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Am J Physiol Cell Physiol 277: C1044-C1049, 1999;
0363-6143/99 $5.00
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Vol. 277, Issue 6, C1044-C1049, December 1999

EDITORIAL FOCUS
Time-dependent changes in myosin heavy chain mRNA and protein isoforms in unloaded soleus muscle of rat

Laurence Stevens1,2, Karim R. Sultan1, Heidemarie Peuker1, Bärbel Gohlsch1, Yvonne Mounier2, and Dirk Pette1

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. MHCIalpha 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 MHCIalpha 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 MHCIbeta right-arrow MHCIIa right-arrow MHCIId(x) right-arrow MHCIIb. Our findings indicate that MHCIalpha is transiently upregulated in some fibers as an intermediate step during the transition from MHCIbeta to MHCIIa.

hindlimb suspension; messenger ribonucleic acid; myosin heavy chain isoforms; reverse transcriptase-polymerase chain reaction; slow-to-fast transition


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