivated mouse peritoneal macrophages by measurement of transfer of acid phosphatase to polyvinyltoluene (PVT)-containing phagolysosomes. Enzyme transfer was found to be directly and significantly related to the uptake of PVT and to be independent of time allowed for phagolysosome formation over time periods of 15 min to 18 h. In addition, the extent of transfer of lysosomal enzyme to phagolysosomes was unaffected by treatment of the cells with 10(-6) M colchicine, a dose which eradicates morphologically identifiable microtubules in this cell type within 2 h. The data indicate that intracellular fusion of lysosomes with phagosomes in the macrophage does not require formed microtubules and suggest that fusion occurs promptly after interiorization of inert particles.

scholarly journals Characterization of murine peritoneal macrophage receptors for fibrin(ogen) degradation products

Blood ◽  
1986 ◽  
Vol 67 (5) ◽  
pp. 1224-1228 ◽  
Author(s):  
S Rajagopalan ◽  
SV Pizzo
Keyword(s):  
Degradation Products ◽  
Peritoneal Macrophages ◽  
Receptor System ◽  
Human Fibrinogen ◽  
Murine Peritoneal Macrophage ◽  
High Affinity ◽  
Macrophage Receptors ◽  
Low Concentrations ◽  
Mouse Peritoneal Macrophages

Abstract The binding of human fibrinogen degradation fragments D1, E, X, and Y, as well as fibrin fragment D1 dimer, to mouse peritoneal macrophages was examined. A Scatchard plot of fragment D1 binding was biphasic, suggesting two classes of receptors. Fragments D1, D1 dimer, X, and Y in low concentrations bound to macrophages with high affinity (Kd = 23 to 73 X 10(-11) mol/L). Fragment E bound specifically but at a much lower level than the other fragments. Fragment D1 was able to compete for the binding of radiolabeled fragments X and Y but not radiolabeled fragment E. These studies indicate that fragments D and E are recognized by separate receptor systems but that all of the fibrinogen degradation products that contain the D domain are recognized by the same receptor system.

Characterization of membrane melatonin receptor in mouse peritoneal macrophages: inhibition of adenylyl cyclase by a pertussis toxin-sensitive G protein

1999 ◽  
Vol 95 (1-2) ◽  
pp. 85-94 ◽  
Author(s):  
Antonio Garcı́a-Pergañeda ◽  
Juan M Guerrero ◽  
Mohammed Rafii-El-Idrissi ◽  
M Paz Romero ◽  
David Pozo ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
G Protein ◽  
Pertussis Toxin ◽  
Peritoneal Macrophages ◽  
Melatonin Receptor ◽  
Mouse Peritoneal Macrophages

scholarly journals Characterization of murine peritoneal macrophage receptors for fibrin(ogen) degradation products

Blood ◽  
1986 ◽  
Vol 67 (5) ◽  
pp. 1224-1228 ◽  
Author(s):  
S Rajagopalan ◽  
SV Pizzo
Keyword(s):  
Degradation Products ◽  
Peritoneal Macrophages ◽  
Receptor System ◽  
Human Fibrinogen ◽  
Murine Peritoneal Macrophage ◽  
High Affinity ◽  
Macrophage Receptors ◽  
Low Concentrations ◽  
Mouse Peritoneal Macrophages

The binding of human fibrinogen degradation fragments D1, E, X, and Y, as well as fibrin fragment D1 dimer, to mouse peritoneal macrophages was examined. A Scatchard plot of fragment D1 binding was biphasic, suggesting two classes of receptors. Fragments D1, D1 dimer, X, and Y in low concentrations bound to macrophages with high affinity (Kd = 23 to 73 X 10(-11) mol/L). Fragment E bound specifically but at a much lower level than the other fragments. Fragment D1 was able to compete for the binding of radiolabeled fragments X and Y but not radiolabeled fragment E. These studies indicate that fragments D and E are recognized by separate receptor systems but that all of the fibrinogen degradation products that contain the D domain are recognized by the same receptor system.

scholarly journals THE EFFECT OF GLUCOCORTICOSTEROIDS ON THE KINETICS OF MONONUCLEAR PHAGOCYTES

1970 ◽  
Vol 131 (3) ◽  
pp. 429-442 ◽  
Author(s):  
Jan Thompson ◽  
Ralph van Furth
Keyword(s):  
Peritoneal Cavity ◽  
Peripheral Blood ◽  
Peritoneal Macrophages ◽  
Rapid Decrease ◽  
Mononuclear Phagocytes ◽  
Water Soluble ◽  
Hydrocortisone Acetate ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Kinetics Of

The effect of glucocorticosteroids on the kinetics of mononuclear phagocytes, i.e., peripheral blood monocytes and peritoneal macrophages, was studied in normal mice, as well as in mice in which an inflammatory reaction was evoked in the peritoneal cavity. The administration of glucocorticosteroids resulted in a rapid decrease (within 3–6 hr) in the number of circulating monocytes, the duration being dependent on the nature and dose of the compound. The water-soluble dexamethasone sodium phosphate is only briefly active (less than 12 hr), but hydrocortisone acetate, which forms a subcutaneous depot, reduced the number of monocytes for more than 2 wk. In normal mice, hydrocortisone did not affect the number of macrophages already present in the peritoneal cavity, but the transit of mononuclear phagocytes from the circulation into the peritoneal cavity was arrested. During an inflammatory response in the peritoneal cavity, hydrocortisone suppresses both the increase in the number of monocytes in the peripheral blood and the increase in the number of peritoneal macrophages. This reduction of the inflammatory exudate appeared to be due to a diminished influx of mononuclear phagocytes from the peripheral blood. No lytic action of glucocorticosteroids on the mononuclear phagocytes could be demonstrated.

scholarly journals Purification and Structural Characterization of a Novel Water-Soluble Neutral Polysaccharide from Cantharellus cibarius and Its Immunostimulating Activity in RAW264.7 Cells

2017 ◽  
Vol 2017 ◽  
pp. 1-9 ◽  
Author(s):  
Long Chen ◽  
Xichun Peng ◽  
Jiaying Lv ◽  
Siyin Liao ◽  
Shiyi Ou ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Functional Food ◽  
Peritoneal Macrophages ◽  
Water Soluble ◽  
Raw264.7 Cells ◽  
Molar Ratio ◽  
Immunostimulating Activity ◽  
Ft Ir ◽  
Mouse Peritoneal Macrophages

Polysaccharide is one of the important active ingredients of Cantharellus cibarius. The aims of this work were to analyze preliminary characterization and to investigate immunostimulating activity of a novel water-soluble neutral polysaccharide named JP1, which was purified from the fruiting body of Cantharellus cibarius using DEAE-FF chromatography and Sephadex G-100 chromatography. The characteristics of JP1 were determined by HPGPC, FT-IR spectra, gas chromatography, and Congo Red Method. Immunostimulating activity of JP1 was investigated in RAW264.7 cells. Results indicated that JP1 consisted of L-Arabinose, D-Mannose, D-Glucose, and D-Galactose in a molar ratio of 1 : 1.06 : 1.95 : 1.17 with a molecular weight of 336 kDa. JP1 is nontoxic to RAW264.7 cells at this concentration range (62.5–1000 μg/mL). Furthermore, JP1 can promote mouse peritoneal macrophages to secrete NO and enhance the secretion of macrophages’ cytokines IL-6 in RAW264.7 cells. These results suggested that JP1 could have potential immunostimulating activity applications as medicine or functional food.

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