ABSTRACT
The supernatant obtained from the mouse thymocytes incubated with oligopeptide thymic factor can partially restore autorosette formation in heated at 45 degrees C and washed thymocytes which have lost the receptors for autologous erythrocytes. It is supposed that decreased level of autorosette formation after treatment of thymocytes with thymic factor is caused by shedding of receptors for autologous erythrocytes.
Subject(s)
Erythrocytes/immunology , Receptors, Immunologic/immunology , Rosette Formation , T-Lymphocytes/immunology , Thymic Factor, Circulating/pharmacology , Thymus Hormones/pharmacology , Animals , Cells, Cultured , Mice , OligopeptidesSubject(s)
Antibody Formation/drug effects , Oligopeptides/pharmacology , Receptors, Cell Surface/drug effects , T-Lymphocytes/drug effects , Thymus Gland/immunology , Animals , Erythrocytes/immunology , Mice , Mice, Inbred CBA , Oligopeptides/isolation & purification , Receptors, Cell Surface/immunology , Receptors, Cell Surface/isolation & purification , Rosette Formation , Solubility , T-Lymphocytes/immunologyABSTRACT
A receptor structure that has an affinity to autologous and xenogenic red blood cells was isolated from rat thymocytes by means of adsorption on immobilized rabbit IgG. This structure restores the rosette formation on addition to thymocytes deprived of their receptors for autologous red blood cells and having no capacity for rosette formation. The substance affinity for red blood cells and rabbit IgG is caused by its glycoprotein with a molecular weight of 12 000 daltons, that displays the properties inherent in thymocyte Fc-receptors. The purified glycoprotein can also restore rosette formation in thymocytes deprived of their receptors for autologous red blood cells. A suggestion is made that at least one of Fc-receptors of the T-lymphocyte membrane is capable of reacting with red blood cells.
Subject(s)
Erythrocytes/immunology , Glycoproteins/immunology , Receptors, Fc/analysis , Receptors, Immunologic/analysis , T-Lymphocytes/analysis , Animals , Glycoproteins/analysis , Hemagglutination , Rats , Rosette FormationABSTRACT
Some properties of glycoprotein isolated from rat thymocytes were studied. The glycoprotein (its molecular weight is found to be about 12000 Daltons) has an affinity for autologous and xenogenous red blood cells as well as for Fc portion of IgG. It is shown that the glycoprotein belongs to the thymocyte plasma membrane receptors responsible for interaction with erythrocytes and possesses the Fe receptor properties. The data give reason to conclude that at least one of the Fc receptors has the affinity for SRBC, ARBC and Fe portion of IgG.
