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  • Cell & Developmental Biology  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    The role of erythropoietin in the production of principal erythrocyte proteins other than hemoglobin during terminal erythroid differentiation (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 126 (1986), S. 259-265 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Erythropoietin (EP) controls the terminal phase of differentiation in which proerythroblasts and their precursors, the colony forming units-erythroid (CFU-e), develop into erythrocytes. Biochemical studies of this hormone-directed terminal differentiation have been hindered by the lack of a homogeneous population of erythroid cells at the developmental stages of CFU-e and proerythroblasts that will synchronously differentiate in response to EP. Such a population of cells can be prepared from the spleens of mice with the acute erythroblastosis resulting from infection with anemia-inducing Friend virus (FVA). Using these FVA-infected erythroid cells, which were induced to differentiate with EP, four proteins other than hemoglobin that have key functions in mature erythrocytes were monitored during the 48-hour period of terminal differentiation. Synthesis of spectrin and membrane band 3 proteins were determined by immunoprecipitation and SDS-polyacrylamide gel electrophoresis; accumulation of the cytoskeletal protein band 4.1 was monitored by immunoblotting; carbonic anhydrase activity was measured electro-metrically. Band 3 synthesis and band 4.1 accumulation could be detected only after exposure of the cells to EP. Spectrin synthesis was ongoing prior to culture with EP, but it did increase after exposure to the hormone. Carbonic anhydrase-specific activity changed very little throughout the terminal differentiation process. These results reveal at least three patterns of production of principal erythrocyte proteins during EP-mediated terminal differentiation of FVA-infected erythroid cells. Depending on the specific protein examined, de novo synthesis can be induced by EP, an ongoing production can be enhanced by EP, or the production of a protein can be completed at a developmental stage prior to EP-mediated differentiation in these cells.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041260216
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Monolayer freeze-fracture - a modified procedure (1986)
    New York, NY : Wiley-Blackwell
    Journal of Electron Microscopy Technique 3 (1986), S. 439-451 
    Details
    ISSN: 0741-0581
    Keywords: Monolayer freeze-fracture ; Trans-membrane proteins ; Erythrocyte membrane proteins ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Monolayer freeze-fracture of biological membranes is a valuable tool for integrating membrane morphology with biochemical analysis of membrane components. This correlation has been restricted by the purity of the biochemical sample. In this article, the method is reviewed, and an improved method is described. The essential modification was the use of a polysaccharide-coated microscope slide, instead of a copper plate, to cover cells attached to a polylysine-coated coverslip. It was found that proper freeze-fracture will not occur unless there is a distinct temperature gradient, with its accompanying stresses, across the cell monolayer during the freezing process. This gradient is achieved by using glass slides of different thickness to cover each side of the monolayer. Comparison of the results with those obtained when using a copper-glass system demonstrated a consistently purer sample for the glass-glass system, with whole-cell contamination of the external membrane leaflet being reduced to 0.4%. Problems associated with obtaining pure samples for biochemical analysis are discussed, and the results of freeze-fracture with the glass-glass and glass-copper systems are compared. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of polypeptides associated with the separate halves of the erythrocyte membrane demonstrated that band 3, the anion transport protein, separates with the cytoplasmic face, whereas only sialoglycoproteins and their fragments are retained in the external face. This finding, obtained with the glass-glass system, is consistent with results of our earlier freeze-fracture study that used a copper-glass system which showed that covalent bonds may be broken during this procedure.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1060030407
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    Paper (German National Licenses)
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