NDLI: Adaptation of the ubiquitin-proteasome proteolytic pathway in cancer cachexia

Content Provider	Springer Nature Link
Author	Attaix, Didier Combaret, Lydie Tilignac, Thomas Taillandier, Daniel
Copyright Year	1999
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.
Starting Page	77
Ending Page	82
Page Count	6
File Format	PDF
ISSN	03014851
Journal	Molecular Biology Reports
Volume Number	26
Issue Number	1-2
e-ISSN	15734978
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1999-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Animal Biochemistry Animal Anatomy / Morphology / Histology
Content Type	Text
Resource Type	Article
Subject	Genetics Medicine Molecular Biology

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Adaptation of the ubiquitin-proteasome proteolytic pathway in cancer cachexia