Glycogen synthase binds to sarcoplasmic reticulum and is phosphorylated by CaMKII in fast-twitch skeletal muscle

2007 ◽  
Vol 459 (1) ◽  
pp. 115-121 ◽  
Author(s):  
Roberta Sacchetto ◽  
Elisa Bovo ◽  
Leonardo Salviati ◽  
Ernesto Damiani ◽  
Alfredo Margreth
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Glycogen Synthase ◽  
Fast Twitch

scholarly journals Evidence for membrane microheterogeneity in the sarcoplasmic reticulum of fast twitch skeletal muscle.

1982 ◽  
Vol 257 (19) ◽  
pp. 11689-11695
Author(s):  
W B Van Winkle ◽  
R J Bick ◽  
D E Tucker ◽  
C A Tate ◽  
M L Entman
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Fast Twitch ◽  
Membrane Microheterogeneity

Control of glycogen synthesis is shared between glucose transport and glycogen synthase in skeletal muscle fibers

2000 ◽  
Vol 278 (2) ◽  
pp. E234-E243 ◽  
Author(s):  
Iñaki Azpiazu ◽  
Jill Manchester ◽  
Alexander V. Skurat ◽  
Peter J. Roach ◽  
John C. Lawrence
Keyword(s):  
Skeletal Muscle ◽  
Glucose Transport ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Muscle Fibers ◽  
Fiber Types ◽  
Oxidative Potential ◽  
Glycogen Accumulation ◽  
Tibialis Muscle ◽  
Fast Twitch

The effects of transgenic overexpression of glycogen synthase in different types of fast-twitch muscle fibers were investigated in individual fibers from the anterior tibialis muscle. Glycogen synthase was severalfold higher in all transgenic fibers, although the extent of overexpression was twofold greater in type IIB fibers. Effects of the transgene on increasing glycogen and phosphorylase and on decreasing UDP-glucose were also more pronounced in type IIB fibers. However, in any grouping of fibers having equivalent malate dehydrogenase activity (an index of oxidative potential), glycogen was higher in the transgenic fibers. Thus increasing synthase is sufficient to enhance glycogen accumulation in all types of fast-twitch fibers. Effects on glucose transport and glycogen synthesis were investigated in experiments in which diaphragm, extensor digitorum longus (EDL), and soleus muscles were incubated in vitro. Transport was not increased by the transgene in any of the muscles. The transgene increased basal [14C]glucose into glycogen by 2.5-fold in the EDL, which is composed primarily of IIB fibers. The transgene also enhanced insulin-stimulated glycogen synthesis in the diaphragm and soleus muscles, which are composed of oxidative fiber types. We conclude that increasing glycogen synthase activity increases the rate of glycogen synthesis in both oxidative and glycolytic fibers, implying that the control of glycogen accumulation by insulin in skeletal muscle is distributed between the glucose transport and glycogen synthase steps.

Diazepam reveals different rate-limiting processes in rat skeletal muscle contraction

1987 ◽  
Vol 65 (2) ◽  
pp. 272-273 ◽  
Author(s):  
Michael Chua ◽  
Angela F. Dulhunty
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Calcium Binding ◽  
Extensor Digitorum Longus ◽  
Calcium Uptake ◽  
Rat Skeletal Muscle ◽  
Skeletal Muscle Contraction ◽  
Slow Twitch ◽  
Fast Twitch ◽  
Rate Limiting

The action of the tranquilizer diazepam on rat skeletal muscle showed that relaxation of isometric twitches is controlled by different processes in extensor digitorum longus (fast-twitch) and soleus (slow-twitch) muscles. Diazepam caused an increase in the amplitude of twitches in fibres from both muscles but increased the twitch duration only in soleus. The amplitude of fused tetani were reduced in both muscles and the rate of relaxation after the tetanus slowed by as much as 34% when the amplitude of the tetanus was reduced by only 11%. The slower tetanic relaxation indicated that calcium uptake by the sarcoplasmic reticulum was slower than normal in slow- and fast-twitch fibres. We conclude therefore that calcium uptake by the sarcoplasmic reticulum is rate limiting for twitch relaxation in slow-twitch but not fast-twitch fibres and suggest that calcium binding to parvalbumin controls relaxation in the fast fibres.

Activation of glycogen synthase in skeletal muscle: effects of insulin in slow- and fast-twitch muscles in vivo

1997 ◽  
Vol 25 (1) ◽  
pp. 102S-102S
Author(s):  
Lee G. D. Fryer ◽  
Mark J. Holness ◽  
Mary C. Sugden
Keyword(s):  
Skeletal Muscle ◽  
Glycogen Synthase ◽  
Fast Twitch

scholarly journals A novel interaction mechanism accounting for different acylphosphatase effects on cardiac and fast twitch skeletal muscle sarcoplasmic reticulum calcium pumps

FEBS Letters ◽  
1999 ◽  
Vol 443 (3) ◽  
pp. 308-312 ◽  
Author(s):  
Chiara Nediani ◽  
Claudia Fiorillo ◽  
Stefania Rigacci ◽  
Francesca Magherini ◽  
Michela Francalanci ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Interaction Mechanism ◽  
Calcium Pumps ◽  
Fast Twitch ◽  
Sarcoplasmic Reticulum Calcium

Characterization of cDNA and Genomic DNA Encoding SERCA1, the Ca2+-ATPase of Human Fast-Twitch Skeletal Muscle Sarcoplasmic Reticulum, and Its Elimination as a Candidate Gene for Brody Disease

Genomics ◽  
1995 ◽  
Vol 30 (3) ◽  
pp. 415-424 ◽  
Author(s):  
Yilin Zhang ◽  
Junichi Fujii ◽  
Michael S. Phillips ◽  
Hai-Shiene Chen ◽  
George Karpati ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Candidate Gene ◽  
Genomic Dna ◽  
Dna Encoding ◽  
Fast Twitch
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