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Physiological role of skeletal muscle glycogen in starved mice.

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THE ANATOMICAL RECORD 218:267-274 (1987)
Physiological Role of Skeletal Muscle Glycogen in
Starved Mice
MINORU SAKAIDA, JUN WATANABE, SHINSUKE KANAMURA, HIROHIKO
TOKUNAGA, AND RYOKEI OGAWA
Department of Anatomy and Orthopedics, Kansai Medical University, Fumizonecho 1,
Moriguchi, Osaka, 570 Japan
ABSTRACT
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.
Glycogen in skeletal muscle is utilized as the energy
source for muscle contraction. However, we recently observed that in the skeletal muscle (rectus femoris muscle) of starved mice glucose 6-phosphatase (GGPase) and
glycogen phosphorylase a activities increase and glycogen content decreases, and we supposed that the role of
the increased G6Pase in skeletal muscle fibers of starved
mice is to release glucose into the blood by hydrolyzing
glucose 6-phosphate (G6P) produced through the increased phosphorylase activity from their glycogen (Hirose et al., 1986). In the present study, to obtain further
evidence supporting this hypothesis, we examined 1)
whether the changes in phosphorylase a activity and
glycogen content occur predominantly in any fiber type
of the rectus femoris muscle (histochemical and ultrastructural studies) and 2) whether glycogen mobilization
in the skeletal muscle occurs before or after the glycogen
mobilization in the liver, which is the greatest glucose
supplier into the blood during starvation (biochemical
study).
phorylase activity assay), 8, 12, 16, 24, 48, or 96 hours
(glycogen content assay), and 12, 24, 48, and 96 hours
(blood glucose assay). Starvation was started at 10 A.M.
for morphologic experiments and a t 6 or 10 A.M. for
chemical experiments. Experiments of starvation for 5
days or more were not carried out because about a half
of the animals died at 5 days of starvation. The animals
were killed by cervical dislocation.
Light Microscopy
Rectus femoris muscles were removed quickly and frozen on dry ice. Serial transverse sections (10 pm in
thickness) were cut in a cryostat through the midbelly
portion of the muscles.
Classification of fiber types
Serial fresh frozen sections were incubated for 1)acidstable myofibrilar adenosine triphosphatase (ATPase)
activity (Padykula and Herman, 1955; as modified by
Brooke and Kaiser, 1970), for 2) alkaline-stable ATPase
activity (Guth and Samaha, 19701, and for 3) succinate
dehydrogenase (SDH) activity (Barka and Anderson,
MATERIALS AND METHODS
1963). Muscle fibers showing dark reaction for acid-staTwo hundred thirty male ddY mice, 2 months old, ble ATPase and light reaction for alkaline-stable ATwere used. The animals were divided into two groups
and individually housed in cages. One group of animals
had free access to food and water prior to the experiReceived August 12,1986; accepted January 27,1987.
ments (fed animals) and the other group of animals
Address reprint requests to Dr. Shinsuke Kanamura, Department
(starved animals) was given only water for 2 or 4 days of Anatomy, Kansai Medical University, Fumizono-cho 1,Moriguchi,
(morphologic experiments), 24, 48, or 96 hours (phos- Osaka, 570 Japan.
0 1987 ALAN R. LISS, INC
268
M. SAKAIDA ET AL.
269
MUSCLE GLYCOGEN
Electron Microscopy
Pase were classified as type I, and the fibers showing
light reaction for acid-stable ATPase and dark reaction
for alkaline-stable ATPase were classified as type 11.
Type I1 fibers were subclassified into type IIA if they
had intense SDH reaction, into type IIB if they showed
weak SDH reaction, and into atypical type 11if they had
moderate SDH reaction.
Rectus femoris muscles were quickly removed and cut
into small pieces. The blocks were immersed in 2.5%
glutaraldehyde in 0.1 M phosphate buffer (pH 7.4) a t
4°C for 2.5 hours, washed with 8% sucrose in 0.1 M
phosphate buffer (pH 7.4) at 4°C for 20 minutes, postfixed with buffered 1% osmium tetroxide at 4°C for 2
hours, dehydrated in graded ethanol, and embedded in
Glycogen
Spurr's resin. Longitudinal ultrathin sections were
Fresh frozen sections were stained with the periodic stained with uranyl acetate and lead citrate and examacid Schiff (PAS) reaction and mounted in glycerin-jelly. ined in a JEM-100s electron microscope.
For control, the sections were preincubated with saliva
The fiber types at the electron microscope level were
a t 37 "C for 30 minutes and stained with PAS reaction.
identified on the basis of the size and distribution of
mitochondria in the muscle cells (Maxwell et al., 1977;
Phosphorylase activity
Armstrong, 1980).
For histochemical demonstration of total phosphoryBiochemical Methods
lase activity, fresh frozen sections were incubated in the
reaction medium containing 10.6 mM glucose l-phos- Glycogen content
phate (GlP), 2.3 mM adenosine monophosphate (AMP),
Rectus femoris muscles or livers were digested with
80 pg/ml glycogen, 3 mM ethylenediaminetetraacetic 20 volumes of 30%KOH at 95°C for 20 minutes. Glycoacid (EDTA), 5 mM NaF, and 0.1 M acetate buffer (pH gen in the digest was purified with ethanol according to
5.7) at 20°C for 1hour (Takeuchi, 1956). For phosphory- the method of Hassid and Abraham (1957), and the glylase a (active form) activity, the sections were incubated cogen amount was estimated by the anthrone reaction
in the medium lacking AMP (Godlewski, 1963). The (Hassid and Abraham, 1957). The content of glycogen
sections were immersed in 10% Gram solution for 3 was expressed as milligrams glycogen per gram of wet
minutes and mounted in iodoglycerin. The sections were tissue.
incubated in the medium lacking G1P (for total activity)
or lacking G1P and AMP (for phosphorylase a activity) Phosphorylase activity
as controls.
Rectus femoris muscles were homogenized a t 4°C with
20 volumes of 0.2 M Tris-maleate buffer (pH 6.1) conFigs. 1-12. Serial transverse sections of the rectus femoris muscles. taining 50 mM NaF and 5 mM EDTA for 1 minute at
A, type IIA fiber; B, type IIB fiber; X, atypical type I1 fiber. x 120.
2,000 rpm. The homogenate was centrifuged a t 4°C for
10 minutes at 3,OOOg. Phosphorylase activity was asFigs. 1-6. Fed (10 A.M.).
sayed by the method of Saheki et al. (1971). An aliquot
Fig. 1. Incubated for adenosine triphosphatase (ATPase) activity
(0.05 ml) of the supernatant was incubated with 0.15 ml
after acid preincubation.
of the medium (40 mM GlP, 100 mg/ml glycogen, 13 mM
NaF, 1.3 mM EDTA, 50 mM Tris-maleate, pH 6.1) in
Fig. 2. Incubated for ATPase activity after alkaline preincubation.
the presence or absence of 1 mM AMP a t 30°C for 5
Fig. 3. Incubated for succinate dehydrogenase activity.
minutes. The inorganic phosphorus released was determined by Phosphor C-test. The reaction in the presence
Fig. 4. PAS reaction. The staining reaction is strong.
of AMP shows total phosphorylase activity and the reFig. 5. Histochemical demonstration of total phosphorylase activity. action in the absence of AMP shows phosphorylase a
The staining reaction is strong in type IIA fibers (A) and moderate in activity. The activity was expressed a s micrograms
type IIB (B) and atypical type I1 (X) fibers.
phosphorus liberated per minute per gram of wet tissue.
Fig. 6. Histochemical demonstration of phosphorylase a activity. No
staining reaction is seen.
Blood glucose
Animals were anesthetized with chloroform. Blood was
taken from the right atrium by syringe and centrifuged
at 4°C for 30 minutes at 3,OOOg. Then, glucose in the
Fig. 7. Succinate dehydrogenase activity.
serum was assayed by the mutarotase-glucose oxidase
Fig. 8. PAS reaction. The staining reaction becomes weak in type method (Miwa et al., 1972).
IIB fibers (B) but moderate in type IIA (A) and atypical type I1 (XI
Figs. 7, 8. Starved for 2 days (10 A.M.).
fibers.
Figs. 9-12. Starved for 4 days (10A.M.).
Fig. 9. Succinate dehydrogenase activity.
Fig. 10. PAS reaction. The staining reaction almost disappears in
type IIB (B) and atypical type I1 (X) fibers although it remains very
weak in type IIA fibers (A).
Fig. 11. Total phosphorylase activity. The staining reaction is strong
in type IIB fibers (B), atypical type I1 fibers (X), and few type IIA fibers
mostly moderate in type IIA fibers (A).
(*) and
Fig. 12. Phosphorylase a activity. The staining reaction is moderate
in type IIB (B) and atypical type I1 (X) fibers and weak in type IIA
fibers (A).
Statistical analysis
Results were expressed as means k S.E. Student's ttest was used for comparison o€ values between experimental groups.
RESULTS
The starved mice became gradually less active than
the fed mice, and they appeared curled up after 2 or
more days of starvation.
Average body weight of fed mice was 38.3 k 0.6 g
(means + S.E., n = 32). The weight decreased after 2
days (33.9
0.4 g, n = 11)( P < .01) and 4 days of
starvation (29.8 0.6 g, n = 11)( P < .01).
270
M. SAKAIDA ET AL.
Figs. 13-15. Electron micrographs of muscle fibers in rectus femoris
muscles of mice.
Fig. 14. Portion of a type IIB fiber from a n animal starved for 2 days.
A few glycogen particles are seen in the sarcoplasm between myofibrils
at the I bands, whereas the particles are rare or absent in other
Fig. 13. Portions of type IIB fibers from fed animals (10 A.M.). A
Glycogen particles are abundant in sarcoplasm near the triads and
between myofibrils. X30,OOO. B: High-power magnification. Numerous
particles, 25-30 nm in diameter, are observed in sarcoplasm near the
triad. Some particles are also present between myofilaments (arrows).
portions of sarcoplasm. ~ 3 0 , 0 0 0 .
~50,000.
Fig. 15. Portions of muscle fibers from animals starved for 4 days. A
Portion of a type IIB fiber. Glycogen particles are absent. ~ 3 0 , 0 0 0B:
.
Portion of a type IIA fiber. A few particles are seen in sarcoplasm
between myofibrils (arrows). ~ 3 0 , 0 0 0 .
271
MUSCLE GLYCOGEN
Morphologic Results
Distribution of fiber types
h
?!v)
v)
.c
Rectus femoris muscles contained numerous type IIB
fibers (fed: 63.1 rf: 2.5%, starved for 2 days: 65.8 rf: 3.4%,
starved for 4 days: 62.9 & 1.8%, n = 4), a few type IIA
fibers (fed 25.4 2.3%, starved for 2 days: 26.3 2.3,
starved for 4 days: 26.0 & 1.5%), a few atypical type I1
fibers (fed: 11.5 & 1.3%, starved for 2 days: 7.9 rf: 2.7%,
starved for 4 days: 11.1 rf: 1.4%), and no type I fibers
(Figs. 1-3,7,9).
-E"
PAS reaction
% I -
The staining reaction was strong in muscle fibers of
fed mice (Fig. 4). The reaction, however, became weak
in type IIB fibers and moderate in type IIA and atypical
type I1 fibers after 2 days of starvation (Fig. 8).Although
very weak reaction was sometimes seen in type IIA
fibers, the staining almost disappeared after 4 days of
starvation (Fig. 10).
-U0x
+
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3
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c
2-
C
a,
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C
0
0
C
0
Glycogen phosphorylase activity
In muscle fibers of fed mice, the staining reaction for
total phosphorylase activity was strong in type IIA fibers and moderate in type IIB and atypical type I1 fibers
(Fig. 5). Phosphorylase a (active form) activity was undetected in muscle fibers of fed mice (Fig. 6).
After 2 days of starvation, the reaction for the total
activity was somewhat intense, although it was slightly
stronger in type IIB and atypical type I1 fibers than in
type IIA fibers. The reaction for phosphorylase a activity
appeared very weak in type IIA fibers and weak in type
IIB and atypical type I1 fibers.
After 4 days of starvation, the reaction for the total
activity became intense, although it was generally
stronger in type IIB fibers than in type IIA fibers (Fig.
11). The reaction for phosphorylase a activity became
moderate in type IIB and atypical type I1 fibers and
weak in type IIA fibers (Fig. 12).
Electron microscopy
Electron microscopic observations were carried out on
typical type IIA and IIB fibers, because atypical type I1
fibers could not be identified under the electron microscope. In fed animals, numerous glycogen particles (beta
particles) were observed in the sarcoplasm between myofibrils of all muscle fibers, particularly near the triad
(Fig. 13A,B). A few particles were occasionally present
in spaces between myofilaments. After 2 days of starvation, the particles decreased markedly, although a few
were still seen in the sarcoplasm between myofibrils a t
the I-bands (Fig. 14). The remaining particles appeared
more numerous in type IIA fibers than in type IIB fibers.
After 4 days of starvation, the particles almost disappeared (Fig. 15A), although a few granules were occasionally found in the sarcoplasm between myofibrils of
some type IIA fibers (Fig. 15B).
Biochemical Results
Glycogen content
Muscle glycogen content did not differ from values of
corresponding fed animals by 12 hours of starvation,
although the value decreased to 40% of that of animals
at the start of starvation (Fig. 16). After 24, 48, and 96
hours, the values became 23, 18, and 7% of that at the
v)
8
12
16
2
2,
3
"I
6
Hours of Starvation
Fig. 16. Glycogen content i n rectus femoris muscles of fed (open
column) and starved (dotted column) mice. Animals were starved from
6:OO A.M. Each point represents t h e mean of four mice and standard
error i s shown as a vertical line. The values of starved animals for 24
hours or longer are different significantly from values of corresponding
fed animals ( P < .001,.001,,001).Values at 12,24,48, and 96 hours of
starvation were not different from those of animals starved from 1O:OO
AM.
start of starvation-smaller than those of corresponding
fed animals (P < . 001, .001, .001). However, liver glycogen content already decreased after 8 hours to 27% of
that at the start of starvation ( P < . 02) and was 33% of
that of corresponding fed animals (P <. 02) (Fig. 17).
After 12 hours, the value became 3% of that at the start
of starvation, the minimal level.
There were no differences in values at 12, 24, 48, and
96 hours of starvation between animals starved from
6:OO A.M. and from 1O:OO A.M.
Glycogen phosphorylase activity
Total glycogen phosphorylase activity did not change
during 96 hours of starvation. However, phosphorylase
a activity increased between the start and 48 hours ( P
< .01)and markedly between 48 and 96 hours of starvation (P <. 05) (Fig. 18).
There were no differences in values between animals
starved from 6:OO A.M. and from 1O:Oo A.M.
Blood glucose
The values decreased to 44% of that in fed animals
after 24 hours of starvation and then remained unchanged (Table 1).
DISCUSSION
In the present results, PAS reaction for glycogen and
glycogen particles almost disappeared, and histochemical phosphorylase a activity increased in the muscle
fibers during 4 days of starvation. These are consistent
with our previous biochemical results on glycogen and
phosphorylase a activity in the rectus femoris muscle of
mice starved for 4 days and support our hypothesis on a
physiological role of skeletal muscle glycogen in starved
mice (Hirose et al., 1986).
272
M. SAKAIDA ET AL.
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Hours of Starvation
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Fig. 17. Glycogen content in the liver of fed (open column) and
starved (dotted column) mice. Animals were starved from 6:OO A.M.
Each point represents the mean of four animals and standard error is
shown as a vertical line. The values of starved animals for 8 hours or
longer are significantly different from values of corresponding fed
animals. ( P < .02, .05, ,001, ,001,.001).Values at 12, 24,48,and 96
hours of starvation were not different from those of animals starved
from 1O:OO A.M.
Phosphorylase a activity was higher and PAS reaction
for glycogen decreased more markedly in type IIB fibers
than in type IIA fibers after 2 and 4 days of starvation.
Type IIA fibers contain numerous mitochondria (Eisenberg and Kuda, 1976; Galvas et al., 1982) and the pathway of the aerobic glycolysis (Jobsis and Duffield, 1967;
Burke et al., 1973), whereas type IIB fibers have few
mitochondria (Eisenberg and Kuda, 1975; Galvas et al.,
1982) and the anaerobic glycolysis occurs in the fibers
(Burke et al., 1973). In type IIB fibers, G6P produced via
the glycogenolysis is converted into lactate by the anaerobic glycolysis (Conn and Stumpf, 1972; Burke et al.,
1973). Lactate thus produced is released into the blood
and changed via the Cori-cycle in the liver and kidney
into glucose that is released into the blood (Felig et al.,
1970; Kusaka and Ui, 1977). On the other hand, in type
IIA fibers, G6P is converted into pyruvate by the aerobic
glycolysis (Jobsis and Duffield, 1967; Burke et al., 1973).
During the process of the aerobic glycolysis, no metabolites that are sources of the blood glucose are released
from type IIA fibers (Conn and Stumpf, 1972; Burke et
al., 1973). Thus, via the anaerobic glycolysis and Coricycle, some of the glycogen in type IIB fibers is probably
used for maintaining the blood glucose level in starved
mice.
Ichihara and Ui (1974) and Kusaka and Ui (1977)
observed a decrease in glucose uptake and increase in
lactate production in skeletal muscles of epinephrinetreated rats. The authors noticed these changes to be
similar to changes in glucose and lactate in skeletal
muscles of starved animals and supposed that epinephrine is the most important factor regulating glucose
metabolism in skeletal muscle of starved animals. Further, the authors showed that, in rats injected with
epinephrine, most of the lactate released from the skeleta1 muscle into the blood is not derived from its glyco-
c
a
Hours of Starvation
Fig. 18. Phosphorylase activity in rectus femoris muscles of fed and
starved mice. Animals were starved from 6:OO A.M. Each point represents the mean of five animals and standard error is shown as a
vertical line. Total activity (open histogram dotted histogram) is not
changed but phosphorylase a activity (dotted histogram) increases
between the start and 48 hours (P < ,011and markedly between 48
and 96 hours of starvation ( P < .05).These values were not different
from those of animals starved from 1O:OO A.M.
+
TABLE 1. Blood glucose level (mgldl) of fed and
starved mice
Group
Blood glucose
Fed
at 10 A.M.
at 10 P.M.
Starved for:
12 hours
(at 10 P.M.)
24 hours
(at 10 A.M.)
48 hours
(at 10 A.M.)
96 hours
(at 10 A.M.)
219.8 k 9.57
192.1 k 27.91
131.4 f 17.04*
96.8 f 2.69**
89.6 k 12.24**
99.3 +
- 10.43**
+
Values are means
S.E. for five animals. *P < .05, **P < ,001:
Significantly different from the value of corresponding fed animals
(Student's t-test).
gen but from the blood glucose in spite of a marked
decrease in muscle glycogen by increased glycogen phosphorylase activity (Ichihara and Ui, 1974; Kusaka and
Ui, 1977). Therefore, if changes in glucose and lactate in
skeletal muscles of epinephrine-treated animals are similar to those of starved animals, most of the G6P produced via the glycogenolysis in skeletal muscles of
starved animals is possibly metabolized through a pathway other than the anaerobic glycolysis and Cori-cycle
mentioned above. We recently found G6Pase activity
and its marked increase by starvation in murine skeletal muscle fibers (Watanabe et al., 1986; Hirose et al.,
1986). It is therefore likelv that G6P derived from d v cogen in skeletal muscle; of starved mice is largely
hydrolyzed by G6Pase activity to produce glucose that
is released directly into the blood.
U
"
273
MUSCLE GLYCOGEN
Glycogen is more abundant in the white muscle containing numerous type I1 fibers than in the red muscle
including numerous type I fibers (Beatty et al., 1963;
Bocek et al., 1966).G6Pase activity is also higher in type
I1 fibers than in type I fibers Watanabe et al., 19861,
and it increases in both type IIA and type IIB fibers as
a result of starvation (Hirose et al., 1986). As shown in
the present study, decrease in glycogen and activation
of phosphorylase activity during starvation occur predominantly in type IIB fibers. Thus, type IIB fibers
possibly play a main role in releasing glucose into the
blood in starved mice.
ATP is shown to inhibit the activation of phosphorylase in the skeletal muscle of the rabbit (Sanner and
Tron, 1975; Kamogawa and Fukui, 1975). ATP production is four times more in aerobic glycolysis than in
anaerobic glycolysis (Fairly and Kilgour, 1966). Thus,
high ATP concentration is probably a cause of less phosphorylase activation in type IIA fibers than in type IIB
fibers. Other factors regulating phosphorylase activation-various hormones, such as insulin, glucagon, and
glucocorticoids, and the concentration of G6P, Ca++,
phosphorylase b-kinase, and others in the muscle fibers-are known. However, the detailed mechanism of
the regulation by these factors is unknown.
Liver glycogen decreased to 33%of that of corresponding fed animals after 8 hours and to the minimal level
(3%of the value of fed animals at the start of starvation)
after 12 hours. However, muscle glycogen content did
not differ by 16 hours from values of corresponding fed
animals, and it decreased gradually and became smaller
than those of corresponding fed animals after 24, 48,
and 96 hours. Thus, glycogen decrease in the liver precedes that in the skeletal muscle; glycogen in the muscle
is mobilized after its depletion in the liver in starved
mice. At the beginning of starvation, liver glycogen
maintains the blood glucose level and, after depletion of
liver glycogen, muscle glycogen is utilized to maintain
the blood glucose level. The blood glucose level decreased to 44% after 24 hours of starvation and then
remained unchanged. Some of the blood glucose after 24
or longer hours of starvation is probably derived from
muscle glycogen. However, the mechanism of such a
combination of the liver and muscle for glucose supply
to the blood in starved mice is unknown.
The amount of muscle protein decreases during starvation (Li et al., 1979; Hirose et al., 1986). Therefore,
protein catabolism in the muscle might be also related
t o the maintenance of blood glucose level in starved
animals. Felig et al. (1970) reported that alanine, produced by the breakdown of muscle protein and released
into the blood, serves as precursor for gluconeogenesis
in the liver (glucose-alaninecycle).However, Kusaka and
Ui (1977) showed that the amount of glucose produced
via the glucose-alanine cycle is very small in starved
animals. Further, Garlick et al. (1975) and Li et al.
(1979) found that the reduction in muscle protein in
starved animals is not due to an increase in the rate of
protein catabolism but is the result of a decrease in the
rate of protein synthesis.
In the present results, rectus femoris muscles of mice
contained no type I fibers, although Ariano et al. (1973)
reported the presence of at least a small percentage of
type I fibers in the muscles of the guinea pig, rat, cat,
lesser bushbaby, and slow loris. Moreover, rectus fe-
moris muscles of mice contained a few atypical type I1
fibers. Thus, the fiber type composition of the rectus
femoris muscle of the mouse is slightly different from
that of other species. Histochemical findings for fiber
type classification in atypical type I1 fibers were intermediate between those in type IIA and IIB fibers. The
fibers are probably “transitional fibers between type IIA
and type IIB fibers” as suggested by Wirtz et al. (1983).
The starved mice became less active than the fed mice
and appeared curled up after 2 or more days of starvation. Therefore, there is probably no necessity to consider the possibility that the glycogen depletion in the
muscle observed in the present study is due to high
activity of starved mice.
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muscle fiber populations in five mammals. J. Histochem. Cytochem. 21:51-55.
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Barka, T., and P.J. Anderson (1963) Histochemistry. New York: Harper
and Row, p. 314.
Beatty, C.H., R.D. Peterson, and R.M. Bocek (1963) Metabolism of red
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Godlewski, H.G. (1963) Are active and inactive phosphorylases histochemically distinguishable? J. Histochem. Cytochem., 11:108-112.
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(1986)Significance of the increase in glucose 6-phosphatase activity
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