Protein Kinase A from Bat Skeletal Muscle: A Kinetic Study of the Enzyme from a Hibernating Mammal

1998 ◽  
Vol 358 (2) ◽  
pp. 243-250 ◽  
Author(s):  
Clark P. Holden ◽  
Kenneth B. Storey
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Kinetic Study ◽  
Protein Kinase A ◽  
Kinase A

scholarly journals Stress-induced increase in skeletal muscle force requires protein kinase A phosphorylation of the ryanodine receptor

2012 ◽  
Vol 590 (24) ◽  
pp. 6381-6387 ◽  
Author(s):  
Daniel C. Andersson ◽  
Matthew J. Betzenhauser ◽  
Steven Reiken ◽  
Alisa Umanskaya ◽  
Takayuki Shiomi ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Ryanodine Receptor ◽  
Muscle Force ◽  
Kinase A

scholarly journals Protein kinase A–dependent modulation of Ca2+ sensitivity in cardiac and fast skeletal muscles after reconstitution with cardiac troponin

2009 ◽  
Vol 133 (6) ◽  
pp. 571-581 ◽  
Author(s):  
Douchi Matsuba ◽  
Takako Terui ◽  
Jin O-Uchi ◽  
Hiroyuki Tanaka ◽  
Takao Ojima ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Cardiac Muscle ◽  
Protein Kinase A ◽  
Striated Muscle ◽  
Physiological Mechanism ◽  
Adrenergic Stimulation ◽  
Fast Skeletal Muscle ◽  
Psoas Muscles ◽  
Kinase A

Protein kinase A (PKA)-dependent phosphorylation of troponin (Tn)I represents a major physiological mechanism during β-adrenergic stimulation in myocardium for the reduction of myofibrillar Ca2+ sensitivity via weakening of the interaction with TnC. By taking advantage of thin filament reconstitution, we directly investigated whether or not PKA-dependent phosphorylation of cardiac TnI (cTnI) decreases Ca2+ sensitivity in different types of muscle: cardiac (porcine ventricular) and fast skeletal (rabbit psoas) muscles. PKA enhanced phosphorylation of cTnI at Ser23/24 in skinned cardiac muscle and decreased Ca2+ sensitivity, of which the effects were confirmed after reconstitution with the cardiac Tn complex (cTn) or the hybrid Tn complex (designated as PCRF; fast skeletal TnT with cTnI and cTnC). Reconstitution of cardiac muscle with the fast skeletal Tn complex (sTn) not only increased Ca2+ sensitivity, but also abolished the Ca2+-desensitizing effect of PKA, supporting the view that the phosphorylation of cTnI, but not that of other myofibrillar proteins, such as myosin-binding protein C, primarily underlies the PKA-induced Ca2+ desensitization in cardiac muscle. Reconstitution of fast skeletal muscle with cTn decreased Ca2+ sensitivity, and PKA further decreased Ca2+ sensitivity, which was almost completely restored to the original level upon subsequent reconstitution with sTn. The essentially same result was obtained when fast skeletal muscle was reconstituted with PCRF. It is therefore suggested that the PKA-dependent phosphorylation or dephosphorylation of cTnI universally modulates Ca2+ sensitivity associated with cTnC in the striated muscle sarcomere, independent of the TnT isoform.

scholarly journals Ryanodine receptor remodeling in cardiomyopathy and muscular dystrophy caused by lamin A/C gene mutation

2021 ◽  
Author(s):  
Haikel Dridi ◽  
Wei Wu ◽  
Steven R Reiken ◽  
Rachel M Ofer ◽  
Yang Liu ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Muscular Dystrophy ◽  
Protein Kinase A ◽  
Ryanodine Receptor ◽  
Lamin A ◽  
Muscle Dysfunction ◽  
Skeletal Muscle Dysfunction ◽  
Lmna Mutation ◽  
Kinase A

Abstract Mutations in the lamin A/C gene (LMNA), which encodes A-type lamins, cause several diseases called laminopathies, the most common of which is dilated cardiomyopathy with muscular dystrophy. The role of Ca2+ regulation in these diseases remain poorly understood. We now show biochemical remodeling of the ryanodine receptor (RyR)/intracellular Ca2+ release channel in heart samples from human subjects with LMNA mutations, including protein kinase A-catalyzed phosphorylation, oxidation and depletion of the stabilizing subunit calstabin. In the LmnaH222P/H222P murine model of Emery-Dreifuss muscular dystrophy caused by LMNA mutation, we demonstrate an age-dependent biochemical remodeling of RyR2 in heart and RyR1 in skeletal muscle. This RyR remodeling is associated with heart and skeletal muscle dysfunction. Defective heart and muscle function are ameliorated by treatment with a novel Rycal small molecule drug (S107) that fixes ‘leaky’ RyRs. SMAD3 phosphorylation is increased in hearts and diaphragms of LmnaH222P/H222P mice, which enhances NADPH oxidase binding to RyR channels, contributing to their oxidation. There is also increased generalized protein oxidation, increased calcium/calmodulin-dependent protein kinase II-catalyzed phosphorylation of RyRs and increased protein kinase A activity in these tissues. Our data show that RyR remodeling plays a role in cardiomyopathy and skeletal muscle dysfunction caused by LMNA mutation and identify these Ca2+ channels as a potential therapeutic target.

scholarly journals Protein Kinase A Modifies Skeletal Muscle Contractile Function Via Modification Of Mybp-C

2021 ◽  
Vol 53 (8S) ◽  
pp. 121-121
Author(s):  
Grace E. Privett ◽  
Karen W. Needham ◽  
Austin W. Ricci ◽  
Scott J. Mongold ◽  
Damien M. Callahan
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Contractile Function ◽  
Muscle Contractile ◽  
Kinase A

PROTEIN KINASE A IN SKELETAL MUSCLE PLASTICITY 1295

1997 ◽  
Vol 29 (Supplement) ◽  
pp. 226
Author(s):  
T. E. Wills ◽  
C. M. Sheehan ◽  
L. P. Koziris ◽  
W. K. Palmer
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Muscle Plasticity ◽  
Kinase A

scholarly journals Protein Kinase A-based Modulation Of Ca2+ Sensitivity In Skinned Skeletal Muscle Fibers Reconstituted With Cardiac Troponin

2009 ◽  
Vol 96 (3) ◽  
pp. 501a
Author(s):  
Norio Fukuda ◽  
Douchi Matsuba ◽  
Takako Terui ◽  
Jin O-Uchi ◽  
Hiroyuki Tanaka ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Cardiac Troponin ◽  
Muscle Fibers ◽  
Skeletal Muscle Fibers ◽  
Kinase A
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