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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 32 (1919), S. 637-679 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 125 (1985), S. 608-612 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Cultured myeloid leukemia cells display transferrin receptors but decrease receptor display after differentiation induction or accumulation of intracellular iron. To determine whether regulation of transferrin receptors and ferritin were linked under these disparate conditions, serum-free and fetal bovine serum (FBS) cultures of HL60 promyelocytic leukemia cells were used to investigate relationships between transferrin receptor display and intracellular ferritin. Using 125I- transferrin binding and immunofluorescence staining for transferrin receptors, HL60 cells cultured in serum-free, transferrin-free medium expressed fewer transferrin receptors and contained increased ferritin when compared to cells cultured with FBS or transferrin supplemented, serum-free medium. When placed in medium containing transferrin, cells previously grown in transferrin-free medium rapidly re-expressed transferrin receptors and decreased their ferritin content. HL60 cells induced to differentiate into granuiocytes or macrophages also decreased transferrin receptor display and increased their ferritin content. Transferrin receptor display and ferritin content in both proliferating and differentiating myeloid leukemia cells are inversely related and their regulation is closely linked. Regulation of transferrin receptor display and ferritin synthesis may be important events regulating myeloid cell growth and differentiation.
    Additional Material: 1 Ill.
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  • 3
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The human T cell-derived cytokines interleukin (IL)-3, granulocyte-macrophage colony-stimulating factor (CM-CSF), and IL-5 were examined for their ability to bind specifically to human basophils and to regulate their function. Scatchard analysis of equilibrium binding studies showed that IL-3 and GM-CSF, bound to basophils with apparent dissociation constants (KD) = 8 × 10-11M and 3.9 × 10-11M, respectively. Specificity studies under conditions that prevent receptor internalization showed that the binding of IL-3, GM-CSF, and IL-5 was not inhibited by tumor necrosis factor (TNF)-α, IL-1β, interferon (IFN)-γ, or G-CSF. However, receptors for IL-3, GM-CSF, and IL-5 interacted with each other on the basophil membrane, showing a unique spectrum of cross-reactivity, with IL-3 competing for GM-CSF and IL-5 binding, whereas GM-CSF and IL-5 showed little or no competition for IL-3 binding. In order to relate the binding properties of these cytokines to function, they were tested for their ability to influence basophil histamine release in an IgE/anti-IgE-dependent system. We found a hierarchy in the stimulation of basophil with the order of potency being IL-3 〉GM-CSF 〉IL-5. In addition, IL-3 stimulated larger amounts of histamine release than GM-CSF or IL-5. The observation that IL-3 interacts with receptors for GM-CSF and IL-5 may have a bearing on its stronger functional effects and suggests a major role for IL-3 in the pathogenesis of hypersensitivity syndromes.
    Additional Material: 8 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    BioEssays 15 (1993), S. 667-674 
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Protein splicing is an extraordinary post-translational reaction that removes an intact central “spacer” domain (Sp) from precursor proteins (N-Sp-C) while splicing together the N- and C-domains of the precursor, via a peptide bond, to produce a new protein (N-C). All of the available data on protein splicing fit a model in which these intervening sequences excise at the protein level via a self-splicing mechanism. Several proteins have recently been discovered that undergo protein splicing, and in two such cases, the excised spacer protein is an endonuclease. Such endonucleases are capable of conferring genetic mobility upon the intervening sequences that encodes them. These intervening sequences define a new family of mobile genetic elements that are translated yet remain phenotypically silent by excising at the protein rather than the RNA level.
    Additional Material: 7 Ill.
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  • 5
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    Unknown
    Marine Biological Laboratory Archives (Woods Hole, Mass.)
    In:  Viktor Hamburger collection, Box 2, Folder 38, Marine Biological Laboratory Archives
    Publication Date: 2023-01-12
    Description: scholarship award
    Description: thin copy paper
    Description: Correspondence
    Keywords: Awards
    Repository Name: Woods Hole Open Access Server
    Language: English
    Type: Text
    Format: image/tiff
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  • 6
    facet.materialart.
    Unknown
    Marine Biological Laboratory Archives (Woods Hole, Mass.)
    In:  Viktor Hamburger collection, Box 2, Folder 38, Marine Biological Laboratory Archives
    Publication Date: 2023-01-12
    Description: scholarship award
    Description: thin copy paper
    Description: Correspondence
    Keywords: Awards
    Repository Name: Woods Hole Open Access Server
    Language: English
    Type: Text
    Format: image/tiff
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  • 7
    facet.materialart.
    Unknown
    Marine Biological Laboratory Archives (Woods Hole, Mass.)
    In:  Viktor Hamburger collection, Box 2, Folder 38, Marine Biological Laboratory Archives
    Publication Date: 2023-01-12
    Description: scholarship award
    Description: thin copy paper, torn edge
    Description: Correspondence
    Keywords: Awards
    Repository Name: Woods Hole Open Access Server
    Language: English
    Type: Text
    Format: image/tiff
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