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Am J Physiol Regul Integr Comp Physiol 274: R30-R37, 1998;
0363-6119/98 $5.00
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Vol. 274, Issue 1, R30-R37, January 1998

Sepsis-induced increase in muscle proteolysis is blocked by specific proteasome inhibitors

Scott C. Hobler1,2, Greg Tiao1,2, Josef E. Fischer1,2, John Monaco3,4, and Per-Olof Hasselgren1,2

1 Shriners Burns Institute, Departments of 2 Surgery and 3 Molecular Genetics, University of Cincinnati, Cincinnati, Ohio 45267; and 4 Howard Hughes Medical Institute Research Laboratory, Chevy Chase, Maryland 20815

Recent studies suggest that sepsis stimulates ubiquitin-dependent protein breakdown in skeletal muscle. The 20S proteasome is the catalytic core of the ubiquitin-dependent proteolytic pathway. We tested the effects in vitro of the proteasome inhibitors N-acetyl-L-leucinyl-L-leucinal-L-norleucinal (LLnL) and lactacystin on protein breakdown in incubated muscles from septic rats. LLnL resulted in a dose- and time-dependent inhibition of protein breakdown in muscles from septic rats. Lactacystin blocked both total and myofibrillar muscle protein breakdown. In addition to inhibiting protein breakdown, LLnL reduced muscle protein synthesis and increased ubiquitin mRNA levels, probably reflecting inhibited proteasome-associated ribonuclease activity. Inhibited muscle protein breakdown caused by LLnL or lactacystin supports the concept that the ubiquitin-proteasome pathway plays a central role in sepsis-induced muscle proteolysis. The results suggest that muscle catabolism during sepsis may be inhibited by targeting specific molecular mechanisms of muscle proteolysis.

ubiquitin; N-acetyl-L-leucinyl-L-leucinal-L-norleucinal; lactacystin; 20S proteasome; catabolic


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