Concurrent medullary and papillary thyroid carcinoma in the same thyroid lobe and in siblings.
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Biomedical subjects
Publications and source records attributed to S Stenman.
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Fibronectin is a glycoprotein found in body fluids, loose connective tissue matrix and in basement membranes. Fibronectin in rheumatoid arthritis synovial fluid was immunologically indistinguishable from the plasma form, as shown by double-diffusion analysis. Fibronectin isolated from rheumatoid synovial fluid by affinity chromatography on gelatin--Sepharose had a polypeptide pattern similar to that of plasma fibronectin in SDS--polyacrylamide gel electrophoresis. In fifty-one patients with rheumatoid arthritis and related diseases fibronectin concentrations is synovial fluid were 445 +/- 103 micrograms/ml (mean +/- SD) and within normal range, 335 +/- 52 micrograms/ml, in plasma. Immunofluorescence staining showed a prominent increase of fibronectin in the proliferating synovial connective tissue in rheumatoid arthritis as compared to normal synovial membrane. The results suggest an increased local production of fibronectin in rheumatoid synovial tissue.
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Fibronectin is a polymorphic glycoprotein of plasma, other body fluids and connective tissue, and it occurs in an insoluble and a soluble form. Insoluble fibronectin is found associated with basement membranes and in loose connective tissue matrix as well as in the pericellular matrix formed around cultured adherent cells, such as endothelial, fibroblastic and smooth muscle cells. In these positions fibronectin apparently functions as a substrate for cell attachment and as a scaffold for cell migration and movement. Soluble fibronectin, present e.g. in the circulation (300 micronm/ml) exhibits some important interations with other proteins. It is covalently cross-linked to fibrin during thrombus formation and binds to collagen. Fibronectin is released from platelets during their aggregation and soluble fibronectin potentiates the action of plasminogen activator. We have detected fibronectin in the sub-endothelium, in the matrix of smooth muscle cells of the media and in the adventitia of arteries. By using immunohistological techniques we have further found that fibronectin is prominent in atherosclerotic lesions of the intima, especially in developing fibrous plaques. Fibronectin was also prominent in experimentally induced atherosclerotic lesions. These findings suggest that fibronectin is an indicator of connective tissue formation in atherosclerotic processes and that the protein can have a role in their pathogenesis.
A disease characterized by massive tumorous cutaneous hyalinosis has been studied histologically, immunologically, and biochemically. The precipitated hyalin material differed from amyloid in being Congo-red-negative and ultrastructurally nonfibrillary. In lipoid proteinosis, massive hyalin deposits have not been encountered and the clinical course is distinct from the course of massive cutaneous hyalinosis. The clinical and histologic pictures of both adult and juvenile forms of colloid milium differed from that found in our patient, although the colloid milium in adult form is ultrastructurally also nonfibrillary like the hyalin from our patient. A strong humoral immune response to components of the cytoskeleton of fibroblasts and especially to keratin was found in our patient.
The supradiaphragmatic inferior vena cava was syngeneically transplanted into the infrarenal part of the abdominal aorta in rats of inbred strains. The initial histologic changes coincided with the changes usually seen in wound healing during the inflammatory phase and the phase of fibroplasia. Later the reparative process occurred predominantly in the luminal part of the vein wall, and was usually seen as intimal hyperplasia. In some grafts this process caused a narrowing of the lumen. In this particular experimental model the thickening of the intimal layer was mainly due to organization of fibrin layering thrombus. This was shown by detection of lamellar fibrin deposits and a high concentration of fibronectin in this layer. A large amount of fibronectin was detected in and around the proliferating fibroblasts and in thrombi. This explains the high concentration of fibronectin in the proliferating intimal layer of the graft.
The sequential appearance of fibronectin and collagenous proteins was studied by immunofluorescence in experimental granulation tissue in the mouse. Granulation tissue was induced by subcutaneous implantation of viscous cellulose sponges into the neck. When sponges were invaded by granulation tissue, fibronectin appeared early together with the invading fibroblasts. Interstitial collagens, type III and type I, appeared 2 to 7 days later. When the collagen had matured into bundles, fibronectin diminished or disappeared. The results suggest that fibronectin functions as a primary matrix for organization of the collagenous connective tissue during the tissue repair process.
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Cultured human glioma cells were studied by double indirect immunofluorescence technique using antisera against intermediate filaments and glial fibrillary acidic protein. With both antisera cytoplasmic fibrillar fluorescence was seen. Perinuclear bundles of intermediate-sized filaments, induced by vinblastine treatment, were strongly stained with both antisera. The degree of codistribution of the two types of antigenic determinants varied considerably from cell to cell. The results suggest that two types of filament-related antigenic determinants can be present in the same cell, and also that glial fibrillary acidic protein-related filaments may possess functional similarities to the intermediate filaments found in other cells. Glial fibrillary acidic protein remains as a useful and specific antigenic marker for the study of glial cells in vitro.
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Antibodies specific for cytoskeletal intermediate (10 nm) filaments reacted both with the hyaline deposits in alcoholic liver disease (Mallory bodies) and with perinuclear hyaline material of cultured hepatoma cells used as a model for hyaline formation in vitro. Our results suggest that disorganization and accumulation of intermediate filaments is an important step in the pathogenesis of alcoholic liver injury.
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The expression of fibronectin, a cell surface-associated transformation-sensitive glycoprotein, was studied in hetero- and homokaryons of normal and SV40-transformed human fibroblasts. In immunofluorescence, fibroblast homokaryons had an intense surface-associated and intracelluar fibronectin fluorescence similar to that of normal fibroblasts. Transformed cells and their homokaryons had a minimal surface-associated and a weak intracellular fibronectin fluorescence. In heterokaryons formed between transformed and normal fibroblasts, the expression of fibronectin fell within 24 h to the level of the transformed cell homokaryons. The change was detectable already at 3 h after fusion and was gene-dose dependent. These results show that the transformed genotype determines fibronectin expression in the heterokaryons.
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