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    Endotoxicosis Induced by Coxiella burnetii Lipopolysaccharide Stimulates a Ribosomal Protein S6 Kinase: Some Properties of the Partially Purified Enzyme

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    Picking_1989.pdf (1.229Mb)
    Issue Date
    1989-12
    Author
    Picking, William D.
    Hackstadt, T.
    Paretsky, D.
    Publisher
    American Society for Microbiology
    Type
    Article
    Article Version
    Scholarly/refereed, publisher version
    Published Version
    http://iai.asm.org/content/57/12/3683.long
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    Abstract
    Guinea pig endotoxicosis induced by lipopolysaccharide from Coxiella burnetii Nine Mile phase I stimulates phosphorylation of liver ribosomal protein S6, with a 50% increase at 12 h postinoculation. The responsible protein kinase (S6PK) has been partially purified from liver; its activity is independent of cyclic AMP and of Ca2+ plus phosphatidyl serine or diacylglycerol. The preparation has an apparent optimum concentration of 20 mM Mg2+, while Ca2+ and Mn2+ are each inhibitory at 2 mM. The apparent Km for ATP is 30 microM with intact ribosomes. Because of the central role of phosphorylation in metabolic regulation and a purported role of phosphorylated S6 in protein synthesis, the lipopolysaccharide-induced stimulation of S6PK suggests a significant regulatory role of such enzymes in the pathobiochemistry of Q fever infection and endotoxicosis.
    URI
    http://hdl.handle.net/1808/21321
    Collections
    • Pharmaceutical Chemistry Scholarly Works [327]
    Citation
    Picking, W. D., Hackstadt, T., & Paretsky, D. (1989). Endotoxicosis induced by Coxiella burnetii lipopolysaccharide stimulates a ribosomal protein S6 kinase: some properties of the partially purified enzyme. Infection and Immunity, 57(12), 3683–3688.

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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