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  • 1
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    Induction of interleukin 2 messenger RNA inhibited by cyclosporin A (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-12-21
    Description: Cyclosporin A blocked production of the lymphokine interleukin 2 by activated T lymphocytes. In a human and a murine cell line this inhibition reflected an absence of interleukin 2 messenger RNA. Under conditions in which these cells are normally stimulated to secrete high levels of interleukin 2, they failed to do so in the presence of cyclosporin A. In both cell lines this failure was accompanied by an absence of interleukin 2 messenger accumulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Elliott, J F -- Lin, Y -- Mizel, S B -- Bleackley, R C -- Harnish, D G -- Paetkau, V -- New York, N.Y. -- Science. 1984 Dec 21;226(4681):1439-41.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6334364" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cyclosporins/*pharmacology ; Humans ; Interleukin-2/biosynthesis/*genetics ; Mice ; Protein Biosynthesis/drug effects ; RNA, Messenger/*metabolism ; T-Lymphocytes/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
    Electronic Resource
    Electronic Resource
    An evolutionary model for the insect vitellins (1982)
    Springer
    Journal of molecular evolution 18 (1982), S. 405-413 
    Details
    ISSN: 1432-1432
    Keywords: Insect Vitellins ; Immunological crossreactivity ; Evolutionary model ; Amino acid composition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Insects can be divided into three groups based on the sizes of the polypeptide constituents of their vitellogenins and vitellins. In order to determine the relationships between these groups, antisera to the vitellins of seven insects from six taxonomic orders were used to assess immunological cross-reactivity. Antigenic relatedness was observed only between vitellins from species within the same family. Amino acid compositional data for vitellins from nine species were used to assess homology by difference matrices. The SΔQ values were similar for both intra-order and inter-order comparisons and strongly suggested relatedness. The SΔn comparisons supported the immunological data that indicated that the vitellins were evolving rapidly. For most insect vitellins there are two distinct size classes of polypeptides that seem to be derived from a single asymmetric proteolytic cleavage of a precursor. We propose a model that suggests that the different size polypeptides represent distinct domains and that in the evolution of the vitellogenin genes of the Diptera and Hymenoptera there has been domain elimination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01840888
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