Subject(s)
Lymphocyte Activation , Receptors, Concanavalin A , Animals , Rats , Rats, Inbred StrainsABSTRACT
The possibility of using fluoresceine isothiocyanate to label plasmatic membranes of lymphocytes was explored. Membrane labeling can be done under physiological conditions. The label interacted with the surface located membrane component, and the binding centers became saturated with the label concentration which left the membrane undamaged. Modification of the membrane surface resulting from fluoresceine isothiocyanate treatment influenced significantly intercellular interactions mediating mitogen-induced blast transformation.
Subject(s)
Cell Membrane/ultrastructure , Fluoresceins , Lymphocytes/ultrastructure , Thiocyanates , Kinetics , Lymphocyte Activation , MitogensABSTRACT
It is shown that mitogenic stimuli from concanavalin A and phytohemagglutinin are summed up in the time. Under given experimental conditions each of the mitogens used did not induce mitogenesis when the interaction with lymphocytes continued for 14 and/or 20 hours. The results obtained are discussed from the point of view of the cell-to-cell interaction between the lymphocytes. It is assumed that the ability of the stimuli to sum up in the time underlies the nonspecific mechanism of defense from tolerance.
Subject(s)
Lectins/pharmacology , Lymphocytes/drug effects , Mitogens , Animals , Cell Membrane/drug effects , Concanavalin A/pharmacology , DNA/metabolism , In Vitro Techniques , Lymphocytes/metabolism , Phytohemagglutinins/pharmacology , Rats , Thymidine/metabolism , Time FactorsSubject(s)
Cardiolipins/immunology , Haptens , Phosphatidylinositols/immunology , Animals , Cattle , Complement Fixation Tests , Cross Reactions , Mice , Rabbits/immunologySubject(s)
Cell Membrane , Animals , Antibodies , Biophysical Phenomena , Biophysics , Cell Membrane/metabolism , Cell Movement , Chemical Phenomena , Chemistry , Cricetinae , Humans , Lectins , Membrane Lipids/metabolism , Membrane Proteins/metabolism , Membranes, Artificial , Mice , Models, Biological , Receptors, Drug , Rhodopsin/metabolism , Surface Properties , Thermodynamics , Time FactorsABSTRACT
Adsorption isotherm and enzymatic activity of protein interacting with the surface of solid carrier formed by oriented fat lipid chains of differently oxidized phospholipids have been studied. It has been found that the appearance of peroxide groups in fat acid chains results in a twofold decrease of protein limiting adsorption on the lipid monolayer. The data on enzymatic activity of proteins at variously filled suface with protein molecules indicate that the peroxide groups produce an activating effect under the conditions when protein interactions can be neglected. Superoxidation of phospholipid fat acids is suggested to be one of the mechanisms involved in the control of the processes proceeding on the membranes.