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Title: Burn-induced enhancement of mRNA of lysosomal cathepsins in skeletal muscle

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6079440

A localized burn injury to a rat hindlimb results in atrophy of soleus muscle (in the absence of cellular damage) which is attributable to an increase in muscle protein breakdown. Previous work has shown that lysosomal enzyme activities (cathepsins B, L, and D) are elevated in muscle from the burned leg by 50% to 100%. Activities are only slightly elevated by 1 day postburn but are maximal by 2 days. Incubation of muscles in the presence of /sup 3/H-mannose show that microsomal glycoprotein synthesis is specifically elevated by 1 day postburn. To determine the cause of the increased protein synthesis, total RNA was extracted from muscles of burned and control legs and electrophoresed in agarose. Northern blots of these samples were hybridized to nick translated cDNA clones which were obtained from several sources. Quantitative analysis of autoradiograms indicated that mRNA of cathepsin B was elevated 5 to 30 fold by one day postburn and remained high during the next two days. Changes in cathepsin D mRNA was less marked. The increased mRNA levels correlate in time with the increased protein synthesis in the microsomal glycoprotein fraction, but precede the increase in cathepsin activity. These results indicate that burns increase the synthesis of lysosomal proteases in skeletal muscle by increasing the level of cathepsin mRNA.

Research Organization:
Louisiana State Univ. Medical Center, New Orleans
OSTI ID:
6079440
Report Number(s):
CONF-870644-; TRN: 87-037130
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 46:6; Conference: 78. annual meeting of the American Society of Biological Chemists conference, Philadelphia, PA, USA, 7 Jun 1987
Country of Publication:
United States
Language:
English