Characterization of Liposomes Containing the Chemotactic Peptide N-formyl-methionylleucyl-phenylalanine (FMLP) and Their Interaction with Mouse Macrophages

1987 ◽  
Vol 4 (4) ◽  
pp. 233-244 ◽  
Author(s):  
RAJIV NAYAR ◽  
KIYOSHI MORIKAWA ◽  
ISAIAH J. FIDLER
Keyword(s):  
Chemotactic Peptide ◽  
Mouse Macrophages

scholarly journals Identification and Characterization of Poly(I:C)-induced Molecular Responses Attenuated by Nicotine in Mouse Macrophages

2012 ◽  
Vol 83 (1) ◽  
pp. 61-72 ◽  
Author(s):  
Wen-Yan Cui ◽  
Shufang Zhao ◽  
Renata Polanowska-Grabowska ◽  
Ju Wang ◽  
Jinxue Wei ◽  
...  
Keyword(s):  
Poly I:C ◽  
Molecular Responses ◽  
Mouse Macrophages ◽  
Identification And Characterization

scholarly journals Characterization of an oligopeptide chemoattractant receptor on human blood monocytes using a new radioligand

Blood ◽  
1984 ◽  
Vol 63 (3) ◽  
pp. 588-592 ◽  
Author(s):  
MC Benyunes ◽  
R Snyderman
Keyword(s):  
Human Blood ◽  
Polymorphonuclear Leukocytes ◽  
Specific Radioactivity ◽  
Blood Monocytes ◽  
Chemotactic Peptide ◽  
Peripheral Blood Monocytes ◽  
Peptide Receptor ◽  
Human Polymorphonuclear Leukocytes ◽  
Dissociation Constant Kd

Abstract The study of chemoattractant receptors on human monocytes had been limited by the lack of a radioligand suitable for use with the small numbers of cells routinely available from human donors. A new synthetic oligopeptide radioligand f[35S]met-leu-phe, with a higher specific radioactivity than was available with the tritiated compound, was used to characterize a chemoattractant receptor on freshly isolated human blood monocytes. These cells bind f[35S]met-leu-phe with a dissociation constant (KD) of 30.2 +/- 5.6 nM and contain 84,000 +/- 11,300 receptors per cell. f[35S]met-leu-phe does not bind specifically to blood lymphocytes. The specificity of the oligopeptide receptor on monocytes is indistinguishable from the oligopeptide chemoattractant receptor on human polymorphonuclear leukocytes. Using f[35S]met-leu- phe, it will now be feasible to study the chemotactic peptide receptor on small numbers of partially purified peripheral blood monocytes from patients with defects of immune function.

Cloning and characterization of inducible nitric oxide synthase from mouse macrophages

Science ◽  
1992 ◽  
Vol 256 (5054) ◽  
pp. 225-228 ◽  
Author(s):  
Q. Xie ◽  
H. Cho ◽  
J Calaycay ◽  
R. Mumford ◽  
K. Swiderek ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Inducible Nitric Oxide Synthase ◽  
Mouse Macrophages ◽  
Oxide Synthase ◽  
Inducible Nitric Oxide

scholarly journals Phagosome-lysosome fusion. Characterization of intracellular membrane fusion in mouse macrophages.

1980 ◽  
Vol 85 (3) ◽  
pp. 754-765 ◽  
Author(s):  
M C Kielian ◽  
Z A Cohn
Keyword(s):  
Incubation Temperature ◽  
Intracellular Membrane ◽  
Intact Mouse ◽  
Thorium Dioxide ◽  
Mouse Macrophages ◽  
Enzymatic Marker ◽  
Secondary Lysosomes ◽  
Intracellular Membrane Fusion ◽  
Number Of Particles

Several approaches have been used to study the determinants of phagosome-lysosome fusion in intact mouse macrophages. Lysosomes were labeled with the fluorescent vital dye acridine orange and the rate and extent of their fusion with yeast-containing phagosomes was monitored by fluorescence microscopy. Fusion was also assayed by electron microscopy, using horseradish peroxidase or thorium dioxide as a marker for secondary lysosomes. Good agreemen samples with an enzymatic marker, and thorium dioxide-labeled samples evaluated by stereology. The rate of usion as assayed by fluorescence was not affected by the number of particles ingested, serum concentration, or prior uptake of digestible or nondigestible substances. With this assay it was possible to observe the rate of fusion separate from and uninfluenced by the phagocytic rate. Both the rate and extent of fusion were dramatically increased after several days in culture and similar changes were found by use of the EM assays. Fusion was strongly affected by incubation temperature, having a Q10 of 2.5 No detectable fusion occurred below 15 degrees C, and this inhibition was rapidly reversed when cells were returned to 37 degrees C.

scholarly journals Characterization of an oligopeptide chemoattractant receptor on human blood monocytes using a new radioligand

Blood ◽  
1984 ◽  
Vol 63 (3) ◽  
pp. 588-592
Author(s):  
MC Benyunes ◽  
R Snyderman
Keyword(s):  
Human Blood ◽  
Polymorphonuclear Leukocytes ◽  
Specific Radioactivity ◽  
Blood Monocytes ◽  
Chemotactic Peptide ◽  
Peripheral Blood Monocytes ◽  
Peptide Receptor ◽  
Human Polymorphonuclear Leukocytes ◽  
Dissociation Constant Kd

The study of chemoattractant receptors on human monocytes had been limited by the lack of a radioligand suitable for use with the small numbers of cells routinely available from human donors. A new synthetic oligopeptide radioligand f[35S]met-leu-phe, with a higher specific radioactivity than was available with the tritiated compound, was used to characterize a chemoattractant receptor on freshly isolated human blood monocytes. These cells bind f[35S]met-leu-phe with a dissociation constant (KD) of 30.2 +/- 5.6 nM and contain 84,000 +/- 11,300 receptors per cell. f[35S]met-leu-phe does not bind specifically to blood lymphocytes. The specificity of the oligopeptide receptor on monocytes is indistinguishable from the oligopeptide chemoattractant receptor on human polymorphonuclear leukocytes. Using f[35S]met-leu- phe, it will now be feasible to study the chemotactic peptide receptor on small numbers of partially purified peripheral blood monocytes from patients with defects of immune function.

scholarly journals Characterization of a Glutathione Metabolic Mutant of Mycobacterium tuberculosis and Its Resistance to Glutathione and Nitrosoglutathione

2006 ◽  
Vol 188 (4) ◽  
pp. 1364-1372 ◽  
Author(s):  
Yaswant K. Dayaram ◽  
Meliza T. Talaue ◽  
Nancy D. Connell ◽  
Vishwanath Venketaraman
Keyword(s):  
Nitric Oxide ◽  
Mycobacterium Tuberculosis ◽  
Metabolic Enzyme ◽  
Bacterial Cells ◽  
Wild Type ◽  
Mouse Macrophages ◽  
Carrier Molecule ◽  
Glutamyl Transpeptidase

ABSTRACT Glutathione is a tripeptide and antioxidant, synthesized at high levels by cells during the production of reactive oxygen and nitrogen intermediates. Glutathione also serves as a carrier molecule for nitric oxide in the form of S-nitrosoglutathione. Previous studies from this laboratory have shown that glutathione and S-nitrosoglutathione are directly toxic to mycobacteria. Glutathione is not transported into the cells as a tripeptide. Extracellular glutathione is converted to a dipeptide due to the action of transpeptidase, and the dipeptide is then transported into the bacterial cells. The processing of glutathione and S-nitrosoglutathione is brought about by the action of the enzyme γ-glutamyl transpeptidase. The function of γ-glutamyl transpeptidase is to cleave glutathione and S-nitrosoglutathione to the dipeptide (Cys-Gly), which is then transported into the bacterium by the multicomponent ABC transporter dipeptide permease. We have created a mutant strain of Mycobacterium tuberculosis lacking this metabolic enzyme. We investigated the sensitivity of this strain to glutathione and S-nitrosoglutathione compared to that of the wild-type bacteria. In addition, we examined the role of glutathione and/or S-nitrosoglutathione in controlling the growth of intracellular M. tuberculosis inside mouse macrophages.

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