Macrophage Receptors and Leishmania

1992 ◽  
pp. 17-30 ◽  
Author(s):  
Mary E. Wilson ◽  
John E. Donelson ◽  
Richard D. Pearson ◽  
Ramesh Ramamoorthy
Keyword(s):  
Macrophage Receptors

Atomic force microscopy-based molecular studies on the recognition of immunogenic chlorinated ovalbumin by macrophage receptors

2012 ◽  
Vol 25 (2) ◽  
pp. 82-88 ◽  
Author(s):  
Szczepan Zapotoczny ◽  
Rafał Biedroń ◽  
Janusz Marcinkiewicz ◽  
Maria Nowakowska
Keyword(s):  
Atomic Force Microscopy ◽  
Force Microscopy ◽  
Macrophage Receptors ◽  
Atomic Force ◽  
Molecular Studies

Two independent macrophage receptors for acetylated high-density lipoprotein

1993 ◽  
Vol 1170 (2) ◽  
pp. 143-150 ◽  
Author(s):  
Miyazaki Akira ◽  
Sakai Masakazu ◽  
Yamaguchi Eiji ◽  
Sakamoto Yu-Ichiro ◽  
Shichiri Motoaki ◽  
...  
Keyword(s):  
High Density Lipoprotein ◽  
Density Lipoprotein ◽  
High Density ◽  
Macrophage Receptors

STUDIES ON THE PHYSIOLOGY OF MACROPHAGE RECEPTORS FOR ?-MACROGLOBULIN � PROTEASE COMPLEXES

1983 ◽  
Vol 421 (1 Chemistry and) ◽  
pp. 442-455 ◽  
Author(s):  
Jerry Kaplan ◽  
Elissa A. Keogh
Keyword(s):  
Macrophage Receptors

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.

Th-P15:104 Triglyceride-rich lipoproteins derived from pomace olive oil have differential effects on the expression of MRNA for macrophage receptors

2006 ◽  
Vol 7 (3) ◽  
pp. 515-516
Author(s):  
R. Cabello-Moruno ◽  
J.S. Perona ◽  
E. Montero ◽  
M. Avella ◽  
K.M. Botham ◽  
...  
Keyword(s):  
Olive Oil ◽  
Differential Effects ◽  
Macrophage Receptors

Influence of minor components of olive oils on the composition and size of TRLs and on macrophage receptors involved in foam cell formation

2007 ◽  
Vol 35 (3) ◽  
pp. 470-471 ◽  
Author(s):  
R. Cabello-Moruno ◽  
J.S. Perona ◽  
V. Ruiz-Gutierrez
Keyword(s):  
Dietary Fat ◽  
Foam Cell ◽  
Cell Formation ◽  
Epidemiologic Studies ◽  
Dietary Fats ◽  
Foam Cell Formation ◽  
Minor Components ◽  
Cardiovascular Heart Disease ◽  
Macrophage Receptors

Metabolic and epidemiologic studies support the idea that the type of dietary fat is more important than the total amount of fat with respect to the development of atherosclerosis and the risk of cardiovascular heart disease. Dietary fat is carried in CMs (chylomicrons), which can be taken up by macrophages without need of further oxidation, leading to the formation of foam cells and initiating or aggravating the atherogenic process. Evidence from different studies has shown that dietary fat can influence the composition and size of TRLs (triacylglycerol-rich lipoproteins), which might modulate their atherogenicity to a certain extent. In particular, experiments in vitro have shown the anti-atherogenic effects of minor components from olive oil when forming part of TRL, as these particles give minor lipid components the opportunity to interact with the cells implicated in endothelial dysfunction and atherogenesis. However, the exact mechanisms mediating CM uptake by macrophages still remain unclear. Thus further studies are needed to understand how the modifications of TRL composition caused by dietary fats could modulate the expression of macrophage receptors and foam cell formation, or even improve the atherogenic risk of these particles.

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.

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