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Amylin activates glycogen phosphorylase in the isolated soleus muscle of the rat
Author(s) -
Young Andrew A.,
Mott David M.,
Stone Karen,
Cooper Garth J.S.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80380-l
Subject(s) - amylin , glycogenolysis , glycogen phosphorylase , medicine , endocrinology , glycogen , soleus muscle , glycogen synthase , skeletal muscle , insulin , chemistry , glycogenesis , in vivo , biology , biochemistry , microbiology and biotechnology , islet
The pancreatic β‐cell hormone amylin acts in isolated rat skeletal muscle to decrease insulin‐stimulated incorporation of glucose into glycogen. It also increases blood levels of lactate and glucose in fasted rats in vivo. However, it remained uncertain whether amylin exerts direct effects to stimulate muscle glycogenolysis. We now report that amylin caused a dose‐dependent increase in activity of muscle glycogen phosphorylase in isolated rat soleus muscle by stimulating phosphorylase a . Insulin inhibited amylin‐stimulated activation of phosphorylase. Effects of amylin to stimulate muscle glycogenolysis are consistent with observed effects of amylin in vivo and could be a major mechanism whereby amylin modulates carbohydrate metabolism.