Parathyroid hormone-related protein is rapidly up-regulated in blood vessels of rat skeletal muscle by low-frequency stimulation

1999 ◽  
Vol 439 (1) ◽  
pp. 167-173 ◽  
Author(s):  
A.G. Schneider ◽  
K. Leuthäuser ◽  
D. Pette
Keyword(s):  
Skeletal Muscle ◽  
Parathyroid Hormone ◽  
Blood Vessels ◽  
Low Frequency ◽  
Related Protein ◽  
Rat Skeletal Muscle ◽  
Parathyroid Hormone Related Protein ◽  
Low Frequency Stimulation ◽  
Frequency Stimulation

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.

Reduced glycolytic metabolism in regenerated fast-twitch skeletal muscle

1991 ◽  
Vol 261 (1) ◽  
pp. C169-C176 ◽  
Author(s):  
M. A. Wineinger ◽  
F. Gorin ◽  
R. Tait ◽  
B. Froman ◽  
R. C. Carlsen
Keyword(s):  
Skeletal Muscle ◽  
Low Frequency ◽  
Small Population ◽  
Intact Control ◽  
Low Frequency Stimulation ◽  
Glycolytic Activity ◽  
Frequency Stimulation ◽  
Relative Decline ◽  
Fast Twitch ◽  
Maximum Expression

Freely grafted rat extensor digitorum longus (EDL) muscles were subjected to low-frequency stimulation in an anaerobic environment to determine whether regenerating fast-twitch muscles regain normal glycolytic metabolic capacity. Regenerating muscles were tested at 28, 42, and 76 days after the graft procedure. Stabilized grafts (76 days) produced approximately 60% of the lactate generated by intact, control EDL subjected to the same stimulus paradigm and developed half the estimated increase in H+. The grafts exhibited the same relative decline in force after 5 min of anaerobic stimulation as control EDL but maintained relatively constant levels of ATP while consuming phosphocreatine. This study indicates that regenerating fast-twitch skeletal muscle has a reduced ability to initiate glycolytic activity during exercise. The data also indicate that a small population of regenerating fast-twitch fibers express the slow isoform of myosin heavy chain (beta-MHC) with maximum expression occurring at 56 days postsurgery.

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