Increased mRNA levels for components of the lysosomal, Ca2+-activated, and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients
| Autor: | Yves Boirie, Bernard Beaufrère, E. Aurousseau, Odile Mansoor, Cécile Rallière, Maurice Arnal, Didier Attaix, Daniel Taillandier, Pierre Schoeffler |
|---|---|
| Přispěvatelé: | Service de Réanimation, Hôpital Robert Debré, Centre de Recherche en Nutrition Humaine, Laboratoire de Nutrition Humaine, Centre de Recherche en Nutrition Humaine, Université d'Auvergne - Clermont-Ferrand I (UdA), UR 0551 Laboratoire d'étude du Métabolisme azoté, Institut National de la Recherche Agronomique (INRA), UR 0551 CL THEIX METAB AZO Laboratoire d'étude du Métabolisme azoté, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Clermont Université, Université d'Auvergne (Clermont Ferrand 1) (UdA) |
| Rok vydání: | 1996 |
| Předmět: |
Male
muscle [SDV]Life Sciences [q-bio] protéine myofibrillaire Gene Expression Cathepsin D 0302 clinical medicine Ubiquitin Reference Values Craniocerebral Trauma adaptation métabolique 0303 health sciences Multidisciplinary biology protein breakdown Glyceraldehyde-3-Phosphate Dehydrogenases Interleukin muscle squelettique Calpain homme Cysteine Endopeptidases Protein catabolism medicine.anatomical_structure activité protéolytique 030220 oncology & carcinogenesis Female calpain Research Article Adult Proteasome Endopeptidase Complex medicine.medical_specialty 03 medical and health sciences Multienzyme Complexes Internal medicine medicine Humans cathepsin RNA Messenger human Muscle Skeletal Ubiquitins 030304 developmental biology Interleukin-6 Tumor Necrosis Factor-alpha Skeletal muscle Blotting Northern proteasome voluntary muscle Endocrinology Proteasome biology.protein Calcium Lysosomes Myofibril Interleukin-1 |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 1996, 93 (7), pp.2714-2718. ⟨10.1073/pnas.93.7.2714⟩ Proceedings of the National Academy of Sciences of the United States of America, 1996, 93 (7), pp.2714-2718. ⟨10.1073/pnas.93.7.2714⟩ |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.93.7.2714 |
| Popis: | The cellular mechanisms responsible for enhanced muscle protein breakdown in hospitalized patients, which frequently results in lean body wasting, are unknown. To determine whether the lysosomal, Ca2+-activated, and ubiquitin-proteasome proteolytic pathways are activated, we measured mRNA levels for components of these processes in muscle biopsies from severe head trauma patients. These patients exhibited negative nitrogen balance and increased rates of whole-body protein breakdown (assessed by [13C]leucine infusion) and of myofibrillar protein breakdown (assessed by 3-methylhistidine urinary excretion). Increased muscle mRNA levels for cathepsin D, m-calpain, and critical components of the ubiquitin proteolytic pathway (i.e., ubiquitin, the 14-kDa ubiquitin-conjugating enzyme E2, and proteasome subunits) paralleled these metabolic adaptations. The data clearly support a role for multiple proteolytic processes in increased muscle proteolysis. The ubiquitin proteolytic pathway could be activated by altered glucocorticoid production and/or increased circulating levels of interleukin 1beta and interleukin 6 observed in head trauma patients and account for the breakdown of myofibrillar proteins, as was recently reported in animal studies. |
| Databáze: | OpenAIRE |
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