Abstract
Glycogen, a branched polymer of glucose, serves as an energy reserve in many organisms. The degree of branching likely reflects the balance between the activities of glycogen synthase and branching enzyme. Mice overexpressing constitutively active glycogen synthase in skeletal muscle (GSL30) have elevated muscle glycogen. To test whether excess glycogen synthase activity affected glycogen branching, we examined the glycogen from skeletal muscle of GSL30 mice. The absorption spectrum of muscle glycogen determined in the presence of iodine was shifted to higher wavelengths in the GSL30 animals, consistent with a decrease in the degree of branching. As judged by Western blotting, the levels of glycogenin and the branching enzyme were also elevated. Branching enzyme activity also increased approximately threefold. However, this compared with an increase in glycogen synthase of some 50-fold, so that the increase in branching enzyme in response to overexpression of glycogen synthase was insufficient to synthesize normally branched glycogen.
| Original language | English |
|---|---|
| Pages (from-to) | 826-830 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 305 |
| Issue number | 4 |
| DOIs | |
| State | Published - Jun 13 2003 |
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Keywords
- Branching enzyme
- Glycogen
- Glycogen synthase
- Glycogenin
- Lafora
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Overexpression of glycogen synthase in mouse muscle results in less branched glycogen. / Pederson, Bartholomew A.; Csitkovits, Anna G.; Simon, Renee; Schroeder, Jill M.; Wang, Wei; Skurat, Alexander; Roach, Peter.
In: Biochemical and Biophysical Research Communications, Vol. 305, No. 4, 13.06.2003, p. 826-830.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Overexpression of glycogen synthase in mouse muscle results in less branched glycogen
AU - Pederson, Bartholomew A.
AU - Csitkovits, Anna G.
AU - Simon, Renee
AU - Schroeder, Jill M.
AU - Wang, Wei
AU - Skurat, Alexander
AU - Roach, Peter
PY - 2003/6/13
Y1 - 2003/6/13
N2 - Glycogen, a branched polymer of glucose, serves as an energy reserve in many organisms. The degree of branching likely reflects the balance between the activities of glycogen synthase and branching enzyme. Mice overexpressing constitutively active glycogen synthase in skeletal muscle (GSL30) have elevated muscle glycogen. To test whether excess glycogen synthase activity affected glycogen branching, we examined the glycogen from skeletal muscle of GSL30 mice. The absorption spectrum of muscle glycogen determined in the presence of iodine was shifted to higher wavelengths in the GSL30 animals, consistent with a decrease in the degree of branching. As judged by Western blotting, the levels of glycogenin and the branching enzyme were also elevated. Branching enzyme activity also increased approximately threefold. However, this compared with an increase in glycogen synthase of some 50-fold, so that the increase in branching enzyme in response to overexpression of glycogen synthase was insufficient to synthesize normally branched glycogen.
AB - Glycogen, a branched polymer of glucose, serves as an energy reserve in many organisms. The degree of branching likely reflects the balance between the activities of glycogen synthase and branching enzyme. Mice overexpressing constitutively active glycogen synthase in skeletal muscle (GSL30) have elevated muscle glycogen. To test whether excess glycogen synthase activity affected glycogen branching, we examined the glycogen from skeletal muscle of GSL30 mice. The absorption spectrum of muscle glycogen determined in the presence of iodine was shifted to higher wavelengths in the GSL30 animals, consistent with a decrease in the degree of branching. As judged by Western blotting, the levels of glycogenin and the branching enzyme were also elevated. Branching enzyme activity also increased approximately threefold. However, this compared with an increase in glycogen synthase of some 50-fold, so that the increase in branching enzyme in response to overexpression of glycogen synthase was insufficient to synthesize normally branched glycogen.
KW - Branching enzyme
KW - Glycogen
KW - Glycogen synthase
KW - Glycogenin
KW - Lafora
UR - http://www.scopus.com/inward/record.url?scp=0038581181&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0038581181&partnerID=8YFLogxK
U2 - 10.1016/S0006-291X(03)00862-3
DO - 10.1016/S0006-291X(03)00862-3
M3 - Article
C2 - 12767905
AN - SCOPUS:0038581181
VL - 305
SP - 826
EP - 830
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 4
ER -