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1 Faculty of Biology, University of Konstanz, D-78457 Konstanz, Germany; and 2 Laboratoire de Plasticité Neuromusculaire, Université des Sciences et Technologies de Lille, F-59655 Villeneuve d'Ascq, France
Time-dependent changes in myosin heavy chain
(MHC) isoform expression were investigated in rat soleus muscle
unloaded by hindlimb suspension. Changes at the mRNA level were
measured by RT-PCR and correlated with changes in the pattern of MHC
protein isoforms. Protein analyses of whole muscle revealed that MHCI
decreased after 7 days, when MHCIIa had increased, reaching a transient maximum by 15 days. Longer periods led to inductions and progressive increases of MHCIId(x) and MHCIIb. mRNA analyses of whole muscle showed
that MHCIId(x) displayed the steepest increase after 4 days and
continued to rise until 28 days, the longest time period investigated.
MHCIIb mRNA followed a similar time course, although at lower levels.
MHCI
mRNA, present at extremely low levels in control soleus, peaked
after 4 days, stayed elevated until 15 days, and then decayed.
Immunohistochemistry of 15-day unloaded muscles revealed that MHCI
was present in muscle spindles but at low amounts also in extrafusal
fibers. The slow-to-fast transitions thus seem to proceed in the order
MHCI
MHCIIa
MHCIId(x)
MHCIIb. Our
findings indicate that MHCI
is transiently upregulated in some
fibers as an intermediate step during the transition from MHCI
to MHCIIa.
hindlimb suspension; messenger ribonucleic acid; myosin heavy chain isoforms; reverse transcriptase-polymerase chain reaction; slow-to-fast transition
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