scholarly journals Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation

2005 ◽  
Vol 1752 (2) ◽  
pp. 166-176 ◽  
Author(s):  
Pamela Donoghue ◽  
Philip Doran ◽  
Paul Dowling ◽  
Kay Ohlendieck
Keyword(s):  
Skeletal Muscle ◽  
Differential Expression ◽  
Low Frequency ◽  
Fast Skeletal Muscle ◽  
Low Frequency Stimulation ◽  
Muscle Proteome ◽  
Frequency Stimulation

scholarly journals Muscle LIM protein is upregulated in fast skeletal muscle during transition toward slower phenotypes

2001 ◽  
Vol 280 (2) ◽  
pp. C273-C279 ◽  
Author(s):  
Raffaella Willmann ◽  
Justine Kusch ◽  
Karim R. Sultan ◽  
Achim G. Schneider ◽  
Dirk Pette
Keyword(s):  
Low Frequency ◽  
Hindlimb Suspension ◽  
Fast Skeletal Muscle ◽  
Experimental Conditions ◽  
Lim Protein ◽  
Protein Levels ◽  
Low Frequency Stimulation ◽  
Muscle Lim Protein ◽  
Frequency Stimulation ◽  
Fast Muscles

Muscle LIM protein (MLP) is constitutively expressed in slow, but undetectable in fast, muscles of the rat. Here we show that MLP was upregulated at both the mRNA and protein levels under experimental conditions leading to transitions from fast to slower phenotypes. Chronic low-frequency stimulation and mechanical overloading by synergist removal both induced fast-to-slow shifts in myosin heavy chain (MHC) isoforms and expression of MLP in fast muscles. High amounts of MLP mRNA and protein were also present in fast muscles of the myotonic, hyperactive ADR mouse. Hypothyroidism evoked shifts in myosin composition toward slower isoforms and increased the MLP protein content of soleus (SOL) muscle but failed to induce MLP in fast muscles. Unweighting by hindlimb suspension elicited slow-to-fast transitions in MHC expression without altering MLP levels in SOL muscle. Hyperthyroidism shifted the MHC pattern toward faster isoforms but did not affect MLP content in SOL muscle. We conclude that alterations in MLP expression are associated with transitions from fast to slower phenotypes but not with slow-to-fast muscle fiber transitions.

Selected Contribution: Low-frequency stimulation of fast muscle affects the abundance of Ca2+-ATPase but not its oligomeric status

2001 ◽  
Vol 90 (1) ◽  
pp. 371-379 ◽  
Author(s):  
Shona Harmon ◽  
Gabriele R. Froemming ◽  
Elmi Leisner ◽  
Dirk Pette ◽  
Kay Ohlendieck
Keyword(s):  
Skeletal Muscle ◽  
Protein Interactions ◽  
Low Frequency ◽  
Transition Process ◽  
Fast Muscle ◽  
Rapid Decline ◽  
Ion Pump ◽  
Low Frequency Stimulation ◽  
Frequency Stimulation ◽  
Rapid Stimulation

After chronic, low-frequency stimulation, a rapid decline in Ca2+ pump activity is observed during the early stages of skeletal muscle transformation. However, this variation in enzymatic activity does not coincide with a drastic reduction in the amount of sarcoplasmic reticulum Ca2+-ATPases. To investigate whether changes in subunit interactions within Ca2+ pump complexes contribute to this phenomena, we performed a chemical cross-linking analysis of 4 days continuously, and 4 days discontinuously, electrostimulated fast muscle fibers. The abundance of the slow and fast Ca2+-ATPase isoforms sarco(endo)plasmic reticulum Ca2+- ATPase types 1 and 2 was affected during the fast-to-slow transition process, demonstrating that, even after short-term stimulation, distinct changes in the isoform expression pattern of muscle proteins occur. However, the oligomeric status of both ion pump species did not change. Hence, chemical modifications of critical enzyme domains must be responsible for the rapid stimulation-induced activity changes, not variations in protein-protein interactions within Ca2+-ATPase units. Oligomerization appears to be of central importance to the proper physiological functioning of the Ca2+-ATPase and does not undergo changes during skeletal muscle conditioning.

scholarly journals Salbutamol and chronic low-frequency stimulation of canine skeletal muscle.

1996 ◽  
Vol 496 (1) ◽  
pp. 221-227 ◽  
Author(s):  
P Hu ◽  
K M Zhang ◽  
J J Feher ◽  
S W Wang ◽  
L D Wright ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Low Frequency ◽  
Low Frequency Stimulation ◽  
Frequency Stimulation ◽  
Stimulation Of

Changes of skeletal muscle proteases activities during a chronic low-frequency stimulation period

2001 ◽  
Vol 442 (5) ◽  
pp. 745-751 ◽  
Author(s):  
Matilde Parreño ◽  
Albert Pol ◽  
Joan Cadefau ◽  
Joan Parra ◽  
Luisa Alvarez ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Low Frequency ◽  
Low Frequency Stimulation ◽  
Frequency Stimulation ◽  
Stimulation Period

scholarly journals Calpain activity in fast, slow, transforming, and regenerating skeletal muscles of rat

2000 ◽  
Vol 279 (3) ◽  
pp. C639-C647 ◽  
Author(s):  
Karim R. Sultan ◽  
Bernd T. Dittrich ◽  
Dirk Pette
Keyword(s):  
Skeletal Muscle ◽  
Fiber Type ◽  
Low Frequency ◽  
Protein Isoforms ◽  
Calpain Activity ◽  
Adult Skeletal Muscle ◽  
Low Frequency Stimulation ◽  
Frequency Stimulation ◽  
Edl Muscle

Fiber-type transitions in adult skeletal muscle induced by chronic low-frequency stimulation (CLFS) encompass coordinated exchanges of myofibrillar protein isoforms. CLFS-induced elevations in cytosolic Ca2+ could activate proteases, especially calpains, the major Ca2+-regulated cytosolic proteases. Calpain activity determined by a fluorogenic substrate in the presence of unaltered endogenous calpastatin activities increased twofold in low-frequency-stimulated extensor digitorum longus (EDL) muscle, reaching a level intermediate between normal fast- and slow-twitch muscles. μ- and m-calpains were delineated by a calpain-specific zymographical assay that assessed total activities independent of calpastatin and distinguished between native and processed calpains. Contrary to normal EDL, structure-bound, namely myofibrillar and microsomal calpains, were abundant in soleus muscle. However, the fast-to-slow conversion of EDL was accompanied by an early translocation of cytosolic μ-calpain, suggesting that myofibrillar and microsomal μ-calpain was responsible for the twofold increase in activity and thus involved in controlled proteolysis during fiber transformation. This is in contrast to muscle regeneration where m-calpain translocation predominated. Taken together, we suggest that translocation is an important step in the control of calpain activity in skeletal muscle in vivo.

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