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Glycogen, glycogen phosphorylase, and glucose 6-phosphatase (G6Pase) activities were examined cytochemically in chondrocytes of femoral epiphyseal cartilages and cartilaginous ribs of 3- and 7-day-old rats. G6Pase activity was also examined biochemically. Glycogen was abundant in chondrocytes of the reserve zone, while it became scarce in the cells of the proliferative zone. From the upper part (adjoining the proliferative zone) to the lower part of the hypertrophic zone, glycogen accumulated in chondrocytes and decreased in the cells of the degenerative zone. Inversely, glycogen phosphorylase a and G6Pase activities were relatively high in chondrocytes of the proliferative zone and upper hypertrophic zone and were low in the cells of the reserve zone, lower hypertrophic zone, and degenerative zone. The reaction product for G6Pase was present in the endoplasmic reticulum and nuclear envelope of all types of chondrocytes composing the cartilages, although the amounts of reaction product varied with the cell types in parallel with the histochemical results. Biochemical G6Pase activity was higher in epiphyseal cartilages than in cartilaginous ribs. The possible mechanism and significance of the accumulation and decrease of glycogen in chondrocytes of the epiphyseal cartilage were discussed.
Anat Rec 1987 Dec
PMID:Glucose 6-phosphatase and glycogen phosphorylase activities in chondrocytes in epiphyseal cartilage of growing rats. 283 83

The effects of starvation on glucose 6-phosphatase (G6Pase; EC 3.1.3.9., D-glucose 6-phosphate phosphohydrolase) and glycogen phosphorylase (EC 2.4.1.1.) activities, and on glycogen content, were studied in skeletal muscles (m. rectus femoris) of mice. In the muscle cells from fed animals, the cytochemical reaction product for G6Pase activity was observed in moderate amounts in the terminal cisternae of sarcoplasmic reticulum and in small amounts in the nuclear envelope, and was rare or absent in the intermyofibrillar sarcoplasmic reticulum. After 4 days of starvation, however, the reaction product became abundant in all of the terminal cisternae, intermyofibrillar sarcoplasmic reticulum, and nuclear envelope. Biochemical G6Pase and glycogen phosphorylase a (active form) activities were higher in the muscles of starved mice than in those of fed animals. The glycogen content decreased markedly in the muscles of starved mice. The results suggest that the role of the increased G6Pase in skeletal muscle cells of starved mice is to release glucose into the blood by hydrolyzing glucose 6-phosphate produced through the increased phosphorylase activity.
Anat Rec 1986 Oct
PMID:Significance of the increase in glucose 6-phosphatase activity in skeletal muscle cells of the mouse by starvation. 302 18

To study the physiological role of skeletal muscle glycogen in starved animals, effects of starvation on glycogen and glycogen phosphorylase (EC 2.4.1.1.) activity were studied in muscle fibers (morphologic study) and in whole muscles (biochemical study) of the rectus femoris muscle of mouse. Glycogen content in the liver of the starved animals was also measured. PAS reaction, strong in muscle fibers of fed animals, became weak predominantly in type IIB fibers after 2 days and almost disappeared after 4 days of starvation. Glycogen particles, numerous in the sarcoplasm between myofibrils of muscle fibers, decreased markedly predominantly in type IIB fibers after 2 days and almost disappeared after 4 days. Phosphorylase a activity, undetected in fibers of fed mice, appeared weak in type IIB fibers and very weak in type IIA fibers after 2 days and became moderate in type IIB fibers and weak in type IIA fibers after 4 days. Muscle glycogen content did not differ by 16 hours from the values of corresponding fed animals. However, liver glycogen content had already decreased after 8 hours and markedly so after 12 hours. The results support our hypothesis-"skeletal muscle glycogen is used for maintaining the blood glucose level in starved mice" (Hirose et al.: Anat. Rec., 216:133-138, 1986)-and show that type IIB fibers play a main role in maintaining the glucose level and that muscle glycogen is utilized after depletion of liver glycogen.
Anat Rec 1987 Jul
PMID:Physiological role of skeletal muscle glycogen in starved mice. 363 41

This study was designed to correlate changes in the rate-limiting enzymes of glycogen synthesis (glycogen synthase) and glycogen breakdown (glycogen phosphorylase) with the ultrastructural changes which occur in the soleus muscle following tenotomy. Soleus muscles were removed at 1, 2, 3, 7, 14, 21, and 63 days after tenotomy and were prepared for electron microscopy or frozen for enzyme analysis. In the first 7 days posttenotomy, soleus muscle fibers underwent a series of degenerative changes, while both synthase and phosphorylase activities decreased. Over the next 8 weeks the histological appearance of the soleus muscle eventually returned to normal while synthase and phosphorylase activities increased. We suggest that recovery from tenotomy involves an increase in the energy demands of the muscle, resulting in the increased activity of the key rate-limiting enzymes of muscle glycogen metabolism from the drastically reduced levels observed in the period before recovery begins.
Anat Rec 1983 Jul
PMID:Ultrastructural and biochemical changes in rat soleus muscle following tenotomy. 641 93