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(Received for publication, February 26, 1996, and in revised form, July 12, 1996)
From the Department of Cell Biology, Harvard Medical School,
Boston, Massachusetts 02115
Recent studies have suggested that activation of
the ubiquitin-proteasome pathway is primarily responsible for the rapid
loss of muscle proteins in various types of atrophy. The present
studies were undertaken to test if different classes of muscle proteins
are degraded by this pathway. In extracts of rabbit psoas muscle, the
complete degradation of soluble proteins to amino acids was stimulated
up to 6-fold by ATP. Peptide aldehyde inhibitors of the
proteasome or the removal of proteasomes markedly inhibited only the
ATP-dependent process. Addition of purified myosin, actin,
troponin, or tropomyosin to these extracts showed that these proteins
served as substrates for the ubiquitin-proteasome pathway. By
contrast, degradation of myoglobin did not require ATP, proteasomes, or
any known proteases in muscles.
When myosin, actin, and troponin were added as actomyosin complexes or
as intact myofibrils to these extracts, they were not hydrolyzed at a
significant rate, probably because in these multicomponent complexes,
these proteins are protected from degradation. Accordingly, actin (but
not albumin or troponin) inhibited the degradation of
125I-myosin, and actin was found to selectively inhibit
ubiquitin conjugation to 125I-myosin. Also, the presence of
tropomyosin inhibited the degradation of 125I-troponin.
However, neither actin nor tropomyosin inhibited the degradation of
125I-lysozyme or soluble muscle proteins. Thus, specific
interactions between the myofibrillar proteins appear to protect them
from ubiquitin-dependent degradation, and the rate-limiting
step in their degradation is probably their dissociation from the
myofibril.
Volume 271, Number 43,
Issue of October 25, 1996
pp. 26690-26697
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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