ABSTRACT
The data on changes in expression of H-2 complex and Thy-1 antigens on cell surface of thymocytes resulting from their incubation with peritoneal macrophages has been presented. The process of joint cultivation of thymocytes with macrophages leads to significant decrease in number of cells with Thy-2-antigen and increase in that with H-2 complex antigens. An increase in H-2K+ cells in experimental thymocytes as compared to control ones was observed. No changes in H-2D expression was observed. A significant increase in Ia+ macrophages was observed after interaction with thymocytes as compared with intact mononuclear phagocytes.
Subject(s)
Antigens, Surface/analysis , H-2 Antigens/analysis , Histocompatibility Antigens Class II/analysis , Macrophages/immunology , T-Lymphocytes/immunology , Animals , Antigen-Presenting Cells/immunology , Cells, Cultured , Mice , Mice, Inbred C57BL , Mice, Inbred CBA , Thy-1 AntigensSubject(s)
Amyloidosis/drug therapy , Colchicine/therapeutic use , Adolescent , Adult , Amyloidosis/complications , Animals , Child , Familial Mediterranean Fever/complications , Female , Humans , Male , Mice , Mice, Inbred BALB CABSTRACT
Among different variants of immunoperoxidase method preference is given to its indirect variant with labeling of pure antibody with peroxidase by a two-step procedure. Examples of the use of this method for the detection of serum proteins, tissue antigens, and autoantibody are presented. The best results are achieved in treatment of sections with pure antibody instead of antisera.
Subject(s)
Immunoenzyme Techniques , Animals , Antibodies/isolation & purification , Antigens/analysis , Autoantibodies/analysis , Blood Proteins/analysis , Humans , Immunoglobulin G/analysis , Methods , Precipitin TestsABSTRACT
The indirect electron microscope immunoperoxidase method utilizing pure rabbit antibodies to protein of mouse amyloid fibrils was used for studying casein-induced amyloidosis in mice. At the early stages of amyloidosis there appeared deposits of fine granular material in the mouse myocardium. These deposits contained an antigen similar to the amyloid fibrils antigen, but the deposits had no fibrillar ultrastructure. The results testify to the presence of early nonfibrillar stage of amyloid formation.
Subject(s)
Amyloid/immunology , Antigens/analysis , Myocardium/immunology , Amyloidosis/immunology , Animals , Mice , Microscopy, Electron , Peroxidases/immunology , RabbitsABSTRACT
The immunomorphological Coons' method (its indirect variant) was used to discover specific amyloid protein AA in the organs of mice with experimental amyloidosis and normal mice (adult, newborn, embryo). The use of pure antiprotein-AA-antibodies allowed to reveal the minimal deposits of amyloid protein at the earliest stages of amyloidogenesis. The organs of normal mice (adult, newborn, embryo) did not contain this protein.
Subject(s)
Amyloid/deficiency , Amyloid/immunology , Amyloidosis/immunology , Animals , Animals, Newborn , Antibodies/analysis , Antibody Specificity , Fluorescent Antibody Technique , MiceABSTRACT
Early stages of amyloidogenesis were studied in mice with experimental amyloidosis. According to indirect Coons' method the cryostat sections of the spleens and other organs of mice were incubated first with pure rabbit fibrillar protein antiamyloid antibodies, and then with pure fluorescein-labeled foat antirabbit IgG antibodies. At the early period after 1--2 casein injections there appeared amyloid protein in the intercellular space and in the blood filling the spleen and liver sinuses. Formation of the typical amyloid deposits in the spleen were completed by the 5th--7th day of the experiment after 3--4 casein injections.
Subject(s)
Amyloid/biosynthesis , Amyloidosis/metabolism , Spleen/metabolism , Animals , Fluorescent Antibody Technique , Kidney/metabolism , MiceABSTRACT
Amyloid fibrillae yere isolated from the spleen of a patient with secondary amyloidosis and their antigenic specificity was demonstrated. Pure antibody to the specific amyloid antigen was obtained. The possibility of mmunomorphological detecton of amyloid in tissues was proven. Amyloid protein was found to be absent in normal organs of adults and embryos.
Subject(s)
Amyloid/immunology , Amyloidosis/immunology , Antigens/isolation & purification , Autoantigens/isolation & purification , Animals , Embryo, Mammalian/immunology , Epitopes , Female , Fluorescent Antibody Technique , Humans , Pregnancy , Rabbits , Spleen/immunologySubject(s)
Amyloid/analysis , Amino Acids/analysis , Amyloid/isolation & purification , Amyloidosis/metabolism , Animals , Autoanalysis , Humans , In Vitro Techniques , MiceABSTRACT
Electron-microscopic investigation carried out following the intravenous administration of ferritin revealed an increase in permeability of the myocardium capillary wall in mice in experimental casein amyloidosis. Additionally, a complex electron-microscopic, immunohistochemical and histological investigation of the development of amyloidosis in the myocardium of mice was conducted. It was established that deposits of typical amyloid in the myocardium of mice consisted of two ultrastructural components--granular material and fibrils. It was shown that formation of amyloid with characteristic tinctorial properties was preceded by depositions of specific antigen fibrils of granular ultrastructure.