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Biomedical subjects

E Schmid

Publications and source records attributed to E Schmid.

At least 199 records · Page 11Linked to original sources
PubMed1982

Chromosome changes in lymphocytes after occupational exposure to toluene.

Cytogenetic analyses were carried out in peripheral lymphocytes from 20 male workers exposed only to toluene in a rotogravure plant for more than 16 years. As compared with a group of 24 unexposed controls, significantly higher yields of chromatid breaks, chromatid exchanges and gaps were observed. The number of SCEs was significantly increased in smoking and non-smoking toluene-exposed workers compared with the corresponding control groups.

Chemical Industry↗
PubMed1982

Desmoplakins of epithelial and myocardial desmosomes are immunologically and biochemically related.

Guinea pig antibodies against desmoplakins from bovine muzzle epidermis showed specific reaction in several epithelial tissues with desmoplakin I (Mr 250,000) and desmoplakin II (Mr 215,000). By immunofluorescence microscopy, prominent punctate staining was observed in various lines of cultured epithelial cells, revealing desmosomal junctions at sites of established cell-to-cell contacts as well as hemidesmosomes and internalized desmosome-derived membrane domains. On frozen tissue sections punctate staining was observed along plasma membranes of epithelial cells, and electron microscopy using the immunoperoxidase technique revealed that the antibodies were specifically localized at the plaques associated with desmosomes and hemidesmosomes. Of a large number of non-epithelial cells examined positive staining was only observed on desmosome-like junctions of myocardial cells and Purkinje fiber cells. In both epithelial and myocardial tissues the antibodies showed a broad range of cross-reactivity between diverse vertebrate species such as man, cow, rodent, and chicken, indicating that desmoplakins contain determinants strongly conserved during evolution. When binding of these antibodies to cytoskeletal polypeptides separated by gel electrophoresis and blotted on nitrocellulose paper sheets was examined, specific reaction was noted with desmoplakin I and, to a variable degree, also desmoplakin II from various epithelial cells. Reaction was also observed with a myocardial polypeptide from bovine and human hearts which had a similar Mr value (250,000) and isoelectric pH range as desmoplakin I. We conclude that desmoplakins are the major proteins present in the desmosomal plaques of both epithelial and myocardial cells and that the desmoplakin polypeptides present in these two different cell types are very similar, if not identical.

Animals↗
PubMed1981

Analysis of structural chromosome changes and SCE after occupational long-term exposure to electric and magnetic fields from 380 kV-systems.

Chromosome analyses were carried out in lymphocytes of 32 workers occupationally exposed for more than 20 years to 50 Hz alternating electric magnetic fields in 380 kV switchyards. As compared with a control group of 22 workers of similar age and occupation but without field exposure neither the yields of structural chromosome changes nor the SCE-frequencies were increased. The difference of cytogenetic data after occupational exposure to ionizing radiation is discussed.

Adult↗
PubMed1981

Vascular smooth muscle cells differ from other smooth muscle cells: predominance of vimentin filaments and a specific alpha-type actin.

Smooth muscle cells of the digestive, respiratory, and urogenital tracts contain desmin as their major, if not exclusive, intermediate-size filament constituent and also show a predominance of gamma-type smooth muscle actin. We have now examined smooth muscle tissue of different blood vessels (e.g., aorta, small arteries, arterioles, venules, and vena cava) from various mammals (man, cow, pig, rabbit, rat) by one- and two-dimensional gel electrophoresis of cell proteins and by immunofluorescence microscopy using antibodies to different intermediate-sized filament proteins. Intermediate-sized filaments of vascular smooth muscle cells contain abundant amounts of vimentin and little, if any, desmin. On gel electrophoresis, vascular smooth muscle vimentin appears as two isoelectric variants of apparent pI values of 5.30 and 5.29, shows the characteristic series of proteolytic fragments, and is one of the major cell proteins. Thus vimentin has been demonstrated in a smooth muscle cell present in the body. Vascular smooth muscle cells are also distinguished by the predominance of a smooth muscle-specific alpha-type actin, whereas gamma-type smooth muscle actin is present only as a minor component. It is proposed that the intermediate filament and actin composition of vascular smooth muscle cells reflects a differentiation pathway separate from that of other smooth muscle cells and may be related to special functions and pathological disorders of blood vessels.

Actins↗
PubMed1981

Antibodies to the major insoluble milk fat globule membrane-associated protein: specific location in apical regions of lactating epithelial cells.

Milk lipid globules of various species are surrounded by a membrane structure that is separated from the triglyceride core of the globule by a densely staining fuzzy coat layer of 10- to 50-nm thickness. This internal coat structure remains attached to the membrane during isolation and extraction with low- and high-salt buffers, is insoluble in nondenaturing detergents, and is enriched in an acidic glycoprotein (butyrophilin) with an apparent Mr of 67,000. Guinea pig antibodies against this protein, which show cross-reaction with the corresponding protein in some (goat) but not other (human, rat) species, have been used for localization of butyrophilin on frozen sections of various tissues from cow by immunofluorescence and electron microscopy. Significant reaction is found only in milk-secreting epithelial cells and not in other cell types of mammary gland and various epithelial tissues. In milk-secreting cells, the staining is restricted to the apical cell surface, including budding milk lipid globules, and to the periphery of the milk lipid globules contained in the alveolar lumina. These findings indicate that butyrophilin, which is constitutively secreted by surface budding in coordination with milk lipid production, is located at the apical surface and is not detected at basolateral surfaces, in endoplasmic reticulum, and in Golgi apparatus. This protein structure represents an example of a cell type-specific cytoskeletal component in a cell apex. It is suggested that this antigen provides a specific marker for the apical surface of milk-secreting cells and that butyrophilin is involved in the vectorial discharge of milk lipid globules.

Animals↗
PubMed1981

Isolation and characterization of desmosome-associated tonofilaments from rat intestinal brush border.

Epithelial cells of the small intestine, like those of other internal organs, contain intermediate-sized filaments immunologically related to epidermal prekeratin which are especially concentrated in the cell apex. Brush-order fractions were isolated from rat small intestine, and apical tonofilaments attached to desmosomal plaques and terminal web residues were prepared therefrom by extraction in high salt (1.5 M KCl) buffer and Triton X-100. The structure of these filaments was indistinguishable from that of epidermal tonofilaments and, as with epidermal prekeratin, filaments could be reconstituted from solubilized, denatured intestinal tonofilament protein. On SDS polyacrylamide gel electrophoresis of proteins of the extracted desmosome-tonofilament fractions, a number of typical brush-border proteins were absent or reduced, and enrichment of three major polypeptides of Mr 55,000, 48,000, and 40,000 was noted. On two-dimensional gel electrophoresis, the three enriched major polypeptides usually appeared as pairs of isoelectric variants, and the two smaller components (Mr 48,000, and 40,000) were relatively acidic (isoelectric pH values of 5.40 and below), compared to the Mr 55,000 protein which focused at pH values higher than 6.4. The tonofilament proteins were shown to be immunologically related to epidermal prekeratin by immunoreplica and blotting techniques using antibodies to bovine epidermal prekeratins. Similar major polypeptides were found in desmosome-attached tonofilaments from small intestine of mouse and cow. However, comparisons with epidermal tissues of cow and rat showed that all major polypeptides of intestinal tonofilaments were different from the major prekeratin polypeptides of epidermal tonofilaments. The results present the first analysis of a defined fraction of tonofilaments from a nonepidermal cell. The data indicate that structurally identical tonofilaments can be formed, in different types of cells, by different polypeptides of the cytokeratin family of proteins and that tonofilaments of various epithelia display tissue-specific patterns of their protein subunits.

Animals↗
PubMed1981

Antibodies to high molecular weight polypeptides of desmosomes: specific localization of a class of junctional proteins in cells and tissue.

Desmosome-enriched fractions were isolated from bovine muzzle epidermis either as desmosome-tonofilament complexes using a procedure involving treatment at pH9 or in the form of desmosomal residue fractions using a modification of the citric acid buffer (pH 2.3) method of Skerrow and Matoltsy [1]. Major polypeptides of high molecular weights (mol. wt.) were separated by gel electrophoresis, individual polypeptide bands were excised, and protein was eluted and used for immunization. Guinea pig antibodies raised against two prominent polypeptides of high mol. wt. (250,000 and 215,000) showed, on nitrocellulose paper blots of desmosome-tonofilament polypeptides separated by gel electrophoresis, extensive cross-reaction between a group or large polypeptides characteristic of desmosome-containing fractions, most notably polypeptides of 250 K, 215 K, 200 k, 175 K, and 164 K. These antibodies allowed, when used in immunofluorescence microscopy, the specific localization of desmosomal junctions (i) in sections through epithelia-containing tissue (e.g., epidermis, mucosae of tongue and esophagus, cornea, mammary gland, small intestine, liver, thymus, urothelium of bladder) and myocardium; (ii) on dissociated cells from these tissues; (iii) on various epithelial cells grown in culture; an (iv) in tumor-like proliferations of cultured epithelial cells injected into nude mice. Individual desmosomes could be visualized and resolved at the light microscopic level. No reaction was found in cells devoid of desmosomes and on other classes of intercellular junctions. Electron microscopic localization using immunoperoxidase techniques indicated that these proteins are located in, or close to, the desmosomal plague structure. It is proposed to use such antibodies against desmosomal proteins as markers specific to this so far only morphologically define class of junctions. Use of these markers will (i) improve identification and classification of intercellular junctions; (ii) facilitate determinations of the specific patterns of distributions of desmosomes and desmosomal protein in various cells and tissue; (iii) allow studies of formation and disintegration of desmosomes, and of the biosynthesis and possible recycling of their constituents; and (iv) provide tissue group-specific markers valuable in histology and diagnosis, especially for identification of epithelial and carcinoma cells.

Animals↗