Burn injury upregulates the activity and gene expression of the 20 S proteasome in rat skeletal muscle

Clinical Science

Volumn 99, Issue 3, 2000, Pages 181-187

  Fang, C H ^a   Li, B G ^a   Fischer, D R ^a   Wang, J J ^a   Runnels, H A ^a   Monaco, J J ^a   Hasselgren, P O ^a  

^a UNIVERSITY OF CINCINNATI   (United States)

Author keywords

Burn injury; Cachexia; Muscle; Proteasome; Proteolysis; Ubiquitin

Indexed keywords

MESSENGER RNA; PROTEASOME; UBIQUITIN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BURN; CACHEXIA; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBUNIT; GENE EXPRESSION REGULATION; MALE; NONHUMAN; NORTHERN BLOTTING; PRIORITY JOURNAL; PROTEIN DEGRADATION; RAT; RECEPTOR UPREGULATION; SKELETAL MUSCLE;

EID: 0033811417     PISSN: 01435221     EISSN: None     Source Type: Journal    
DOI: 10.1042/cs0990181     Document Type: Article

References (28)

1. Protein dynamics in skeletal muscle after trauma: Local and systemic effects
2. Influence of burn injury on protein metabolism in different types of skeletal muscle and the role of glucocorticoids
3. Burn injury stimulates multiple proteolytic pathways in skeletal muscle, including the ubiquitin-energy-dependent pathway
4. Proteasome blockers inhibit protein breakdown in skeletal muscle after burn injury in rats
5. The ubiquitin system
6. 2+-dependent systems
7. Role of the ubiquitin-proteasome pathway in sepsis-induced muscle catabolism
8. Pathways of muscle protein breakdown in injury and sepsis
9. Structure and functions of the 20 S and 26 S proteasomes
10. The metabolism of the albino rat during prolonged fasting at two different environmental temperatures
11. The molecular regulation of protein breakdown following burn injury is different in Fast- and slow-twitch skeletal muscle
12. Protein measurements with the folin phenol reagent
13. Purification and characterization of a multicatalytic high-molecular-mass proteinase from rat skeletal muscle
14. A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution
15. The activity and expression of the 20 S proteasome are increased in skeletal muscle during sepsis
16. Lactacystin and clastolactacystin β-lactone modify multiple proteasome β-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation
17. Molecular biology of proteasomes
18. Intermediates in the formation of mouse 20 S proteasomes: Implications for the assembly of precursor β subunits
19. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
20. Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes
21. Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy
22. Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting
23. Multicatalytic proteinase activity in skeletal muscle from starving rats
24. Muscle wasting in insulinopenic rats results from activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription
25. Intracellular regulation of protein degradation during sepsis is different in fast- and slow-twitch muscle
26. Phosphorylation of proteasomes in mammalian cells
27. Sepsis stimulates release of myofilaments in skeletal muscle by a calcium-dependent mechanism
28. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown