Alterations of proteasome activities in skeletal muscle tissue of diabetic rats.
During the last years many investigations have shown that a major catalyst within the mechanism of skeletal muscle wasting occurring under conditions like sepsis, injuries, trauma, cancer cachexia, chronic acidosis, fasting, glucocorticoid treatment, and insulinopenia is the ubiquitin-proteasome system. Evidence for this was obtained by findings that the rate of ATP-dependent protein degradation is increased, that m-RNA concentrations of several proteasome subunits and ubiquitin are increased and the amount of ubiquitin-protein conjugates is elevated under these conditions. Additionally, the enhanced protein breakdown was shown to be suppressed by proteasome inhibitors. In the present report we show that most but not all of the proteolytic activities of partially purified 20S/26S proteasomes from skeletal muscle of rats increase after induction of Diabetes mellitus. This finding suggests that part of the mechanism of acceleration of muscle protein breakdown is due to changes in proteasome activities.
Merforth
S
S
Diabetes-Forschungsinstitut, Abteilung für Klinische Biochemie, Düsseldorf, Germany.
Osmers
A
A
Dahlmann
B
B
D000818:Animals; D002852:Chromatography, Ion Exchange; D003546:Cysteine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D003921:Diabetes Mellitus, Experimental / Q000201:enzymology*; D008297:Male; D009097:Multienzyme Complexes / Q000302:isolation & purification / Q000378:metabolism*; D009124:Muscle Proteins / Q000737:chemistry / Q000378:metabolism; D018482:Muscle, Skeletal / Q000201:enzymology*; D046988:Proteasome Endopeptidase Complex; D051381:Rats
D009097:Multienzyme Complexes; D009124:Muscle Proteins; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex