Alterations in the mRNA levels of two metabolic enzymes in rat skeletal muscle during stretch-induced hypertrophy and disuse atrophy

1996 ◽  
Vol 431 (S6) ◽  
pp. 990-992 ◽  
Author(s):  
C. Brownson ◽  
P T Loughna
Keyword(s):  
Skeletal Muscle ◽  
Metabolic Enzymes ◽  
Mrna Levels ◽  
Disuse Atrophy ◽  
Rat Skeletal Muscle

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

1999 ◽  
Vol 87 (1) ◽  
pp. 90-96 ◽  
Author(s):  
Xiao-Yan Han ◽  
Wei Wang ◽  
Raili Myllylä ◽  
Paula Virtanen ◽  
Jarmo Karpakka ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Tibialis Anterior ◽  
Collagen Synthesis ◽  
Plantar Flexion ◽  
Mrna Level ◽  
Type I ◽  
Mrna Levels ◽  
Rat Skeletal Muscle ◽  
Α Subunit ◽  
Fibrillar Collagens

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 α- and β-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 α-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.

Chromium Improves Protein Deposition Through Regulating the mRNA Levels of IGF-1, IGF-1R, and Ub in Rat Skeletal Muscle Cells

2009 ◽  
Vol 137 (2) ◽  
pp. 226-234 ◽  
Author(s):  
Zhongli Peng ◽  
Wei Qiao ◽  
Zhisheng Wang ◽  
Qiuzhong Dai ◽  
Jianhua He ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Mrna Levels ◽  
Rat Skeletal Muscle ◽  
Protein Deposition

scholarly journals Development of insulin sensitivity in rat skeletal muscle Studies of glucose transporter and insulin receptor mRNA levels

FEBS Letters ◽  
1992 ◽  
Vol 301 (1) ◽  
pp. 69-72 ◽  
Author(s):  
Shona Wallace ◽  
Gillian Campbell ◽  
Rachel Knott ◽  
Gwyn W. Gould ◽  
John Hesketh
Keyword(s):  
Skeletal Muscle ◽  
Insulin Sensitivity ◽  
Insulin Receptor ◽  
Glucose Transporter ◽  
Mrna Levels ◽  
Rat Skeletal Muscle ◽  
Receptor Mrna

scholarly journals Sepsis stimulates nonlysosomal, energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle.

1994 ◽  
Vol 94 (6) ◽  
pp. 2255-2264 ◽  
Author(s):  
G Tiao ◽  
J M Fagan ◽  
N Samuels ◽  
J H James ◽  
K Hudson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Mrna Levels ◽  
Rat Skeletal Muscle ◽  
Energy Dependent

scholarly journals Modulation of sodium-channel mRNA levels in rat skeletal muscle.

1987 ◽  
Vol 84 (23) ◽  
pp. 8721-8725 ◽  
Author(s):  
S. S. Cooperman ◽  
S. A. Grubman ◽  
R. L. Barchi ◽  
R. H. Goodman ◽  
G. Mandel
Keyword(s):  
Skeletal Muscle ◽  
Sodium Channel ◽  
Mrna Levels ◽  
Rat Skeletal Muscle

scholarly journals USP19 is a ubiquitin-specific protease regulated in rat skeletal muscle during catabolic states

2005 ◽  
Vol 288 (4) ◽  
pp. E693-E700 ◽  
Author(s):  
Lydie Combaret ◽  
Olasunkanmi A. J. Adegoke ◽  
Nathalie Bedard ◽  
Vickie Baracos ◽  
Didier Attaix ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Mass ◽  
De Novo ◽  
Deubiquitinating Enzyme ◽  
Mrna Levels ◽  
Deubiquitinating Enzymes ◽  
Rat Skeletal Muscle ◽  
Ubiquitin System ◽  
Specific Protease ◽  
Ubiquitin Specific Protease

Ubiquitin-dependent proteolysis is activated in skeletal muscle atrophying in response to various catabolic stimuli. Previous studies have demonstrated activation of ubiquitin conjugation. Because ubiquitination can also be regulated by deubiquitinating enzymes, we used degenerate oligonucleotides derived from conserved sequences in the ubiquitin-specific protease (UBP) family of deubiquitinating enzymes in RT-PCR with skeletal muscle RNA to amplify putative deubiquitinating enzymes. We identified USP19, a 150-kDa deubiquitinating enzyme that is widely expressed in various tissues including skeletal muscle. Expression of USP19 mRNA increased by ∼30–200% in rat skeletal muscle atrophying in response to fasting, streptozotocin-induced diabetes, dexamethasone treatment, and cancer. Increased mRNA levels during fasting returned to normal with refeeding, but 1 day later than the normalization of rates of proteolysis and coincided instead with recovery of muscle mass. Indeed, in all catabolic treatments, USP19 mRNA was inversely correlated with muscle mass and provided an index of muscle mass that may be useful in many pathological conditions, using small human muscle biopsies. The increased expression of this deubiquitinating enzyme under conditions of increased proteolysis suggests that it may play a role in regeneration of free ubiquitin either coincident with or after proteasome-mediated degradation of substrates. USP19 may also be involved in posttranslational processing of polyubiquitin produced de novo in response to induction of the polyubiquitin genes seen under these conditions. Deubiquitinating enzymes thus appear involved in muscle wasting and implicate a widening web of regulation of genes in the ubiquitin system in this process.

scholarly journals Regulation of myosin heavy-chain gene expression during skeletal-muscle hypertrophy

1989 ◽  
Vol 257 (3) ◽  
pp. 691-698 ◽  
Author(s):  
M Periasamy ◽  
P Gregory ◽  
B J Martin ◽  
W S Stirewalt
Keyword(s):  
Skeletal Muscle ◽  
Muscle Hypertrophy ◽  
Compensatory Hypertrophy ◽  
Chain Gene ◽  
Mrna Levels ◽  
Muscle Adaptation ◽  
Myosin Heavy Chain Gene ◽  
Rat Skeletal Muscle ◽  
Skeletal Muscle Hypertrophy ◽  
Myosin Isoenzymes

Changes in the myosin phenotype of differentiated muscle are a prominent feature of the adaptation of the tissue to a variety of physiological stimuli. In the present study the molecular basis of changes in the proportion of myosin isoenzymes in rat skeletal muscle which occur during compensatory hypertrophy caused by the combined removal of synergist muscles and spontaneous running exercise was investigated. The relative amounts of sarcomeric myosin heavy (MHC)- and light (MLC)-chain mRNAs in the plantaris (fast) and soleus (slow) muscles from rats was assessed with cDNA probes specific for different MHC and MLC genes. Changes in the proportion of specific MHC mRNA levels were in the same direction as, and of similar magnitude to, changes in the proportion of myosin isoenzymes encoded for by the mRNAs. No significant changes in the proportion of MLC proteins or mRNA were detected. However, high levels of MLC3 mRNA were measured in both normal and hypertrophied soleus muscles which contained only trace amounts of MLC3 protein. Small amounts of embryonic and neonatal MHC mRNAs were induced in both muscles during hypertrophy. We conclude that the change in the pattern of myosin isoenzymes during skeletal-muscle adaptation to work overload is a consequence of changes in specific MHC mRNA levels.

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