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  • 1985-1989  (2)
  • 1980-1984
  • (Na++K+)-ATPase  (1)
  • Algae-fungi-Chrysochromulina  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular medicine 64 (1986), S. 786-792 
    ISSN: 1432-1440
    Keywords: Erythrocyte ; Heart muscle ; Receptor regulation ; (Na++K+)-ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The assumption that the red blood cell can be used as a model for ouabain receptor regulation in heart muscle has been tested using isolated tissues from humans, guinea pigs, and chickens. The following results were obtained: 1. The affinity of the ouabain receptor was similar in both human erythrocytes and right atrial appendage, but the density of binding sites was much lower on the erythrocytes. There was no correlation between the binding capacity in both tissues. 2. Ouabain receptor occupation was closely correlated with inhibition of Na+/K+-transport in human erythrocytes and chick heart nonmuscle cells in culture. In contrast, in chick heart muscle cells, an occupation of 40% of the receptors decreased the Na+/K+-transport rate by only 10%. 3. In hypokalemia, the ouabain binding capacity was increased in human and guinea pig erythrocytes but not in guinea pig heart muscle. Such increases were seen in chick heart nonmuscle cells in moderate hypokalemia but in heart muscle cells only after severe hypokalemia. Incubation of chick heart muscle cells in toxic but not in “therapeutic” ouabain concentrations increased the number of ouabain receptors. Increases in receptor number attenuated the positive inotropic and toxic actions of ouabain. These variations between ouabain receptor regulation in red blood cells and heart muscle of several species may be attributable to the lack of a “sodium pump reserve” in erythrocytes and heart nonmuscle cells. Such variations indicate that the human erythrocyte is not a suitable model for the ouabain receptor in the human heart.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-072X
    Keywords: Extracellular proteins ; Surface fibrils ; Algae-fungi-Chrysochromulina ; Immunocytochemistry ; Agglutination ; Fimoriae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An extensive network of extracellular fibrils was revealed by negative staining in the greenish gold algal flagellate, Chrysochromulina breviturrita. These fibrils were of uniform diameter (4–5 nm), sometimes exceeding 5 μm in length. In addition there were short, narrower fibrils (2–3 nm) on the surface of the flagella. Six protein bands were isolated from spent culture medium by SDS-PAGE and one of 80,000 Da was found to polymerize after dialysis into 4–5 nm fibrils identical to those found on the cell surface. Two other proteins of 58,000 Da and 65,000 Da also formed 4–5 nm fibrils but these were either rare or of a shorter length and different appearance. An antiserum directed against the surface 7 nm fibrils (fimbriae) of fungi agglutinated cells of C. breviturrita and some other Prymnesiophyceae and Chrysophyceae, but did not agglutinate cells of algal species in other groups. Immunofluorescence and protein A gold labelling confirmed that antigens related to fungal fimbriae were present on the surface of cells of C. breviturrita. Only the 80,000 and 58,000 Da proteins labelled heavily following protein A gold labelling. Some individual 4–5 nm fibrils labelled with gold were observed in the material prepared from the 80,000 Da band. These results therefore establish that C. breviturrita produces a surface network of fibrils that are serologically related to the fimbriae of fungi, and suggest a previously unrecognized relationship between members of the Prymnesiophyceae, Chrysophyceae and fungal groups.
    Type of Medium: Electronic Resource
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