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Adaptation of the ubiquitin-proteasome proteolytic pathway in cancer cachexia

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Abstract

The ubiquitin-proteasome proteolytic pathway is of major importance in the breakdown of skeletal muscle proteins. The first step in this pathway is the covalent attachment of polyubiquitin chains to the targeted protein. Polyubiquitinylated proteins are then recognized and degraded by the 26S proteasome complex. In this review, we critically analyze recent findings in the regulation of ubiquitinylation of protein substrates and of their subsequent proteasome-dependent degradation in animal models of cancer cachexia. In particular, we discuss the influence of various mediators (anorexia, hormones, prostaglandins, cytokines, and proteolysis-inducing factor) in signaling the activation of ubiquitin-proteasome proteolysis in skeletal muscle. These findings have lead to new concepts that are starting to be used for preventing cachexia in cancer and other wasting diseases.

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Authors and Affiliations

  1. Centre de Recherche en Nutrition Humaine de Clermont-Ferrand, Institut National de la Recherche Agronomique, Unité d'Etude du Métabolisme Azoté, 63122, Ceyrat, France

    Didier Attaix, Lydie Combaret, Thomas Tilignac & Daniel Taillandier

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  1. Didier Attaix
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  2. Lydie Combaret
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  3. Thomas Tilignac
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  4. Daniel Taillandier
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Attaix, D., Combaret, L., Tilignac, T. et al. Adaptation of the ubiquitin-proteasome proteolytic pathway in cancer cachexia. Mol Biol Rep 26, 77–82 (1999). https://doi.org/10.1023/A:1006961919775

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