STANOZOLOL DOES NOT ACUTELY AFFECT MAXIMAL FORCE GENERATION OR CALCIUM-SENSITIVITY OF SKELETAL MUSCLE.

1980 ◽  
Vol 21 (Supplement) ◽  
pp. S17
Author(s):  
M. A. Andrews ◽  
M. L. Rosser ◽  
R. E. Godt
2019 ◽  
Vol 94 ◽  
pp. 115-122 ◽  
Author(s):  
Allison B. Wang ◽  
Eric J. Perreault ◽  
Thomas J. Royston ◽  
Sabrina S.M. Lee

Nature ◽  
1995 ◽  
Vol 375 (6533) ◽  
pp. 688-691 ◽  
Author(s):  
Malcolm Irving ◽  
Taylor St Claire Alien ◽  
Cibele Sabido-David ◽  
James S. Craik ◽  
Birgit Brandmeier ◽  
...  

2020 ◽  
Vol 118 (3) ◽  
pp. 122a
Author(s):  
Connor Tyree ◽  
Kyra Peczkowski ◽  
Paul M. Janssen ◽  
Jill Rafael-Fortney ◽  
Jonathan P. Davis

2000 ◽  
Vol 89 (5) ◽  
pp. 2092-2098 ◽  
Author(s):  
Paul G. Smith ◽  
Chaity Roy ◽  
Steven Fisher ◽  
Qi-Quan Huang ◽  
Frank Brozovich

Cultured airway smooth muscle cells subjected to cyclic deformational strain have increased cell content of myosin light chain kinase (MLCK) and myosin and increased formation of actin filaments. To determine how these changes may increase cell contractility, we measured isometric force production with changes in cytosolic calcium in individual permeabilized cells. The pCa for 50% maximal force production was 6.6 ± 0.4 in the strain cells compared with 5.9 ± 0.3 in control cells, signifying increased calcium sensitivity in strain cells. Maximal force production was also greater in strain cells (8.6 ± 2.9 vs. 5.7 ± 3.1 μN). The increased maximal force production in strain cells persisted after irreversible thiophosphorylation of myosin light chain, signifying that increased force could not be explained by differences in myosin light chain phosphorylation. Cells strained for brief periods sufficient to increase cytoskeletal organization but insufficient to increase contractile protein content also produced more force, suggesting that strain-induced cytoskeletal reorganization also increases force production.


1998 ◽  
Vol 84 (4) ◽  
pp. 1166-1173 ◽  
Author(s):  
John J. Labella ◽  
Monica J. Daood ◽  
A. P. Koretsky ◽  
Brian B. Roman ◽  
Gary C. Sieck ◽  
...  

Creatine kinase (CK) provides ATP buffering in skeletal muscle and is expressed as 1) cytosolic myofibrillar CK (M-CK) and 2) sarcomeric mitochondrial CK (ScCKmit) isoforms that differ in their subcellular localization. We compared the isometric contractile and fatigue properties of 1) control CK-sufficient (Ctl), 2) M-CK-deficient (M-CK[−/−]), and 3) combined M-CK/ScCKmit-deficient null mutant (CK[−/−]) diaphragm (Dia) to determine the effect of the absence of M-CK activity on Dia performance in vitro. Baseline contractile properties were comparable across groups except for specific force, which was ∼16% lower in CK[−/−] Dia compared with M-CK[−/−] and Ctl Dia. During repetitive activation (40 Hz, [Formula: see text] duty cycle), force declined in all three groups. This decline was significantly greater in CK[−/−] Dia compared with Ctl and M-CK[−/−] Dia. The pattern of force decline did not differ between M-CK[−/−] and Ctl Dia. We conclude that Dia isometric muscle function is not absolutely dependent on the presence of M-CK, whereas the complete absence of CK acutely impairs isometric force generation during repetitive activation.


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