Responses of mouse fast and slow skeletal muscle to streptozotocin diabetes: Myosin isoenzymes and phosphorous metabolites

1995 ◽  
Vol 148 (2) ◽  
pp. 147-154 ◽  
Author(s):  
Jason G. Fewell ◽  
Timothy S. Moerland
Keyword(s):  
Skeletal Muscle ◽  
Streptozotocin Diabetes ◽  
Slow Skeletal Muscle ◽  
Myosin Isoenzymes

Effect of External Calcium and other Divalent Cations on K+ Contractures in Denervated Slow Skeletal Muscle Fibers of the Frog

2019 ◽  
Author(s):  
Leonardo Hernández
Keyword(s):  
Skeletal Muscle ◽  
Binding Capacity ◽  
Divalent Cations ◽  
Muscle Fibers ◽  
Free Calcium ◽  
Slow Skeletal Muscle ◽  
Skeletal Muscle Fibers ◽  
Free Calcium Concentration ◽  
Chronic Denervation ◽  
Denervated Muscles

The influence of Ca2+ and other divalent cations on contractile responses of slow skeletal muscle fibers of the frog (Rana pipiens) under conditions of chronic denervation was investigated.Isometric tension was recorded from slow bundles of normal and denervated cruralis muscle in normal solution and in solutions with free calcium concentration solution or in solutions where other divalent cations (Sr2+, Ni2+, Co2+ or Mn2+) substituted for calcium. In the second week after nerve section, in Ca2+-free solutions, we observed that contractures (evoked from 40 to 80 mM-K+) of non-denervated muscles showed significantly higher tensions (p<0.05), than those from denervated bundles. Likewise, in solutions where calcium was substituted by all divalent cations tested, with exception of Mn2+, the denervated bundles displayed lower tension than non-denervated, also in the second week of denervation. In this case, the Ca2+ substitution by Sr2+ caused the higher decrease in tension, followed by Co2+ and Ni2+, which were different to non-denervated bundles, as the lowest tension was developed by Mn2+, followed by Co2+, and then Ni2+ and Sr2+. After the third week, we observed a recovery in tension. These results suggest that denervation altering the binding capacity to divalent cations of the voltage sensor.

Slow skeletal muscle myosin-binding protein-C (MyBPC1) mediates recruitment of muscle-type creatine kinase (CK) to myosin

2011 ◽  
Vol 436 (2) ◽  
pp. 437-445 ◽  
Author(s):  
Zhe Chen ◽  
Tong-Jin Zhao ◽  
Jie Li ◽  
Yan-Song Gao ◽  
Fan-Guo Meng ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Muscle Contraction ◽  
Binding Protein ◽  
High Energy ◽  
Functional Coupling ◽  
Muscle Type ◽  
Myosin Binding Protein ◽  
Slow Skeletal Muscle ◽  
Myosin Binding

Muscle contraction requires high energy fluxes, which are supplied by MM-CK (muscle-type creatine kinase) which couples to the myofibril. However, little is known about the detailed molecular mechanisms of how MM-CK participates in and is regulated during muscle contraction. In the present study, MM-CK is found to physically interact with the slow skeletal muscle-type MyBPC1 (myosin-binding protein C1). The interaction between MyBPC1 and MM-CK depended on the creatine concentration in a dose-dependent manner, but not on ATP, ADP or phosphocreatine. The MyBPC1–CK interaction favoured acidic conditions, and the two molecules dissociated at above pH 7.5. Domain-mapping experiments indicated that MM-CK binds to the C-terminal domains of MyBPC1, which is also the binding site of myosin. The functional coupling of myosin, MyBPC1 and MM-CK is further corroborated using an ATPase activity assay in which ATP expenditure accelerates upon the association of the three proteins, and the apparent Km value of myosin is therefore reduced. The results of the present study suggest that MyBPC1 acts as an adaptor to connect the ATP consumer (myosin) and the regenerator (MM-CK) for efficient energy metabolism and homoeostasis.

scholarly journals The myosin alkali light chains of mouse ventricular and slow skeletal muscle are indistinguishable and are encoded by the same gene.

1985 ◽  
Vol 260 (14) ◽  
pp. 8578-8584 ◽  
Author(s):  
P J Barton ◽  
A Cohen ◽  
B Robert ◽  
M Y Fiszman ◽  
F Bonhomme ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Light Chains ◽  
Slow Skeletal Muscle

scholarly journals Properties of the ‘slow’ skeletal muscle fibres of the frog*

1953 ◽  
Vol 121 (2) ◽  
pp. 318-340 ◽  
Author(s):  
Stephen W. Kuffler ◽  
E. M. Vaughan Williams
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibres ◽  
Slow Skeletal Muscle ◽  
Skeletal Muscle Fibres

Assignment of the human slow skeletal muscle troponin gene (TNNI1) to 1q32 by fluorescence in situ hybridisation

1993 ◽  
Vol 62 (2-3) ◽  
pp. 181-182 ◽  
Author(s):  
H.J. Eyre ◽  
P.A. Akkari ◽  
C. Meredith ◽  
S.D. Wilton ◽  
D.C. Callen ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
In Situ Hybridisation ◽  
Fluorescence In Situ Hybridisation ◽  
Slow Skeletal Muscle

scholarly journals Weekly Versus Monthly Testosterone Administration on Fast and Slow Skeletal Muscle Fibers in Older Adult Males

2015 ◽  
Vol 100 (2) ◽  
pp. E223-E231 ◽  
Author(s):  
Robert H. Fitts ◽  
James R. Peters ◽  
E. Lichar Dillon ◽  
William J. Durham ◽  
Melinda Sheffield-Moore ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Older Adult ◽  
Muscle Fibers ◽  
Adult Males ◽  
Slow Skeletal Muscle ◽  
Skeletal Muscle Fibers ◽  
Testosterone Administration

scholarly journals Nerve Activity-dependent Modulation of Calcineurin Signaling in Adult Fast and Slow Skeletal Muscle Fibers

2001 ◽  
Vol 276 (48) ◽  
pp. 45243-45254 ◽  
Author(s):  
Shannon E. Dunn ◽  
Alain R. Simard ◽  
Rhonda Bassel-Duby ◽  
R. Sanders Williams ◽  
Robin N. Michel
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fibers ◽  
Nerve Activity ◽  
Slow Skeletal Muscle ◽  
Skeletal Muscle Fibers ◽  
Activity Dependent ◽  
Calcineurin Signaling
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