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The molecular regulation of protein breakdown following burn injury is different in fast- and slow-twitch skeletal muscle. 1998

C H Fang, and B G Li, and G Tiao, and J J Wang, and J E Fischer, and P O Hasselgren
Department of Surgery, University of Cincinnati, and Shriners Burns Institute, Cincinnati, OH, USA.

We compared the effect of burn injury on the energy-ubiquitin-dependent proteolytic pathway in the fast-twitch extensor digitorum longus (EDL) and the slow-twitch soleus muscle in rats. Rats were subjected to a 30% total body surface area full-thickness burn or sham procedure. At various time points after injury, total and myofibrillar protein breakdown rates were determined in incubated EDL and soleus muscles. The energy-dependent component of protein break-down was determined by incubating muscles in energy-depleting medium. Messenger RNA levels for ubiquitin and RC3, a 20S proteasome subunit, were measured by Northern blot analysis. Burn injury resulted in an approximately 50% increase in total protein breakdown and a 3-4 fold increase in myofibrillar protein breakdown in EDL muscles, and this response reflected increased energy-dependent protein breakdown. In contrast, protein breakdown rates were not significantly influenced by the burn injury in soleus muscles. Ubiquitin mRNA levels were increased almost 10-fold in EDL and approximately 4.5-fold in soleus muscles following burn injury. Burn injury resulted in a 2-fold increase in RC3 mRNA in EDL with no significant changes noted in soleus muscles. The results suggest that the more pronounced effect of burn injury on protein breakdown in fast-twitch than in slow-twitch muscle may reflect different regulation of proteolysis at the molecular level.

UI MeSH Term Description Entries
D008297 Male Males
D009097 Multienzyme Complexes Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES. Complexes, Multienzyme
D009124 Muscle Proteins The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN. Muscle Protein,Protein, Muscle,Proteins, Muscle
D002056 Burns Injuries to tissues caused by contact with heat, steam, chemicals (BURNS, CHEMICAL), electricity (BURNS, ELECTRIC), or the like. Burn
D003546 Cysteine Endopeptidases ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014452 Ubiquitins A family of proteins that are structurally-related to Ubiquitin. Ubiquitins and ubiquitin-like proteins participate in diverse cellular functions, such as protein degradation and HEAT-SHOCK RESPONSE, by conjugation to other proteins. Ubiquitin-Like Protein,Ubiquitin-Like Proteins,Protein, Ubiquitin-Like,Proteins, Ubiquitin-Like,Ubiquitin Like Protein,Ubiquitin Like Proteins
D017207 Rats, Sprague-Dawley A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company. Holtzman Rat,Rats, Holtzman,Sprague-Dawley Rat,Rats, Sprague Dawley,Holtzman Rats,Rat, Holtzman,Rat, Sprague-Dawley,Sprague Dawley Rat,Sprague Dawley Rats,Sprague-Dawley Rats
D046508 Culture Techniques Methods of maintaining or growing biological materials in controlled laboratory conditions. These include the cultures of CELLS; TISSUES; organs; or embryo in vitro. Both animal and plant tissues may be cultured by a variety of methods. Cultures may derive from normal or abnormal tissues, and consist of a single cell type or mixed cell types. Culture Technique,Technique, Culture,Techniques, Culture
D046988 Proteasome Endopeptidase Complex A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme. 20S Proteasome,Ingensin,Macropain,Macroxyproteinase,Multicatalytic Endopeptidase Complex,Multicatalytic Proteinase,Prosome,Proteasome,Complex, Multicatalytic Endopeptidase,Complex, Proteasome Endopeptidase,Endopeptidase Complex, Multicatalytic,Endopeptidase Complex, Proteasome,Proteasome, 20S,Proteinase, Multicatalytic

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