Immunocytochemical localization of acetylated alpha-tubulin in mouse resident peritoneal macrophages.

Antibodies which recognize tubulin, actin and vimentin were used to localize microtubules, microfilaments and intermediate filaments, respectively, in whole Triton X-100 extracted macrophages. The cytoskeleton components were seen by transmission electron microscopy of cells labeled with secondary antibodies coupled to colloidal gold particles. All microtubules were labeled with a monoclonal antibody which recognizes alpha tubulin. In addition, few were labeled with an antibody recognizing acetylated alpha tubulin.

Further studies on the cytoskeleton of resident, stimulated and activated macrophages.

The three-dimensional organization of the cytoskeleton of resident, thioglycolate-elicited and activated macrophages was studied by indirect immunofluorescence microscopy and by transmission electron microscopy of platinum-carbon replicas of Triton X-100 extracted cells and whole extracted cells critical point dried. Examination of the replicas showed with great clarity the organization of cytoplasmic filaments and microtubules. Cytoskeletal preparations revealed filamentous structures around the centrioles, and dense granules dispersed within the lattice of filaments of activated macrophages. X-ray microanalysis showed that they concentrate osmium. Indirect immunofluorescence microscopy revealed filamentous and/or dispersed tubulin, actin, vimentin and myosin-containing structures in the cytoplasm of the macrophages.

Further studies on the cytoskeleton of resident, stimulated and activated macrophages.

The three-dimensional organization of the cytoskeleton of resident, thioglycolate-elicited and activated macrophages was studied by indirect immunofluorescence microscopy and by transmission electron microscopy of platinum-carbon replicas of Triton X-100 extracted cells and whole extracted cells critical point dried. Examination of the replicas showed with great clarity the organization of cytoplasmic filaments and microtubules. Cytoskeletal preparations revealed filamentous structures around the centrioles, and dense granules dispersed within the lattice of filaments of activated macrophages. X-ray microanalysis showed that they concentrate osmium. Indirect immunofluorescence microscopy revealed filamentous and/or dispersed tubulin, actin, vimentin and myosin-containing structures in the cytoplasm of the macrophages.

Distribution of elastic system fibers in hyaline and fibrous cartilages of the rat.

Rat hyaline and fibrous cartilages whose glycosaminoglycans had been removed by hyaluronidase digestion were studied by comparing the ultrastructural features with the observation of sections stained by selective methods for elastic system fibers under the light microscope. Except for the fibrous layer in the perichondrium of tracheal hyaline cartilage, where elastic fibers were found, no elastic fibers could be detected in the cartilages studied. However, cartilaginous tissues contained oxytalan and elaunin fibers. A distinct pattern of distribution of the above-mentioned elastic-related fibers could be observed in both kinds of cartilages. Hyaline cartilages possess oxytalan fibers in the extracellular matrix that surrounds the chondrocytes, whereas elastic fibers were localized in the fibrous layer of the perichondrium that encloses the cartilage. Elaunin fibers could be detected in the transition (chondrogenic) layer adjacent to the perichondrium. The methods used disclosed the presence of oxytalan and elaunin fibers running along the periphery of the collagen bundles in fibrocartilage.