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

被引:32
作者
Han, XY
Wang, W
Myllylä, R
Virtanen, P
Karpakka, J
Takala, TES
机构
[1] Univ Jyvaskyla, Dept Biol Phys Activ, FIN-40351 Jyvaskyla, Finland
[2] Univ Jyvaskyla, Neuromuscular Res Ctr, FIN-40351 Jyvaskyla, Finland
[3] Univ Oulu, Dept Biochem, Div Sports Med, FIN-90220 Oulu, Finland
[4] Univ Oulu, Div Physiol, Div Sports Med, FIN-90220 Oulu, Finland
关键词
muscle atrophy; hydroxyproline; pretranslational control; posttranslational modification;
D O I
10.1152/jappl.1999.87.1.90
中图分类号
Q4 [生理学];
学科分类号
071003 ;
摘要
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.
引用
收藏
页码:90 / 96
页数:7
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