Effects of nutritional level on muscle development, histochemical properties of myofibre and collagen architecture in the pectoralis muscle of male broilers.
ABSTRACT 1. The effects of nutritional level on muscle development, histochemical properties of myofibre and collagen architecture in the pectoralis muscle were evaluated using male broilers of Red Cornish x New Hampshire stock, reared on diets of high nutritional value for up to 80 d (H80d) and low nutritional value for up to 80 d (L80d, same age as H80d) or 95 d (L95d, same body weight as H80d). 2. The total live weight and the weight of pectoralis muscle were lower in L80d than in both H80d and L95d. The muscle weight as a percentage of live weight was 8.7% in L80d, 10.7% in H80d and 11.5% in L95d. 3. Pectoralis muscle was composed only of type IIB myofibres and showed no differences in myofibre type composition among the chicken groups. The largest diameter of type IIB myofibres was observed in L95d, followed by H80d and the smallest in L80d. 4. The total amount of intramuscular collagen did not differ among the chicken groups (1.92 to 1.99 mg/g). Types I and III collagens were immunohistochemically detected in both the perimysia and endomysia. The thin perimysia around the primary myofibre fascicles showed larger width in H80d than L80d and L95d, and also the thick perimysia around the secondary fascicles in H80d than L80d. 5. The collagen structure of the perimysium was most developed in H80d, followed by L95d and on the least in L80d. The development of perimysial collagen fibres could be enhanced by a rapid growth rate of the muscle induced by high nutritional level and depressed by a slow growth rate with low nutritional foods. 6. The endomysial collagen architecture was observed as a felt-like tissue of the fibril bundles with many slits. The thinnest endomysial wall was observed in L80d, followed by H80d and the thickest in L95d. 7. From these results, it was indicated that foods of high nutritional value could enhance growth of the pectoralis muscle of broilers, and this is accompanied by hypertrophy of the type IIB myofibres and development of the perimysial collagen architecture.
- Analytical Chemistry - ANAL CHEM. 04/2002; 35(12).
- Journal of Cellular and Comparative Physiology 02/2005; 15(1):11 - 34.
- [show abstract] [hide abstract]
ABSTRACT: The histochemical profiles of myofibers in Musculus pectoralis (PT) and M. supracoracoideus (SC) fasciculi were compared among Japanese quail strains with large, normal and small body sizes. In male and female adults, both the PT and SC muscles had attained a 2.5–2.7-fold weight gain in the large strain and conversely a 0.43–0.50-fold change in the small strain relative to those of the normal size. The muscles were composed of fasciculi with a central cluster of type IIA fibers surrounded by a peripheral layer of type IIB fibers. In the large strain, the cross sectional area (CSA) of the fasciculus and CSA of the fibers in each type were significantly enlarged compared with those in the normal size, with the exception of the fasciculus in the deep region of the male PT muscle. The hypertrophied type IIA fibers in the large strain showed considerable variation in nicotinamide adenine dinucleotide dehydrogenase activity, some of which might represent a transitional form into type IIB fibers. In the small strain, the fasciculus CSA did not significantly differ from that of the normal size except for the PT surface region of the male. However, fiber atrophy was observed in type IIB fibers of the PT surface region in both sexes, and type IIA fibers of the PT deep region and SC muscle in the small strain male quails. The relative fiber type composition of a fasciculus in each region showed only a slight change across the strains. These results indicate that breast muscle hypertrophy in the large strain could be based mainly on fasciculus and fiber hypertrophy, but muscle atrophy in the small strain is not induced by fasciculus and fiber atrophy.Animal Science Journal 03/2003; 74(2):111 - 118. · 1.04 Impact Factor
British Poultry Science Volume 47, Number 4 (August 2006) pp. 433—442
Effects of nutritional level on muscle development, histochemical
properties of myofibre and collagen architecture in the pectoralis
muscle of male broilers
B.C. ROY, I. OSHIMA, H. MIYACHI1, N. SHIBA2, S. NISHIMURA3, S. TABATA3AND
Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka-shi,
1Yokoo & Co., Ltd, Tosu-shi,2National Agriculture Research Centre for Tohoku Region, Morioka-shi, and
3Faculty of Agriculture, Graduate School, Kyushu University, Fukuoka-shi, Japan
myofibre and collagen architecture in the pectoralis muscle were evaluated using male broilers of Red
Cornish?New Hampshire stock, reared on diets of high nutritional value for up to 80d (H80d) and low
nutritional value for up to 80d (L80d, same age as H80d) or 95d (L95d, same body weight as H80d).
2. The total live weight and the weight of pectoralis muscle were lower in L80d than in both H80d
and L95d. The muscle weight as a percentage of live weight was 8?7% in L80d, 10?7% in H80d and 11?5%
3. Pectoralis muscle was composed only of type IIB myofibres and showed no differences in myofibre
type composition among the chicken groups. The largest diameter of type IIB myofibres was observed
in L95d, followed by H80d and the smallest in L80d.
4. The total amount of intramuscular collagen did not differ among the chicken groups (1?92 to
1?99mg/g). Types I and III collagens were immunohistochemically detected in both the perimysia and
endomysia. The thin perimysia around the primary myofibre fascicles showed larger width in H80d than
L80d and L95d, and also the thick perimysia around the secondary fascicles in H80d than L80d.
5. The collagen structure of the perimysium was most developed in H80d, followed by L95d and on the
least in L80d. The development of perimysial collagen fibres could be enhanced by a rapid growth
rate of the muscle induced by high nutritional level and depressed by a slow growth rate with low
6. The endomysial collagen architecture was observed as a felt-like tissue of the fibril bundles with many
slits. The thinnest endomysial wall was observed in L80d, followed by H80d and the thickest in L95d.
7. From these results, it was indicated that foods of high nutritional value could enhance growth of the
pectoralis muscle of broilers, and this is accompanied by hypertrophy of the type IIB myofibres and
development of the perimysial collagen architecture.
1. The effects of nutritional level on muscle development, histochemical properties of
The breast is the most valuable part of the
chicken carcase and the pectoralis muscle is about
50% of the breast meat (Iwamoto and Takahara,
1971). When the pectoralis muscle plays an
important role as the exclusive wing depressor,
it attains sometimes one-quarter of body weight
in strongly flying wild birds (Raikow, 1985;
Vollmerhaus, 1992). However, in a poor flyer
such as the domestic chicken, the pectoralis is
about 10% of body weight in spite of being the
largest of all muscles (Iwamoto and Takahara,
1971; Ono et al., 1993; Nakamura et al., 2004b).
Correspondence to: Professor H. Iwamoto, Division of Animal and Marine Bioresource Sciences, Faculty of Agriculture, Kyushu University, Fukuoka-shi
812-8581, Japan. E-mail: email@example.com
Accepted for publication 24th April 2006.
ISSN 0007–1668(print)/ISSN 1466–1799 (online)/06/040433—10 ? 2006 British Poultry Science Ltd
Generally the pectoralis muscle as the main
propulsive organ of flight is composed of fast-
twitch glycolytic-oxidative (type IIA) myofibres
for sustaining the muscle activity and fast-twitch
glycolytic (type IIB) for a burst contraction.
In the chicken the pectoralis muscle is composed
of only type IIB myofibres but in the Japanese
quail, with greater flying ability, it contains
much type IIA and little type IIB (Suzuki, 1978;
Ono et al., 1993; Iwamoto et al., 2003).
Poultry meat is a concentrated source of
protein that has a high biological value because
it contains all essential amino acids for human
nutrition. Meat proteins are generally grouped
into three categories: sarcoplasmic proteins,
(connective tissue protein). Myofibrillar proteins
constitute the major protein fraction of meat and
represent approximately 50% of total proteins of
muscle tissue (Ito et al., 2003). Collagens, fibrous
molecules (Light et al., 1985), are the major
protein constituents of perimysial and endomy-
sial connective tissue and account for about 2 to
6% of dry weight of muscle (Dransfield, 1977).
As the meat productivity of broilers is 85 to
90% under genetic control, it is only the
remainder that the environmental factors can
influence (Sherwood, 1977; Havenstein et al.,
2003). However, the nutritional level of the diet,
which is the major environmental factor, has to
be controlled for a broiler to demonstrate its
maximum genetic potential for meat production
(Marks, 1993), because the nutritional level
has an intimate relation with the endocrine or
paracrine mechanisms for regulating muscle
responds markedly to nutritional alteration and
the red gastrocnemius is less sensitive (Tesseraud
et al., 1996). The fast-twitch glycolytic myofibre
may be responsible for the rapid increase of
the white muscle mass based on increase of the
myofibre size (Henkel, 1991; Velotto and Crasto,
The overall eating quality of a muscle is
determined by the properties of the two major
components, myofibre and connective tissue,
and their interactions (Ramsey and Street,
1940). The perimysium occupying the vast bulk
(about 90%) of the intramuscular connective
tissue should have a major role in determining
the meat texture related to connective tissue
(Light et al., 1985; McCormick, 1999). Meat-type
birds also show a compensatory growth of muscle
induced by recovering the nutritional level after
a period of feed restriction (Washburn and
Bondari, 1978; Acar et al., 2001).
A series of studies for regulating the relative
distribution of skeletal muscles on the forelimbs
and hindlimbs by feeding food of different
nutritional levels has been organised in the
present paper. Firstly, the effects of different
nutritional levels throughout the experimental
period on the relative muscle distribution are
examined and also the morphological changes of
the pectoralis, iliotibialis lateralis and puboischiofe-
moralis muscles are observed. The present study
was intended to evaluate the effects of nutritional
level on the muscle weight, percentage distribu-
tion of myofibre types, and collagen content and
architecture in the pectoralis muscle using the
birds reared with general broiler foods up to 80d
and with lower nutritional value diets up to 80d
(same age) or 95d (same mean body size).
MATERIALS AND METHODS
Chicks, husbandry and diet composition
Male Red Cornish (8)?New Hampshire (9)
(RN, Shaver, Fort Medoc, France) birds were
reared on diets of high nutritional value for a
broiler for 80d (H80d) and on diets of lower
nutritional value for a layer for 80d (L80d) or
95d (L95d) at Yokoo & Co., Ltd (Tosu, Japan).
One-day-old sexed male birds were randomly
allocated to three floor pens (25 chicks/pen;
1?8m?1?8m) in an experimental facility using
litter on a concrete floor. Each pen was for one
group of chicks and equipped with two tube
feeders and one drinker. Feed and water were
provided ad libitum. The averaged group weight
chicks were selected for the experiment. The
chemical compositions of the foods are shown
in Table 1, for which the starters were fed in the
first period of 21d after hatching and thereafter
The chickens were killed by bleeding the
carotid arteries under deep anaesthesia induced
(1ml/kg body weight) into the brachial vein
and the skinned carcases were fully immersed
in ice—water for about 20min. Pectoralis muscles
(Raikow, 1985; Vollmerhaus, 1992) were taken
from both sides and weighed after cleaning out
the peripheral fatty tissue and tendon. Two small
tissue samples (about 1cm3), with parallel myo-
fibre striation, were cut out from the centre
of the ventral belly with longer myofibres of
the muscle. One of the samples was fixed
in glutaraldehyde (20ml/l)—paraformaldehyde
(20ml/l) in a 0?02M phosphate buffer solution
(pH 7?4, PBS) for several days at 4?C for scanning
electron microscopy, and another was frozen
with dry ice—acetone mixture and stored at
?50?C until used for histological preparation.
The other materials (up to 5g) were taken off the
epimysium, frozen with dry ice and stored at
?50?C until used for measuring the total amount
B.C. ROY ET AL.
Histochemical methods and myofibre
Serial frozen sections (8mm thick) were obtained
from the frozen tissue and stained by the
histochemical reactions for myosin adenosine
triphosphatase activities (Padykula and Herman,
1955) after acid (pH 4?3) and alkaline (pH 10?5)
preincubation (Brooke and Kaiser, 1969) and
dehydrogenase (NADH-DH) activity (Okamoto
et al., 1976). Using microscopic photographs
(?250) of the specimen, all of the total 500 to
800 myofibres in each sample were categorised as
type IIB and the diameters of 350 myofibres
were measured as the maximum dimension
perpendicular to its long axis according to the
method of Iwamoto et al. (1992).
The frozen sections were also used to detect
types I and III collagens by immunohistochem-
istry after pre-treatment with a normal goat
serum (10ml/l) (Sigma-Aldrich, St Louis, MO,
USA) in PBS (Hsu et al., 1981). In this method,
rabbit anti-chicken collagen type I polyclonal
antibody and type III (Chemicon International,
Temecula, CA, USA), which were diluted to
1:500 with PBS, were used as primary antibody
and a biotinylated goat anti-rabbit IgG as
secondary with avidin—biotin conjugate (ABC)
CA, USA). Combined peroxidase activity was
drochloride (1ml/l). The thickness of perimy-
sium was measured at 5mm intervals along thick
perimysia around secondary myofibre fascicles
and thin perimysia around primary myofibre
fascicles on 3 to 5 micrographs of immunohisto-
chemical staining of type I collagen, obtained
from each of 6 birds for each group. The mean
thickness was estimated from the measured
Determination of total collagen content
A sample solution was prepared according to
the method of Hill (1966). After isopropanol,
an oxidant solution (7% w/v chloramine T,
1 volume, and acetate/citrate buffer, pH 6?0, 3
volumes) and Ehrlich’s reagent were added to
each sample, the sample was then incubated
at 60?C for 25min and cooled to 20?C followed
by dilution with isopropanol. Within 4h of
sample preparation, spectrophotometric deter-
minationof the hydroxyproline
was carried out (Bergman and Loxley, 1963).
Because skeletal muscle collagen contains 13?3%
hydroxyproline, total collagen content was calcu-
lated by the multiplication of the hydroxyproline
content by 7?25 (Goll et al., 1963; Cross et al.,
1973). To measurecollagen
replicates were used for each group of this
Preparation for scanning electron
The fixed material was sliced transversely with
a razor followed by maceration in 2 N NaOH for
5d with slight modification of the methods of
Tabata et al. (1995). The macerated specimens
were rinsed in distilled water for 3d at 25?C,
treated with tannic acid (10ml/l) for 2h and
postfixed with osmium tetroxide (10ml/l) solu-
tion for 2h. After dehydration in a graded
series of ethanol, the specimens were placed in
t-butyl alcohol and freeze-dried (TIS-U-DRY, FIS
Systems, New York, USA) (Inoue and Osatake,
1988). The specimens were mounted on alumi-
nium holders and coated with Pt—Pd (Eiko IB3,
Hitachinaka, Japan). The collagen architecture
of the muscle was examined under a scanning
electron microscope (SEM, Super Scan SS-550,
Shimadzu, Kyoto, Japan) at an accelerating
voltage of 15kV. The width of the collagen
fibres on the perimysium was measured on
the higher magnified (>2000 times) electron
group, 5 photographs were used to measure at
least 20 collagen fibres on three points of
each and the mean width was estimated from
Table 1. Chemical composition of starter and finisher diets in the high and low nutritional groups
CompositionStarter dietsFinisher diets
Crude protein (g/kg)
Ether extract (g/kg)
Crude fibre (g/kg)
Metabolisable energy (MJ/kg DM)
NUTRITIONAL EFFECTS ON PECTORALIS
Means and standard errors were calculated
among the birds and the t-test was used to look
for significant differences between the broiler
groups in items of live weights, muscle weights,
myofibre diameters, collagen contents, perimy-
sial width and collagen fibre width.
Live weights, muscle weights and
Growth rates were markedly affected by the
different nutritional levels, with H80d gaining
600g more live weight than L80d at the same age.
The broilers reared with the lower nutritional
foods (L95d) required 15d more to reach the
same live weight as the birds fed the higher
nutritional foods (H80d) (Table 2). The total
weight of pectoralis muscles from both sides was
significantly smaller in both absolute weight and
the percentage weight of live weight in L80d than
the other two. From these results, H80d chicken
with the fast body growth seemed to show
production of breast meat. All three groups
The myofibre diameter was the smallest in L80d
and the largest in L95d, and H80d showed only
a little butsignificantly
compared to L95d.
Collagen content and architecture
total amountof collagen
(Table 2). Types I and III collagens were detected
immunohistochemically in both the perimysia
and endomysia of pectoralis muscle (Figure 1a
to f). The endomysia of both collagens surround-
ing each myofibre revealed a network structure
with rather even mesh size within primary
myofibre fasciculus. Each
rounded by thin perimysium, and then several
primary fasciculi were bound together by thick
perimysium as the secondary fasciculus. Both
thin and thick perimysia in H80d showed
the largest width of all chicken groups with one
the thick perimysia between H80d and L95d.
The thick perimysial width was significantly wider
in L95d but the thin perimysia did not differ
significantly between L80d and L95d at the 5%
level (Table 2). On the other hand, closer mesh
size of endomysium was observed in L80d
because of the smaller myofibre size. Low
magnification SEM photographs showed the
endomysial honeycomb structure with empty
cells after resolving out myofibres and the thicker
perimysial bands with many slits as results of
shrinkage during preparation (Figure 2a to c). No
development of adipose tissue was recognised in
The perimysia exhibited different collagen
structures among the chicken groups, namely,
stacks of collagen plates in H80d (Figure 3a), very
loose tissue of slender collagen fibres in L80d
(Figure 3b) and denser tissue of the slender fibres
in L95d (Figure 3c). In H80d the central thick
collagen layer was composed of several fibres
crossing over each other showing a wave-like
course (Figure 4a), then the fibres were made of a
compact arrangement of collagen fibrils or
Table 2. Live weight, muscle weight, myofibre type composition and myofibre diameter, collagen
content and collagen fibre size, and perimysial width in the pectoralis muscle
No. of birds
Live weight (g)
% of live weight
Type IIB (%)
Total amount (mg/g)
Fibre width (mm)1
Perimysial width (mm)
a?cMeans with same letter did not differ significantly (5%) between treatments.
1Width of circular collagen fibres in thick perimysia.
B.C. ROY ET AL.
bundles (Figure 4b). The other fibres also were
very large and showed a smooth surface of
compact fibrils with rather parallel but waving
striation (Figure 4c). There were many slender
fibres and fibril bundles around the thick fibres.
The mean width of circular collagen fibres
observed in the thick perimysia of H80d was
5?62?0?39mm, which was at least twice those of
L80d and L95d (Table 2).
On the other hand, in L80d the slender
collagen fibres, which consisted of loose tissue
of the separate fibrils or bundles, were more
the growth period of 80 to 95d in the low
nutrition chickens, the collagen architecture
had maintained the loose tissue of slender fibres
(Figure 6a). However, each collagen fibre was
composed of a compact arrangement of the fibrils
or bundles having a smooth surface (Figure 6b).
Development of large collagen fibres as in H80d
could not be observed in L95d, of which pectoralis
muscle gained rather larger weight. Mean width
of circular collagen fibres in the thick perimysia
was 2?56?0?21mm in L80d and 2?69?0?19mm in
L95d (Table 2).
A felt-like endomysial wall consisted of
collagen fibrils where the main circular fibrils
were crossed over by oblique and longitudinal
fibrils. Some of the fibrils were combined into
little thicker bundles and strengthened the
endomysial wall by repeating branching off and
joining together with each other (Figure 8).
Although the fundamental architecture did not
differ, the endomysium in L80d appeared like
silk with a light and semi-transparent quality
(Figure 7b). In H80d more collagen fibrils or
bundles were deposited in the endomysium
(Figure 7a) and in L95d the fibrils or bundles
Figure 7(c) looks like a plate with only a
few foramina, its more detailed structure, com-
prising many slits with various dimensions
between the fibrils, is shown in Figure 8.
The detailed structures in L80d and H80d
microphotographs not shown here. The endo-
mysial collagen tissue was most rough in L80d,
followed by H80d and the densest structure was
observed in L95d.
(a, b), L80d (c, d) and L95d (e, f). Bars indicate 90mm.
Immunohistochemically detected type I collagen (left side) and type III (right side) in the pectoralis muscles from H80d
NUTRITIONAL EFFECTS ON PECTORALIS
supracoracoideus and iliotibialis lateralis, show a
positive allometric relationship with live weight
which is subject to age and breed variations (Ono
et al., 1989; Iwamoto et al., 1992), the rapid
increase in live weight induced by genetic or
environmental factors is a good trait for quanti-
tative chicken production. It is also reported that
breast yield of chicken gradually increases in the
post-hatching growth up to 85d (Havenstein
et al., 2003). In the present study, H80d broilers
could produce pectoralis muscle of the same
volume in a growth period of 15d shorter
duration compared with L95d with the same
several muscles,such as pectoralis,
body size, and a higher percentage of pectoralis
muscle than the L80d that have lower live
As muscle growth is based on parallel
increases in both myofibre length and diameter
until 15 weeks of age (Iwamoto et al., 1993), the
myofibre diameter can be compared directly
between the present chickens of 80d and 95d.
In the pectoralis muscle of the present study, the
myofibre diameter increased in relation to
the increase in the muscle weight regardless of
the different growth rates. From these results it
appeared that diets of high nutritional value
could accelerate the muscle growth induced by
development of the myofibres. The pectoralis
the thick perimysia of the pectoralis muscles in H80d (a),
L80d (b) and L95d (c).
Middle magnification SEM photographs showing
pectoralis muscles from H80d (a), L80d (b) and L95d (c).
Low magnification SEM photographs of the
B.C. ROY ET AL.
muscle of chicken was composed of only type IIB
as in previous reports (Sams and Janky, 1990;
Ono et al., 1993). The type IIB (fast-twitch
glycolytic) myofibres are the most sensitive to
(Tesseraud et al., 1996) and in rats (Baillie and
The total amount of collagen in the pectoralis
muscle of chicken increases during the short
period 33 to 52d (Nakamura et al., 1975) and
conversely decreases during the longer term of 2
to 14 weeks (Nakamura et al., 2004b). It could be
that age-related changes in collagen content are
very small in chickens compared with those of
Figure 4. Middle (a) and high (b, c) magnification SEM photographs of the thick perimysia in the pectoralis muscle from H80d.
Figure 5.Middle (a) and high (b) magnification SEM photographs of the thick perimysia in the pectoralis muscle from L80d.
Figure 6. Middle (a) and high (b) magnification SEM photographs of the thick perimysia in the pectoralis muscle from L95d.
NUTRITIONAL EFFECTS ON PECTORALIS
porcine and cattle muscles (Nishimura et al.,
1996; Fang et al., 1999). Nakamura et al. (2004b)
3?94mg/g at 2 weeks, the amount at 11 weeks
was 3?33mg/g, and the smallest at 14 weeks was
2?88mg/g. In the present study, the total amount
of collagen was 1?92 to 1?99mg/g, showing no
difference between different nutritional groups
(H80d and L80d) and no age-related change
(L80d and L95d). These results were rather
similar to 1?71mg/g in normal broilers at 53d
(Nakamura et al., 2004a).
As the perimysium contains mainly types I
and III collagens and the endomysium types I, III
and IV (Listrat et al., 1997), the immunohisto-
chemical reactions for types I and III are positive
in both perimysium and endomysium in the
bovine, porcine and chicken muscles (Nishimura
et al., 1999; Nakamura et al., 2003, 2004a). From
these results, the perimysial and endomysial
collagen bundles or fibres seem to be composed
of a mixture of type I and III fibrils. However,
the major component is type I collagen fibrils
(Nishimura et al., 1997; Listrat et al., 1999). H80d
showed thicker perimysia in the immunostained
preparation compared with L80d and L95d. It is
also reported that a rapid growth of the pectoralis
congenital large body size makes the perimysial
width thicker compared with Red Cornish?
New Hampshire (80d) of the same body size
(Nakamura et al., 2004a). Conversely, indigenous
Thai chicken with very small body size attain
wider perimysia in the pectoralis muscle at
16 weeks of age than the normal broilers of
38d with the same body weight (Wattanachant
et al., 2005).
It is reported that a high energy diet
enhances a deposit of collagen, especially inso-
luble (Crouse et al., 1985). In the perimysium of
the pectoralis muscle of adult Silky fowls, a stack
of several collagen platelets parallel to the
circumference of myofibre fasciculi are observed
(Nakamura et al., 2003). In the present study, the
chickens (H80d) fed on high energy diets had
thick perimysia with large collagen fibres com-
posed of compact accumulated fibrils. When the
large collagen fibres were observed in a low
features resembled a stack of collagen platelets
in the Silky fowls. On the other hand, the
collagen fibres in the chicken (L80d) reared on
Figure 7.Middle magnification SEM photographs of endomysia of the pectoralis muscles in H80d (a), L80d (b) and L95d (c).
endomysium of the pectoralis muscle in L95d.
B.C. ROY ET AL.
low energy diet were arrested at the undeveloped
slender states showing a loose tissue of the fibrils
or bundles. After a further 15d elongation of the
feeding period, the collagen fibres in L95d had
maintained similar size as in L80d but consisted
of a dense tissue of the fibrils or bundles. From
these results, it was suggested that the high or low
nutritional levels used in this study could affect
a prominent influence on the development of
perimysial collagen bundles or fibres.
Development of the endomysial collagen
network may be affected by the nutritional level
because of different features of endomysium
between H80d and L80d. However, as L95d
chicken showed a more developed state of the
endomysium than H80d, the endomysial devel-
opment seemed to be affected by the different
functional demands of the myofibres, when they
showed the largest diameter in L95d, the second
in H80d and the smallest in L80d.
Although the total amount of collagen did
not differ among the chicken groups, their
intramuscular collagen architecture did differ.
The rapid growth rate of the pectoralis muscle
induced by feeding high nutritional value diets
was accompanied by myofibre hypertrophy and
the development of large perimysial collagen
bundles or fibres. The perimysial collagen devel-
opment was a special feature of the chicken
(H80d) fed on high nutritional value diets, while
myofibre hypertrophy was also seen in L95d that
obtained the same muscle weight as in H80d.
We express many thanks to the staff of the Centre
University, for good advice and help with the use
of the scanning electron microscopy.
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