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Evidence for release of free glucose from muscle during amylin‐induced glycogenolysis in rats
Author(s) -
Young Andrew A.,
Carlo Pam,
Smith Pam,
Wolfe-Lopez Deborah,
Pittner Richard,
Wang Ming-Wei,
Rink Timothy
Publication year - 1993
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(93)80702-v
Subject(s) - amylin , glycogenolysis , medicine , endocrinology , hexose , glycogen , chemistry , stimulation , insulin , glycogen synthase , glycogenesis , biochemistry , biology , enzyme , islet
Amylin, a 37 amino acid product of pancreatic β‐cells, inhibits insulin‐stimulated radioglucose incorporation into muscle glycogen. In the current study, we exercised rats and then prelabelled the glycogen pool by infusing [3‐ 3 H]glucose along with glucose and insulin. Subsequent amylin administration increased the rate of appearance of tritiated water 6.4‐fold, consistent with stimulation of glycogenolysis and passage of the released moieties through the hexose → triose step of glycolysis. Further, there was an increase in plasma [3‐ 3 H]glucose after amylin, consistent with the release of free glucose previously sequestered in muscle glycogen. Calcitonin gene‐releated peptide (8–37), an amylin antagonist, prevented these actions.