Protéolyse musculaire ubiquitine-protéasome dépendante
| Autor: | E. Aurousseau, Daniel Larbaud, Thomas Tilignac, Cécile Rallière, Anthony J. Kee, Didier Attaix, Daniel Taillandier, Bertrand Souweine, Lydie Combaret |
|---|---|
| Přispěvatelé: | Unité de nutrition et métabolisme protéique, Institut National de la Recherche Agronomique (INRA), Revues Inra, Import |
| Jazyk: | angličtina |
| Rok vydání: | 1998 |
| Předmět: |
Proteasome Endopeptidase Complex
Proteolysis [SDV]Life Sciences [q-bio] Muscle Proteins 03 medical and health sciences 0302 clinical medicine Ubiquitin Multienzyme Complexes [SDV.BDD] Life Sciences [q-bio]/Development Biology Gene expression Endopeptidases medicine Animals Humans Muscle Skeletal Ubiquitins [SDV.BDD]Life Sciences [q-bio]/Development Biology [SDV.BDLR] Life Sciences [q-bio]/Reproductive Biology ComputingMilieux_MISCELLANEOUS 030304 developmental biology Muscle protein chemistry.chemical_classification 0303 health sciences medicine.diagnostic_test Ubiquitin proteasome biology Skeletal muscle [SDV.BDLR]Life Sciences [q-bio]/Reproductive Biology 3. Good health [SDV.AEN] Life Sciences [q-bio]/Food and Nutrition Cysteine Endopeptidases Enzyme medicine.anatomical_structure Proteasome Biochemistry chemistry 030220 oncology & carcinogenesis biology.protein [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition |
| Zdroj: | Reproduction Nutrition Development Reproduction Nutrition Development, EDP Sciences, 1998, 38, pp.153-165. ⟨10.1051/rnd:19980202⟩ Europe PubMed Central Reproduction Nutrition Development, EDP Sciences, 1998, 38 (2), pp.153-165 Scopus-Elsevier |
| ISSN: | 0926-5287 1297-9708 |
| DOI: | 10.1051/rnd:19980202⟩ |
| Popis: | 3 tables 2 graph.; International audience; The ubiquitin-proteasome proteolytic pathway has recently been reported to be 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. Polyubiquitylated proteins are then recognized and degraded by the 26S proteasome complex. In this review, we critically analyse recent findings in the regulation of this pathway, both in animal models of muscle wasting and in some human diseases. The identification of regulatory steps of ubiquitin conjugation to protein substrates and/or of the proteolytic activities of the proteasome should lead to new concepts that can be used to manipulate muscle protein mass. Such concepts are essential for the development of anti-cachectic therapies for many clinical situations. |
| Databáze: | OpenAIRE |
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