Journal of Applied Physiology Journal of Applied Physiology
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J Appl Physiol 87: 90-96, 1999;
8750-7587/99 $5.00
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Vol. 87, Issue 1, 90-96, July 1999

mRNA levels for alpha -subunit of prolyl 4-hydroxylase and fibrillar collagens in immobilized rat skeletal muscle

Xiao-Yan Han1, Wei Wang1, Raili Myllylä2, Paula Virtanen3, Jarmo Karpakka3, and Timo E. S. Takala1

1 Neuromuscular Research Center and Department of Biology of Physical Activity, University of Jyväskylä, FIN-40351 Jyväskylä; and Departments of 2 Biochemistry and 3 Physiology, Division of Sports Medicine, University of Oulu, FIN-90220 Oulu, Finland

There is evidence that immobilization causes a decrease in total collagen synthesis in skeletal muscle within a few days. In this study, early immobilization effects on the expression of prolyl 4-hydroxylase (PH) and the main fibrillar collagens at mRNA and protein levels were investigated in rat skeletal muscle. The right hindlimb was immobilized in full plantar flexion for 1, 3, and 7 days. Steady-state mRNAs for alpha - and beta -subunits of PH and type I and III procollagen, PH activity, and collagen content were measured in gastrocnemius and plantaris muscles. Type I and III procollagen mRNAs were also measured in soleus and tibialis anterior muscles. The mRNA level for the PH alpha -subunit decreased by 49 and 55% (P < 0.01) in gastrocnemius muscle and by 41 and 39% (P < 0.05) in plantaris muscle after immobilization for 1 and 3 days, respectively. PH activity was decreased (P < 0.05-0.01) in both muscles at days 3 and 7. The mRNA levels for type I and III procollagen were decreased by 26-56% (P < 0.05-0.001) in soleus, tibialis anterior, and plantaris muscles at day 3. The present results thus suggest that pretranslational downregulation plays a key role in fibrillar collagen synthesis in the early phase of immobilization-induced muscle atrophy.

muscle atrophy; hydroxyproline; pretranslational control; posttranslational modification


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