Phosphorylation pattern of liver proteins during the early stages of the acute-phase response.

Authors

  • Roberta Piccoletti,

    1. Istituto di Patologia Generale, Universita degli Studi di Milano; Centro Studio Patologia Cellulare CNR, Via Mangiagalli 31, 20133 MILANO, Italy.
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  • Paola Bendinelli,

    1. Istituto di Patologia Generale, Universita degli Studi di Milano; Centro Studio Patologia Cellulare CNR, Via Mangiagalli 31, 20133 MILANO, Italy.
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  • Danilo Arienti,

    1. Istituto di Patologia Generale, Universita degli Studi di Milano; Centro Studio Patologia Cellulare CNR, Via Mangiagalli 31, 20133 MILANO, Italy.
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  • Paola Maroni,

    1. Istituto di Patologia Generale, Universita degli Studi di Milano; Centro Studio Patologia Cellulare CNR, Via Mangiagalli 31, 20133 MILANO, Italy.
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  • Aldo Bernelli-Zazzera

    1. Istituto di Patologia Generale, Universita degli Studi di Milano; Centro Studio Patologia Cellulare CNR, Via Mangiagalli 31, 20133 MILANO, Italy.
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Abstract

Liver preparations from turpentine-treated rats show an increased capacity to autophosphorylate a protein of 32.5 kDa (p 32.5): both the kinase and the substrate protein are strongly bound to the membrane fraction, but the protein is released to the cytosol after phosphorylation, which occurs exclusively in serine residues. No known second messenger-dependent protein kinase seems to be responsible for the reaction. Phosphorylation of p 32.5 could be an early post-receptorial event after turpentine-treatment possibly caused by cytokines and involved in the pathogenesis of further events of the acute-phase response.

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