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1.
Ross Fiziol Zh Im I M Sechenova ; 86(1): 41-5, 2000 Jan.
Article in Russian | MEDLINE | ID: mdl-10740835

ABSTRACT

Depending on the type of autonomous regulation, differences in basic levels of interleukin-1 beta (IL-1 beta) and tumor necrosis factor alpha (TNF alpha) were revealed under conditions of hyperthermia in healthy subjects aged 19-21. A parasympathetic type of autonomous regulation corresponded to higher initial levels of proinflammatory cytokinesis, whereas a dominating sympathetic type corresponded to lower levels of the IL-1 beta and TNF alpha. The subjects with the latter type of regulation revealed an increase in the IL-1 beta TNF alpha combined with a higher heat tolerance. The subjects with the former type of regulation revealed a lower heat tolerance. The increase in the alpha2-macroglobulin appeared to be a most typical acute phase response of the human body to hyperthermia.


Subject(s)
Acute-Phase Reaction , Autonomic Nervous System/physiology , Hot Temperature , Acute-Phase Proteins/biosynthesis , Adult , Blood Pressure , Body Temperature , Exercise Test , Heart Rate , Humans , Interleukin-1/biosynthesis , Male , Parasympathetic Nervous System/physiology , Sympathetic Nervous System/physiology , Tumor Necrosis Factor-alpha/biosynthesis
3.
Antibiot Khimioter ; 33(12): 906-9, 1988 Dec.
Article in Russian | MEDLINE | ID: mdl-3072930

ABSTRACT

Immunomodulating effects of various agents can be mediated by the system of mononuclear phagocytes (SMP). Immunomodulators are able to interfere with the initial events in activation of mononuclear phagocytes (MP) on their membranes which inevitably has its impact on molecular manifestations of the MP activation: the oxidative outburst events. At the initial (tentative) stage of the screening potential immunomodulators it is expedient to use tests providing estimation of the oxidative outburst intensity by the activity of glucoso-6-phosphate dehydrogenase, the key enzyme of the hexose monophosphate shunt and by the level of superoxydanions production judged by reduction of nitroblue tetrasolium (NBTT). The use of transplantable macrophage-like lines J.744 and P 338D as the targets instead of murine peritoneal MP made it possible to increase reproducibility of the results in screening of immunomodulators. An experimental model of the mouse abdominal cavity clearance within the first hours after intraperitoneal administration of the test bacteria was used for estimating the effect of the potential immunomodulators on the barrier function of the SMP in the host. Experimentally modeled quantitative and functional defects in the SMP served as and adequate test system for study of immunostimulating agents.


Subject(s)
Adjuvants, Immunologic/pharmacology , Models, Biological , Monocytes/immunology , Phagocytosis , Animals , Mice , Monocytes/drug effects , Peptide Fragments/pharmacology , Peritoneal Cavity/cytology , Peritonitis/immunology , Phagocytosis/drug effects , Salmonella Infections/immunology , Salmonella typhimurium , Thymopentin , Thymopoietins/pharmacology
4.
Biull Eksp Biol Med ; 105(1): 58-60, 1988 Jan.
Article in Russian | MEDLINE | ID: mdl-3337882

ABSTRACT

The effect of a synthetic antioxidant 2-tretbutyl-3-hydroxypyridine (TBHP) on the function of murine peritoneal macrophages (MP) has been studied. A direct contact of TBHP with MP in vitro increased the activity of a key enzyme of glucose monophosphate graft--glucose-6-phosphate dehydrogenase and the proportion of flattened MP. as compared to the control. Upon intraperitoneal MP injection the number of MP's in the abdominal cavity of mice increased. They differed from control MP's in enhanced flattening and phagocytosis. In mice with preinduced defect of abdominal clearance TBHP contributed to the recovery of the normal level of antibacterial protection. In all the in vitro and in vivo tests studying its activating effect on MP, the synthetic antioxidant was not inferior to the standard MP activator--bacterial lipopolysaccharide.


Subject(s)
Antioxidants/pharmacology , Macrophage Activation/drug effects , Pyridines/pharmacology , Animals , Ascitic Fluid/cytology , Glucosephosphate Dehydrogenase/metabolism , Mice , Phagocytosis/drug effects
5.
Biull Eksp Biol Med ; 101(6): 658-60, 1986 Jun.
Article in Russian | MEDLINE | ID: mdl-3730542

ABSTRACT

The purpose of this study was to compare the in vitro metabolic changes in mouse peritoneal macrophages exposed to sera of CHD patients and healthy donors. Oxidative (metabolic) burst was estimated by the activity of one of the limiting enzymes of hexose monophosphate shunt--glucoso-6-phosphate dehydrogenase. Pronounced enhancement of glucoso-6-phosphate dehydrogenase activity accompanied the exposure of macrophages to sera of patients with acute myocardial ischemia during the first two days after the onset of anginal pains. The correlation was established between the activity of creatine kinase in the sera of patients with acute myocardial infarction and the ability of these sera to enhance glucoso-6-phosphate dehydrogenase activity in mouse peritoneal macrophages.


Subject(s)
Glucosephosphate Dehydrogenase/metabolism , Macrophage Activation , Macrophages/enzymology , Myocardial Infarction/blood , Adult , Aged , Animals , Enzyme Activation , Humans , Macrophages/physiology , Mice , Middle Aged , Myocardial Infarction/physiopathology , Time Factors
7.
Biokhimiia ; 42(9): 1626-30, 1977 Sep.
Article in Russian | MEDLINE | ID: mdl-20999

ABSTRACT

In the presence of organophosphorus inhibitors (OPI) AChE inhibition is initiated at a lower concentration of ACh; the plot reaction rate versus substrate concentration shows two maxima with a distinct minimum between them. It was shown that extremely mild conditions (short-term heating up to 50 degrees C; acidic or alkaline pH shift by 0.5 units; high concentrations of bivalent cations; erythrocyte storage) which do not affect substrate inhibition, remove this effect. The data obtained suggest that OPI effect is not directed to the site of AChE responsible for enzyme inhibition by ACh excess ("substrate inhibition site"), but to some other area. This results in a change in the conformation of the substrate inhibition site and a pronounced inhibition of the AChE activity takes place at lower substrate concentration.


Subject(s)
Acetylcholinesterase/blood , Erythrocytes/enzymology , Organophosphorus Compounds/pharmacology , Cations, Divalent , Cell Membrane/enzymology , Cholinesterase Inhibitors , Hydrogen-Ion Concentration , Osmolar Concentration , Protein Conformation , Specimen Handling , Temperature
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