scholarly journals Control of rat skeletal-muscle phosphorylase phosphatase activity by adrenaline

1978 ◽  
Vol 176 (1) ◽  
pp. 347-350 ◽  
Author(s):  
S H Tao ◽  
F L Huang ◽  
A Lynch ◽  
W H Glinsmann
Keyword(s):  
Skeletal Muscle ◽  
Cyclic Amp ◽  
Phosphatase Activity ◽  
Glycogen Synthase ◽  
Rat Skeletal Muscle ◽  
Inhibitor Activity ◽  
Phosphatase Inhibitor ◽  
Heat Stable ◽  
Muscle Phosphorylase ◽  
Isolated Rat

Administration of adrenaline to an isolated rat hindlimb preparation rapidly decreased muscle phosphorylase phosphatase (EC 3.1.3.17) activity and increased heat-stable and trypsin-labile phosphatase inhibitor activity. This was associated with increased tissue cyclic AMP concentrations, phosphorylase (EC 2.4.1.1) activation and glycogen synthase (EC 2.4.1.11) inactivation.

Effects of insulin treatment on the activities of phosphoprotein phosphatase and its inhibitors

1980 ◽  
Vol 95 (3) ◽  
pp. 427-432 ◽  
Author(s):  
L. Y. Chang ◽  
L. C. Huang
Keyword(s):  
Skeletal Muscle ◽  
Phosphatase Activity ◽  
Glycogen Synthase ◽  
Rat Skeletal Muscle ◽  
Phosphoprotein Phosphatase ◽  
Heat Stable ◽  
Muscle Extract ◽  
Wide Range ◽  
Heat Stable Protein

Abstract. An increase in glycogen synthase phosphatase (phosphoprotein phosphatase) activity was observed in the rat skeletal muscle extract following insulin administration. The phosphoprotein phosphatase activity present in the muscle extract from insulin treated rats was observed to remain elevated after the extract had been subjected to a molecular sieve chromatography. These results indicate that the stimulatory effets of insulin is due to modification of phosphatase itself or some macromolecular weight modifiers. The heat-stable protein inhibitors of the phosphoprotein phosphatase were isolated from skeletal muscle of insulin treated and control rats and their inhibitory potencies were compared over a wide range of protein concentrations. The inhibitory potency in the insulin treated rat skeletal muscle was found to be significantly less than that in the control muscle. Since type-1 inhibitor is well-known to be active only after being phosphorylated by cyclic AMP-dependent protein kinase, we suggest that the observed change in phosphoprotein phosphatase inhibitor potency is most likely mediated by an alteration in the phosphorylation state of type-1 inhibitor.

Isolation and characterization of cyclic AMP-independent glycogen synthase kinase from rat skeletal muscle

1980 ◽  
Vol 615 (2) ◽  
pp. 324-340 ◽  
Author(s):  
Keith K. Schlender ◽  
Stephen J. Beebee ◽  
James C. Willey ◽  
Stephen A. Lutz ◽  
Erwin M. Reimann
Keyword(s):  
Skeletal Muscle ◽  
Cyclic Amp ◽  
Glycogen Synthase ◽  
Glycogen Synthase Kinase ◽  
Rat Skeletal Muscle ◽  
Isolation And Characterization

The possible existence of a heat-stable alkaline proteinase (HAP) in rat skeletal muscle

1988 ◽  
Vol 89 (2) ◽  
pp. 359-361
Author(s):  
Yasuo Makinodan ◽  
Haruhiko Toyohara ◽  
Yoshihiro Yokoyama ◽  
Masato Kinoshita
Keyword(s):  
Skeletal Muscle ◽  
Rat Skeletal Muscle ◽  
Alkaline Proteinase ◽  
Heat Stable
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