Livestock Science: Y.M. Choi, B.C. Kim

Review article
Muscle ber characteristics, myobrillar protein isoforms, and meat quality

Y.M. Choi, B.C. Kim
Division of Food Bioscience and Technology, College of Life Sciences and Biotechnology, Korea University, 5-1 Anam-dong, Sungbuk-gu, Seoul 136-713, South Korea
a r t i c l e i n f o a b s t r a c t
Article history:
Received 24 August 2007
Revised 27 August 2008
Accepted 27 August 2008
The objectives of this review were to examine the present knowledge on: (1) the muscle ber
characteristics of skeletal muscle, (2) the diversity of the myobrillar protein isoforms and their
relationship to muscle ber characteristics, and (3) the understanding of howthe effects of the
ber characteristics and protein isoforms inuence postmortem metabolism and meat quality,
including the technological aspects and sensory characteristics of meat. The histochemical
characteristics of skeletal muscle are primarily the result of genetic and environmental factors,
including gender, muscle type, breed, age, hormones, exercise, etc. The morphological and
biochemical characteristics of muscle ber are factors that inuence energy metabolism in
living muscle, but they inuence postmortem muscle as well. Muscle bers are divided into
various types, depending on the myosin heavy chain (MHC) isoforms they express. Moreover,
not only the MHC, but also the myosin light chain, troponin, and tropomyosin isoforms can
inuence muscle ber characteristics. On this basis, the isoform composition of myobrillar
protein can inuence postmortem rigor development, and consequently, meat quality. Hence,
muscle ber characteristics and myobrillar protein isoforms are very useful indicators for
examining variations in muscle metabolism at the postmortem period as well as ultimate meat
quality. Moreover, such characteristics from live animals can be used to predict meat quality
and can be applied in selection programs to improve and control meat quality. Still, however,
the effects of the protein isoforms on ultimate meat quality are not yet fully understood.
Therefore, to practically apply this knowledge for the improvement and control of meat quality,
more information must be gathered on how histochemical and biochemical characteristics
inuence meat quality in livestock.
2008 Elsevier B.V. All rights reserved.
Keywords:
Myobrillar protein isoforms
Muscle ber
Meat quality
Contents
1. Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 106
2. Muscle ber characteristics . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 106
2.1. Muscle ber . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 106
2.2. Classication of muscle ber type . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 106
2.3. Characteristics of muscle ber types . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 108
2.4. Factors inuencing histochemical characteristics . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 109
3. Diversity of myosin and other myobrillar protein isoforms . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 110
3.1. Myosin isoforms . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 110
3.2. Other protein isoforms . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 111
3.3. Relationships between myobrillar protein isoforms and muscle ber types . . . . . . . . . . . . . . . . . . . . . 112
4. Muscle ber type, myobrillar protein isoforms, and meat quality . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 113
4.1. Muscle ber type, MHC isoforms, and meat quality . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 113
4.2. Other protein isoforms and meat quality . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 114
Livestock Science 122 (2009) 105118
Corresponding author. Tel.: +82 2 3290 3052; fax: +82 2 925 1970.
E-mail address: bckim@korea.ac.kr (B.C. Kim).
1871-1413/$ see front matter 2008 Elsevier B.V. All rights reserved.
doi:10.1016/j.livsci.2008.08.015
Contents lists available at ScienceDirect
Livestock Science
j our nal homepage: www. el sevi er. com/ l ocat e/ l i vsci
5. Conclusions . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 114
Acknowledgement . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 115
References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 115
1. Introduction
Skeletal muscle is a very heterogeneous tissue that is
composed of a large variety of functionally diverse ber types.
One of the unique features of skeletal muscle is its numerous
ber types and their distinct functional characteristics and
compositions, which contribute to a variety of functional
capabilities (Pette and Staron, 2001). These ber types differ
according to their molecular, metabolic, structural, and
contractile properties, and thus, can be grouped according
to various parameters, including myobrillar protein iso-
forms, metabolic enzyme proles, and structural and con-
tractile properties (Schiafno and Reggiani, 1996; Bottinelli
and Reggiani, 2000). Therefore, the morphological and
biochemical characteristics of muscle ber types are major
factors that inuence energy metabolism within the skeletal
muscles of live animals, as well as during the postmortem
conversion of muscle to meat (Ryu and Kim, 2005, 2006).
Skeletal muscle bers are characterized by their precise
organization of contractile and regulatory proteins into
striated myofbrils, which result fromrepeating units arranged
in series, also known as sarcomeres. The ultra-structure and
molecular composition of the sarcomere are remarkably
similar among different muscle ber types. However, under-
lying this apparent uniformity there is also a high degree of
molecular variability, due to the existence of multiple
isoforms of each myobrillar component (Schiafno and
Reggiani, 1996; Clark et al., 2002).
A protein isoform is a version of a protein having only
small differences to another isoform of the same protein, and
the slight diversity within their amino acid sequences gives
rise to different structural and functional properties (Schiaf-
no and Reggiani, 1996). This diversity is generated based on
gene regulation through two main mechanisms (Bottinelli
and Reggiani, 2000). The rst is a qualitative mechanism
where the isoforms can be derived from the same gene
through alternative splicing or from different genes of the
same family, and the replacement of isoforms generates
diversity among the muscle bers. The second is a quantita-
tive mechanism in which many genes can be up- or down-
regulated independently of each other on the basis of factors.
Therefore, the proportion between the products of these
genes is modied, and new functional or structural features
appear.
In particular, myosin is the most abundant muscle
protein, and myosin isoforms determine the histochemical
ATPase reaction; hence, ber types are often indicated by the
name of the myosin isoform that is expressed (Bottinelli and
Reggiani, 2000). Therefore, myosin isoforms are generally
considered the molecular markers of the muscle ber type.
During muscle contraction, the myosin isoforms work
together with other myobrillar proteins, especially tropo-
nin and tropomyosin, which have different isoforms (Botti-
nelli and Reggiani, 2000). Based on this, the isoform
compositions of the myobrillar proteins inuence the
contractile and biochemical properties of muscle (Schiafno
and Reggiani, 1996; Bottinelli, 2001; Stephenson, 2001),
along with postmortem rigor development, and conse-
quently meat quality, particularly in pork (Gil et al., 2003;
Choi et al., 2007), cattle (Olivan et al., 2004; Muroya et al.,
2007), rabbit (Ramirez et al., 2004), and sheep (Sazili et al.,
2005).
The objectives of this review were to examine the present
knowledge pertaining to muscle ber type characteristics.
Here we describe the molecular diversity of myobrillar
proteins, especially myosin, troponin, and tropomyosin in
skeletal muscle, as well as discuss the diversity of the
myobrillar protein isoforms in relation to the characteristics
of each muscle ber type. Additionally, this reviewspecically
focuses on recent developments contributing to our under-
standing of how the effects of the ber characteristics and
protein isoforms inuence postmortemmetabolismand meat
quality.
2. Muscle ber characteristics
2.1. Muscle ber
Skeletal muscle ber is made up of multinucleate,
membrane-bound cells that are typically 10 to 100 m in
diameter, and their lengths can vary from several millimeters
to more than 30 cm (Bechtel, 1986). This myobril striation
pattern repeats with a periodicity of approximately 2 to 3 m,
and in vertebrate muscle, the sarcomere is a complex
structure containing at least 28 different proteins (Craig and
Padron, 2003).
The diversity of skeletal muscle can be attributed to
the heterogeneous characteristics of the individual muscle
bers and the mosaic composition of the numerous ber
types (Schiafno and Reggiani, 1996; Bottinelli and Reggiani,
2000). Fiber type composition can vary markedly in different
species and muscle types, depending on function (Klont et al.,
1998). Moreover, there are many factors that contribute
to ber type variation, such as sex (Ozawa et al., 2000), age
(Candek-Potokar et al., 1998), breed (Ryu et al., 2008),
hormones (Florini et al., 1996), and physical activity (Jurie
et al., 1999). These ber type variations differ according to
their molecular, metabolic, structural, and contractile proper-
ties (Schiafno et al., 1989). Therefore, having an under-
standing of such muscle ber characteristics is important for
the study of overall muscle characteristics and subsequent
meat quality.
2.2. Classication of muscle ber type
Histochemical staining techniques can be used to describe
the complex characteristics of muscle and to identify different
muscle ber types (Morita et al., 2000; Ozawa et al., 2000).
Different histochemical identication methods for muscle
ber types have been introduced over the years (Fig. 1). The
106 Y.M. Choi, B.C. Kim / Livestock Science 122 (2009) 105118
various ber type classications have focused on one, or a few,
aspects of contractile and metabolic performance, and have
dened ber types based on select parameters (Bottinelli and
Reggiani, 2000). All classications have been applied to
animal muscle.
The most commonly accepted form of classication in
muscle biology is based on differences in the acid and alkaline
stability of the myosin ATPase reaction (Brooke and Kaiser,
1970). Myosin ATPase histochemistry is proven to be useful
for the delineation of ber types. Brooke and Kaiser (1970)
dened the method with a range of pH preincubations, and
were able to distinguish three ber types that included ber
types I, IIA, and IIB. Fiber type I showed a stable, high ATPase
activity after preincubation at either pH 4.3 or 4.6, but it
showed lowATPase activity after preincubation at pH10.4. On
the other hand, type IIB was strongly reactive after pre-
incubation at pH 10.4, and negative after preincubation at
pH 4.3. Type IIA showed a strong reaction after preincubation
at pH10.4, but no reaction after preincubation at pH4.3 or 4.6
(Lind and Kernell, 1991).
Fig. 1. Representative staining of muscle ber cross-sections. A, myosin ATPase staining after acid preincubation (pH 4.3); B, myosin ATPase staining after acid
preincubation (pH 4.6); C, myosin ATPase staining (pH 9.4); D, SDH staining; E, NADH-tetrazolium reductase staining; F, phosphorylase staining; G, Sudan black B
staining; H, H & E staining. Cited and modied from Picard et al. (1995), Ryu (2004), and http://neuromuscular.wustl.edu/lab/mbiopsy.htm#bertype.
Muscle ber typing is based on the histochemical reac-
tions of oxidative capacity, using the enzyme succinate
dehydrogenase (SDH), and of glycolytic capacity, using the
enzyme NADH-tetrazolium reductase (NADH-TR) (Rahelic
and Puac, 1981; Baker and Santer, 1990). Three major ber
types have been distinguished: red, intermediate, and white
bers. Red bers are known to contain higher levels of en-
zymes that are involved in oxidative metabolism and lower
levels of glycolytic enzymes, and have higher myoglobin
contents than white bers. On the other hand, intermediate
bers have characteristics that are intermediate between
red and white bers, and they display both oxidative and
glycolytic capacities (Dubowitz and Pearse, 1960; Jurie et al.,
1999).
Muscle bers are unique and have a continuumof different
properties. Therefore, the classication of different types is
used for convenience, and it reects the actual properties of
individual bers. However, selecting different methods for
ber typing can give differing results for serial sections of the
same bers (Picard et al., 1998) (Fig. 2). According to Staron
(1997), within each myosin ATPase-based ber type there is a
wide range of variation in metabolic enzyme activity, and
furthermore, a large overlap has been found in the structural
and functional properties between bers belonging to dif-
ferent ber types (Picard et al., 1998). As a result, attempts to
combine metabolic enzyme classication with myosin ATPase
classication have generally been unsuccessful (Bottinelli and
Reggiani, 2000). For example, the single ber analysis of
enzyme activity shows a continuum distribution of aerobic
enzyme activity as well as anaerobic enzyme activity, regard-
less of the type dened by the myosin ATPase activity (Pette
et al., 1981; Pette and Spamer, 1986). Moreover, within all
species, both classications only apply to fully differentiated
adult muscle bers, and have limitations for muscle that is
developing, degenerating, or regenerating, as well as for spe-
cic muscles such as masticatory and extraocular muscles
(Bottinelli and Reggiani, 2000).
More recently, the utilization of immuno-histochemistry
with poly- and monoclonal antibodies, and the use of mRNA
expression by in-situ hybridization, have constituted power-
ful approaches to muscle ber typing (Smerdu et al., 1994;
Ennion et al., 1995). Antibody and mRNA staining has led us to
recognize that four myosin heavy chain (MHC)-based ber
types are present: I, IIA, IIX, and IIB.
2.3. Characteristics of muscle ber types
The functional, structural, and metabolic characteristics of
the four major muscle ber types differ in adult animals
(Bottinelli and Reggiani, 2000). Fiber type I, or slow-twitch
bers, generate energy for ATP resynthesis predominantly by
aerobic energy transfer. They possess a low myosin ATPase
activity level and a glycolytic capacity that is less developed
than fast-twitch bers. Slow-twitch bers have a wider Z-
band than fast-twitch bers, with type IIB bers having the
thinner Z-band (Sjostrom and Squire, 1977). In the intrinsic
speed of contraction, the shortening velocities of fast-twitch
bers are approximately three times faster than those of
slow-twitch bers (Schiafno and Reggiani, 1996). Types IIX
and IIA bers display shortening velocities that are similar to
each other, but are slower than type IIB bers (Schiafno and
Reggiani, 1996). Type I bers contain relatively large and
numerous mitochondria, myoglobin, and iron-containing
cytochrome of the electron transfer chain. High concentra-
tions of mitochondrial enzymes and myoglobin also support
an enhanced aerobic metabolic capacity (Nemeth and Lowry,
1984). Moreover, type I bers contain a higher amount of
lipid, some of which presumably serves as a source of aerobic
metabolic fuel; they also contain lower amounts of glycogen
and glucose than type IIB bers (Peter et al., 1972; Hintz et al.,
1984). Thus, type IIB bers predominantly use glucose as fuel.
Also, type IIB bers have a more extensively developed SR and
T-tubule system, both of which are consistent with their more
rapid contraction speed; however, they are relatively easily
fatigued. Therefore, type II bers, especially type IIB, have the
ability to rapidly transfer energy for quick, forceful muscle
actions. For example, the ATP splitting rate is three to four
times faster in type IIB bers than in type I bers, and types
IIA and IIX bers are intermediate (Bottinelli et al., 1994,
Stienen et al., 1996). In addition, the tension cost, which is the
ratio between ATPase and tension, is several times lower in
type I bers than in types IIA, IIX, and IIB bers (Bottinelli
et al., 1994; Stienen et al., 1996). These results imply that
when movements require the generation of mechanical
power, type I bers are energetically more economical than
IIA, IIX, and IIB bers (Bottinelli et al., 1994, Stienen et al.,
1996).
Fig. 2. Myosin ATPase histochemistry after preincubation at pH 4.7 (A) and
pH 10.4 (B) in porcine longissimus dorsi muscle. Representative staining of
muscle ber cross-sections. Magnication of 100 was used. Abbreviations:
I, ber type I (slow-twitch, oxidative); IIA, ber type IIA (fast-twitch, oxido-
glycolytic); IIB, ber type IIB (fast-twitch, glycolytic). Cited from Choi et al.,
2005.
2.4. Factors inuencing histochemical characteristics
Histochemical characteristics are primarily the result of
genetic and environmental factors. Many studies have found
there are sex differences relative to muscle ber character-
istics (Klont et al., 1998; Ozawa et al., 2000). Differences in
ber number and size are primarily under the control of sex
hormones, and differences in ber number between males
and females can arise by hormonal action if differences in
androgen hormones are sufciently high during periods of
prenatal ber formation (Rehfeldt et al., 2004). In addition,
testosterone treatment in later postnatal periods can stimu-
late muscle hypertrophy in a direct or indirect manner
(Yoshioka et al., 2007) by satellite cell proliferation and
muscle protein synthesis, without increasing ber number.
Fiber cross-sectional area (CSA) tends to be larger in intact
males than in females and male castrates (Simoneau et al.,
1985; Miller et al., 1993); although for pigs, partially similar or
larger bers have been reported for females than entire males.
According to Staron et al. (2000), all ber types within the
vastus lateralis muscle are shown to be larger in young men
than in young women. Several examinations have reported a
higher percentage of type I ber in women (Simoneau et al.,
1985; Miller et al., 1993), yet others showa higher percentage
of type I ber in men (Komi and Karlsson, 1978; Essen-
Gustavsson and Borges, 1986), and yet additional reports
suggest there is no difference between the genders (Miller
et al., 1975; Saltin et al., 1977). These conicting ndings may
be related to differences in sample size, age, methodology,
and/or physical activity levels (Staron et al., 2000).
There are marked differences in histochemical character-
istics both between and within muscles. According to Choi
et al. (2006), the porcine longissimus dorsi muscle has a large
percentage of type IIB bers (8090%) and a small percentage
of type I bers (515%), while the vastus intermedius muscle
has a large percentage of type I bers (7080%) (Kiessling
and Hansson, 1983). In contrast, bovine biceps brachii and
brachialis muscles have high percentages of slow-twitch red
bers (approximately 48.7 and 51.4%, respectively), with
lower percentages in the longissimus dorsi and biceps femoris
muscles (approximately 22.3 and 10.5%, respectively) (Kirch-
ofer et al., 2002). In pigs, many muscles have a unique dis-
tribution of bers, where type I bers are grouped in clusters
and type IIA bers are in their close vicinity, and these are
then surrounded by type IIB bers (Henckel et al., 1997).
Within muscle, the deeper muscle area has a greater propor-
tion of type I ber and a higher oxidative capacity than the
more outward area (Rosser et al., 1992; Philippi and Sillau,
1994).
Differences in muscle ber characteristics have been found
between breeds. For example, the metabolic proles of gluteus
and longissimus dorsi muscles of different pig breeds (Hamp-
shire, Yorkshire, and Swedish Landrace) can differ, although
they have similar ber type compositions (Essen-Gustavsson
and Fjelkner-Modig, 1985; Rosser et al., 1992). Furthermore,
Ryu et al. (2008) reported that ber type composition
differences can also occur between pig breeds. They found
that the longissimus dorsi muscle of Berkshire pigs has a larger
percentage of type I ber compared to Landrace and Yorkshire
pigs. Therefore, Berkshire pigs show higher muscle pH and
lower drip loss and lightness than other breeds. Young and
Bass (1984) indicated that the longissimus dorsi muscles of
bulls were similar to those of steers in that they had a higher
proportion of type IIB ber than other breeds examined.
Moreover, double-muscled cattle have twice the ber number
and a larger ber area, and their muscles contain a higher
proportion of type IIB ber than other breeds with normal
muscle mass (Deveaux et al., 2001). Several studies have
reported differences in ber characteristics according to
genetic lines between wild and selected pigs (Oksbjerg et al.,
2000; Serra et al., 1998), or between selected lines of different
origin (Brocks et al., 2000; Gil et al., 2003). In general, many of
the muscles of domestic pigs contain more type IIB bers and
less type I bers than those of wild pigs (Ruusunen and
Puolanne, 2004; Zochowska et al., 2005) and wild cattle
(Picard et al., 1995; Brandstetter et al., 1998).
Muscle bers are dynamic structures capable of altering
their phenotype under various conditions such as aging,
altered hormone proles, and exercise (Pette and Staron,
2000). Muscle ber hyperplasia (an increase in ber number)
is completed at birth, thus postnatal growth consists of
hypertrophy (an increase in ber size) (Dwyer et al., 1993;
Bee, 2004). Developing muscle bers can be classied into
primary and secondary generation bers (Bee, 2004). The
fetal stage of mammals is characterized by the differentiation
of bers strongly expressing the slow MHC isoform, derived
from primary bers, and of bers strongly expressing the
neonatal MHC isoform, derived from both primary and
secondary bers (Condon et al., 1990; Lyons et al., 1990). In
general, muscle at birth is composed of oxidative bers
(Moody et al., 1978). Then, as shown in skeletal muscle, fetal
MHC isoforms disappear between 180 days of fetal life and
21 days of postnatal life in bovine, between 140 days of fetal
life and 28 days of postnatal life in sheep, and between 0 and
30 days of postnatal life in pigs (Picard et al., 2002). Moreover,
a few days after birth, mRNAs of the fast MHC isoform can be
detected. Therefore, during growth, the proportion of oxida-
tive bers decreases, while the proportion of glycolytic bers
increases (Solomon et al., 1990; Karlsson et al., 1999). In
general, the CSA of all bers increases during growth, and
type IIB ber has a larger CSA than type I ber, including in
human muscle. However, there are some exceptions. For
example, according to Staron et al. (2000), the CSA of type IIA
bers tends to be largest in the vastus lateralis muscle of men,
whereas for women, the type I bers have the largest CSA.
Moreover, the growth rate of type IIB is two times greater as
compared to that of type I (Oksbjerg et al., 1994).
Some hormones have a profound inuence on muscle
ber type characteristics (Florini et al., 1996; Karlsson et al.,
1999). Thyroid hormones play an important role during
muscle development and maturation. In general, hypothyr-
odism causes fast-to-slow ber transitions (Ianuzzo et al.,
1977), while hyperthyroidismelicits transitions in the reverse
direction (Pette and Staron, 1997, 2000). Moreover, low
thyroid hormones levels inhibit or delay the appearance of
adult fast-twitch muscle bers, whereas high levels accelerate
the transition from developmental bers to adult fast-twitch
bers, including the MHC isoforms (Butler-Browne and
Whalen, 1984; Adams et al., 1999). According to Oksbjerg
et al. (1995), -agonists increase ber area, and cause ber
types IIA to IIB conversions. Porcine growth hormones are
also shown to increase ber area in porcine longissimus dorsi
muscle (Karlsson et al., 1999). In the case of endocrine factors,
Ryu et al. (2007) reported that serum insulin-like growth
factor-I (IGF-I) concentrations were negatively related to the
percentage of type I ber, whereas serum epidermal growth
factor was positively correlated to the percentage of type I
ber. Furthermore, breeding for high lean meat increases the
proportion of type IIB ber, and has a positive correlationwith
IGF-I expression (Owens et al., 1994).
Physical exercise is an important factor that inuences
adaptation in both the ber characteristics and metabolic
proles of skeletal muscles (Pette and Staron, 2001). A
signicant increase in the percentage of type I ber has
been shown after various forms of aerobic conditioning, such
as endurance cycle training (Allemeier et al., 1994). However,
according to Essen-Gustavsson et al. (1988), pigs that trained
on a treadmill for 1015 min for several weeks had no change
in ber type composition, but oxidative capacity increased
and glycolytic capacity decreased in the muscles involved in
exercise.
3. Diversity of myosin and other myobrillar
protein isoforms
3.1. Myosin isoforms
Myosin (approximately 520 kDa) is the best-known
molecular motor protein. Molecular motor proteins are able
to convert chemical energy into mechanical energy through
structural change. The myosin superfamily is grouped into 15
classes, and the conventional myosins, such as the myosin of
striated muscle, are designated as class II (Bottinelli and
Reggiani, 2000; Clark et al., 2002). The myosin molecule of
class II is characterized into two functional regions: its two
globular heads (subfragment 1) and an -helical coiled-coil
rod (Fig. 3). The globular head (approximately 900 amino
acids) contains the catalytic site for ATP hydrolysis and the
binding site for actin (Rayment et al., 1993) (Fig. 4). The rod
domain is about 150 nm long and 2 nm in diameter, and is
composed of nearly 1000 amino acids, which are the back-
bone of the thick lament (Levitsky, 2004). Myosins in
skeletal muscle are hexamers that are composed of two MHCs
and four myosin light chains (MLCs). Each of the MHCs
associates with two MLC isoforms, one belonging to the alkali
LC (also called the essential light chain, ELC), and one
belonging to the regulatory LC (RLC). These can function to
make ne adjustments to myosin motor activity, as well as
add to the versatility of its kinetics (Reggiani et al., 2000).
In mammals, at least eight distinct class II MHC isoforms [1
or /slow, 2A, 2X, 2B, embryonic (emb), neonatal (neo), ,
and extraocular (exoc) isoforms] are expressed in skeletal
muscle cells, which are encoded by eight separate genes
(Schiafno and Reggiani, 1996; Weiss and Leinwand, 1996).
The rst four isoforms (1, 2A, 2X, and 2B) are the predominant
MHC isoforms in adult skeletal muscle (Talmadge, 2000). The
MHC 1 isoform is expressed in slow-twitch bers of skeletal
muscle and in ventricular myocardium, and three fast iso-
forms (2A, 2X, and 2B) are expressed in fast-twitch bers.
Other isoforms appear to be expressed in muscle in a species-
specic manner. In skeletal muscle, for example, the MHC emb
and neo isoforms are expressed during embryonic and
perinatal development, respectively. The MHC isoform is
expressed in cardiac muscle, masticatory muscle, and in some
red muscle bers. The MHC exoc isoform is a fast isoform
expressed only in extraocular muscle (Bottinelli and Reggiani,
2000; Pette and Staron, 2000). However, the MHC 2B isoform
is not expressed in human, cat, or bovine muscles, but it is
expressed in the muscles of small mammals such as mice, rats,
and rabbits, as well as in pigs (Smerdu et al., 1994; Ennion et
al., 1995; Pette and Staron, 2000; Kohn et al., 2007).
Fig. 3. The myosin molecule in skeletal muscle. Each myosin is formed by two
globular heads and a rod. Myosin is digested with trypsin, and two major
fragments are formed. The largest fragment is heavy meromyosin(HMM) and
the other fragment is light meromyosin (LMM). HMMcan be further digested
toformthe subfragment 1 (S1) and subfragment 2 (S2), as citedfromLevitsky
(2004).
Fig. 4. The three dimensional structure of myosin subfragment 1 in skeletal
muscle. The color scheme is as presented by Rayment et al. (1993).
Abbreviations: HCM, hypertrophic cardiomyopathy; ELC, essential light
chain; RLC, regulatory light chain.
In adult mammals, skeletal muscle contains three ELC
isoforms, including one slow (1s) and two fast (1f, 3f) ELC
isoforms, as well as two RLC isoforms consisting of one slow
(2s) and one fast (2f) isoform (Bottinelli, 2001). The ELC 1f
and emb isoforms are the major transcripts within both
developing fast and slow fetal muscles, whereas MLC 1s
transcripts are rst detected relatively later during the fetal
period, and are also expressed in slowmuscles (Bottinelli and
Reggiani, 2000).
The electrophoretic separation of myosin isoforms repre-
sents the most direct approach to attribute a single muscle
ber to a given type, or to determine the composition of a
given muscle. In general, the MHC isoforms can be separated
in order of decreasing migration rate, fromthe MHC slow(the
fastest migration rate) to MHC fast (the slowest migration
rate) isoforms. The separation of the four MHC isoforms (1,
2A, 2X, and 2B) is more difcult; however, it can be obtained
by gradient gel electrophoresis in rats (Bar and Pette, 1988)
and rabbits (Reiser and Kline, 1998). In contrast, in cattle
(Picard et al., 1999), horses (Rivero et al., 1997), and humans
(Bammman et al., 1999), only three isoforms (MHC 1, 2A, and
2X) show detectable protein bands. However, precise identi-
cation of the MHC isoforms can be achieved by determining
their nucleotide sequences. According to Chikuni et al.
(2004), the MHC 2B isoform is not expressed in bovine and
equine skeletal muscles. These results are conrmed by the
fact that bovine and equine muscles are adapted to slow-
oxidative conditions. However, this does not mean that type
IIB bers are not present in bovine or equine muscles, since
muscle bers are generally classied into types I, IIA, and
IIB bers by histochemistry, which is based on the ATPase
characteristics of the bers (Brooke and Kaiser, 1970). On
the other hand, in pigs, only three protein bands (1, 2A, and
2X+2B) are detectable using gel electrophoresis (Bee et al.,
1999), although the muscles present four adult MHC mRNA
(1, 2A, 2X, and 2B) (Kim et al., 2008).
MHC isoform diversity can generate large variations in
shortening velocity, peak power, optimum efciency at
shortening, and the rate of ATP splitting in isometric con-
ditions (Bottinelli, 2001). The shortening velocity is found
to differ not only between slow-twitch bers containing
the slow MHC isoform and fast-twitch bers containing the
fast MHC isoforms, but also among the fast-twitch ber types
(IIA, IIX, and IIB) containing each fast MHC isoform (2A, 2X,
and 2B, respectively). Moreover, the type IIB bers containing
the MHC 2B isoform have the highest shortening velocity
value (Schiafno and Reggiani, 1996). However, not only the
MHC isoforms, but also the ELC isoforms can inuence modu-
lating motor properties. In particular, the speed of actin
movement increases in relation to the amount of the ELC 3f
isoform (Warshaw, 1996; Reggiani et al., 2000). ATP con-
sumption is substantially higher in muscle bers containing
the fast MHC isoforms than in muscle bers containing the
slow MHC isoforms, and the amount of ATP needed to
maintain a given amount of tension cost is much higher in
fast-twitch than in slow-twitch bers (Schiafno and
Reggiani, 1996; Bottinelli and Reggiani 2000). On the other
hand, no correlations have been found between the ATP
hydrolysis rate and content of the two fast ELC isoforms, ELC
1f and 3f, in a group of bers containing only the MHC 2B
isoform (Reggiani et al., 2000).
The expression of the MHC and MLC genes, during boththe
developmental and adult stages, is controlled by several
factors, including motor neuron discharge patterns, loading
conditions, and certain hormones (Hamalainen and Pette,
1997; Reggiani et al., 2000). In general, each ber expresses
only one MHC gene associated with two MLC genes, and the
MHC isoforms combine with several MLC isoforms to generate
the myosin molecule isoforms (isomyosins) (Talmadge, 2000;
Stephenson, 2001). For example, matched sets of the MHC and
MLC isoforms would be comprised of the fast MHC isoforms
(2A, 2X, and 2B) and the fast MLC isoforms (1f, 2f, and 3f), or
the slow MHC isoform (1) and the slow MLC isoforms (1s
and 2s) (Bortolotto et al., 2000). Whereas mismatched sets
would be comprised of the fast MHC isoforms, and the slow
MLC isoform(1s) and fast MLC isoforms (1f, 2f, and 3f), within
a single muscle ber (Bortolotto et al., 2000). According to
Choi et al. (2007), in an entire muscle study, relationships
between the MHC and MLC isoforms were found to be
somewhat limited in porcine longissimus dorsi muscle. They
reported these differences can be attributed, to some degree,
to the existence of mismatched MHC-MLC hybrids within
single muscle bers (Stephenson, 2001). However, the MHC
fast/slow ratio was positively correlated with the ELC fast/
slowratio inentire muscle, including all ber types (Choi et al.,
2007).
3.2. Other protein isoforms
Myobrillar protein isoforms are differentially expressed
in various muscle types and ber types, and can be co-
expressed within the same ber. Single bers with similar
MHC isoform contents may have variable functional proper-
ties. These variations can be explained by other myobrillar
protein isoforms, especially troponin and tropomyosin iso-
forms (Bottinelli, 2001). Troponin and tropomyosin are the
major proteins of the thin lament in myobrils, and are
calcium activated complexes. Moreover, they are critical for
muscle ultra-structure and are essential components of the
regulatory machinery of muscle contraction (Schiafno and
Reggiani, 1996; Clark et al., 2002).
Troponin (80 kDa) is a cooperative complex of three
subunits (the calcium binding subunit, TnC; the inhibitory
subunit, TnI; and the tropomyosin-binding subunit, TnT,
which functions with tropomyosin in modulating the inter-
action of myosin and actin during force generation in skeletal
muscle bers (Clark et al., 2002). The troponin subunits are
expressed as a number of isoforms whose expression patterns
differ among ber types, and they contribute to the distinct
contractile properties of skeletal muscles (Westfall and
Metzger, 2001). Two TnC isoforms are expressed in skeletal
muscle: the TnC fast and TnC cardiac/slow isoforms (Botti-
nelli and Reggiani, 2000). The TnC fast isoform exhibits two
high afnity and two low afnity sites for calcium binding,
whereas the TnC cardiac/slow isoform exhibits two high
afnity sites and one low afnity site. Thus, the regulatory
function of TnC is based on binding calcium at its low afnity
sites (Collins, 1991).
TnI can bind actin and inhibit actomyosin ATPase activity.
This inhibition is enhanced in the presence of tropomyosin,
and becomes reversible and calcium sensitive in the presence
of the intact troponin complex. Skeletal muscles contain two
TnI isoforms: the TnI fast and slow isoforms (Schiafno and
Reggiani, 1996). TnT binds to TnC and TnI, and also to
tropomyosin in two different regions. One of its two binding
sites for tropomyosin is close to the binding sites for TnC and
TnI, and is calcium sensitive, whereas the other site is calcium
insensitive (Bottinelli and Reggiani, 2000).
The isoform pattern of TnT is very complex; there are at
least six isoforms in adult skeletal muscle, consisting of fast
(1f, 2f, 3f, and 4f) and slow (1s and 2s) isoforms (Schiafno
and Reggiani, 1996). Generally, the fast and slow isoforms are
conned to fast- and slow-twitch bers, but the TnT fast
isoforms are distributed in a less discrete manner. Moreover,
there is no one-to-one correlation between the TnT isoforms
and MHC isoforms, and the TnT isoforms are also distributed
in a less discrete manner. However, in rat muscle, there can be
a correlation between the MHC and TnT isoform canonical
program: coexpression of TnT slow (1s and 2s) and MHC 1,
TnT 2f and MHC 2B, TnT 3f and MHC 2A, and TnT 4f and the
MHC 2X isoform in single bers (Galler et al., 1997).
Tropomyosin (65 kDa) is an elongated protein polymer,
and is constructed of two -helical chains arranged as a
coiled-coil rod, which is wrapped around the actin lament
and partially obscures the binding site. In such a position,
myosin S1 fragments bind only weakly, and cannot create a
power stroke. The tropomyosin laments, which are formed
by head to tail assembly of approximately 35 tropomyosin
dimmers, contribute to thin lament stiffness (Kojima et al.,
1994) and regulate myosinactin interactions (Geeves and
Lehrer, 1994). Three tropomyosin isoforms are expressed in
skeletal muscle: the -slow, -fast, and isoforms, which can
assemble as - and -homodimers or -heterodimers.
In general, there is a higher proportion of the tropomyosin
isoform in fast-twitch bers (Cummins and Perry, 1974);
the isoform is not a major isoform expressed in most
skeletal muscles (Oe et al., 2007).
Slow- and fast-twitch bers differ markedly in their twitch
properties, and these variations depend on the sensitivity of
the myobrillar apparatus to calcium(Bottinelli and Reggiani,
2000). This calcium sensitivity is mainly determined by the
regulatory proteins troponin and tropomyosin (Danieli-Betto
et al., 1990). Although the regulatory calciumbinding sites are
located only on the TnC isoforms, combinations of the TnTand
tropomyosin isoforms contribute in a major way to calcium
sensitivity (Schiafno and Reggiani, 1996). For example, in
fast-twitch muscle bers, a higher proportion of the TnT-2f
and tropomyosin -fast isoforms is related to higher values of
calcium sensitivity than in slow-twitch bers (Schachat et al.,
1987).
3.3. Relationships between myobrillar protein isoforms and
muscle ber types
MHC isoform content is strongly correlated with muscle
ber type composition in humans (Fry et al., 1994), rats
(Talmadge et al., 1995), and horses (Rivero et al., 1997). For
example, the correlation coefcients reported for the
immuno-histochemical identication of muscle ber types
versus the electrophoretical identication of MHC isoforms
range from 0.66 to 0.88 in humans (Staron et al., 2000;
Serrano et al., 2001). In addition, according to Choi et al.
(2006), the correlation coefcients reported for myosin
ATPase-based ber types versus the electrophoretical identi-
cation of MHC isoforms ranged from 0.46 to 0.77 in porcine
longissimus dorsi muscle. More specically, they reported that
MHC 1 isoform content was strongly correlated with the
number (r=0.77) and area (r=0.74) percentage of type I ber.
However, there are some discrepancies between MHC
isoform composition and that of muscle ber type. These
differences can be explained by the existence of (1) pure and
hybrid ber types and (2) the existence of other protein
isoforms (Bottinelli, 2001; Stephenson, 2001). Pure bers
(types I, IIA, IIX, and IIB) are characterized by the expression
of a single MHC isoform (1, 2A, 2X, and 2B, respectively). On
the other hand, hybrid bers (types I/IIA, IIA/I, IIAX, IIXA,
IIXB, and IIBX) contain more than two MHC isoforms (Pette
and Staron, 2000). For example, types I/IIA bers contain the
MHC 1 and 2A isoforms, with type I in excess, whereas types
IIA/I bers also contain the MHC 1 and 2A isoforms, with type
IIA in excess (Pette and Staron, 2000; Bottinelli, 2001). In
small mammals, the content of hybrid bers in hindlimb
muscles is low; for example, 56% in tibialis anterior muscle
(Lucas et al., 2000). On the other hand, in livestock animals,
the proportion of hybrid bers is much higher, such as 21% in
goat muscle (Arguello et al., 2001) and more than 40% in
llama muscle (Graziotti et al., 2001). Hence, hybrid bers are
not a rare phenomenon, and are detected not only in normal,
but also transforming skeletal muscle such as developing and
growing muscle (Stephenson, 2001). For example, the
percentage of hybrid bers increases in young animals
(Bottinelli, 2001). However, within hybrid bers, there is a
relationship between shortening velocity and the MHC
isoform composition of the individual bers, but the specic
contributions of the individual isoforms to the contractile
properties have not been determined. On this basis, the MHC
isoforms are used most often as molecular markers to identify
ber types (Bottinelli and Reggiani, 2000).
The MLC slow isoforms are generally expressed in slow-
twitch bers, whereas the MLC fast isoforms are expressed in
fast-twitch bers (Schiafno and Reggiani, 1996). A role for
the ELC isoforms was suggested by the nding that maximum
shortening velocity is higher in bers that contain a greater
amount of the ELC 3f isoforms (Schiafno and Reggiani, 1996).
According to Sweeny et al. (1988), the ELC 1f isoform is sig-
nicantly more abundant in type IIA ber, whereas the ELC 3f
isoform is more abundant in type IIB ber than in types IIX or
IIA, with the lowest con>centration being found in type IIA.
Similar results were reported by Mabuchi et al. (1982) who
found that the ELC 1f/3f ratio in type IIA ber is higher than in
type IIB ber, and that the ELC 3f/1f ratio in type IIB ber is
higher than in type IIA. However, these results are based on
examining the relationship between MLC isoformcomposition
and pure ber type insingle bers. Whereas inanentire muscle
study of porcine longissimus dorsi muscle including all muscle
ber types, althoughthe content of the ELC1s isoformshoweda
positive correlation with type I ber composition (r=0.36),
correlations between the other MLC isoform compositions
and ber type composition were limited (Choi et al., 2005).
Table 1 presents the myobrillar protein isoforms occur-
ring in adult fast- and slow-twitch muscle bers. It appears
that slow-twitch bers are characterized by the presence of
the MHC 1, ELC 1s, TnC slow/cardiac, TnI slow, and TnT slow
isoforms. These bers would be expected to combine the
slowest shortening velocity with an extremely slow response
to calcium. Type IIA bers contain MHC 2A, a higher ELC 1f/3f
ratio, TnT 3f, and tropomyosin -dimers (Schachat et al.,
1985; Schiafno and Reggiani, 1996). These bers would
contract more slowly than the other fast-twitch bers and
would show graded calcium responsiveness. On the other
hand, type IIB bers are characterized by the presence of MHC
2B, a higher ELC 3f/1f ratio, TnC-fast, TnI-fast, TnT-2f, and
tropomyosin -dimmers in pure single muscle bers. These
bers would be expected to combine the fastest shortening
velocity with the most rapid response to calcium. However,
there is no one-to-one correlation between the TnT isoforms
and MHC isoforms. Moreover, other myobrillar proteins,
including C-protein (Yamamoto and Moos, 1983), titin
(Horowits, 1992), nebulin (Labeit and Kolmerer, 1995), and
-actinin (Schachat et al., 1985), also exist in multiple
isoforms and are distributed unevenly between slow- and
fast-twitch muscles. However, the clear roles of other protein
isoforms and their functions within muscle ber types have
yet to emerge.
4. Muscle ber type, myobrillar protein isoforms, and
meat quality
4.1. Muscle ber type, MHC isoforms, and meat quality
The size and number of muscle bers are factors that
inuence muscle mass and meat quality (Rehfeldt and Kuhn,
2006). During postnatal development, when the number of
muscle bers is high, bers generally grow more slowly;
conversely, bers grow more rapidly when the number of
bers is lowin poultry (Dranseld and Sosnicki, 1999) and pig
(Fiedler et al., 1997). Thus, ber number is negatively
correlated with ber area, whereas both ber number and
area are positively correlated with muscle mass in pigs.
Moreover, in cattle (Picard et al., 2006), there is muscle
hypertrophy with high growth potential due to a higher total
number of bers. According to Lengerken et al. (1997), pigs
with a higher total number of bers tended to exhibit smaller
ber sizes, and exhibited higher muscle pH
45 min
and lower
drip loss than pigs with a lower total ber number and
large ber size. Moreover, the total amount of type I ber is
negatively correlated with drip loss and lightness (Ryu and
Kim, 2006). In contrast, higher amounts of type IIB ber were
associated with increasing drip loss, and were also associated
with differing measurements for water-holding capacity. In
addition, ber size is an important factor in determining meat
tenderness (Seideman and Crouse, 1986). For example, in
cattle (Renand et al., 2001) and pig (Karlsson et al., 1993;
Maltin et al., 1997), muscles with a larger ber size, especially
type IIB ber, exhibit tougher meat than muscles of smaller
ber size. Moreover, for texture parameters, muscles with
greater hardness are related to a larger ber area (Zochowska
et al., 2005). These results suggest that muscles with higher
numbers of low or medium size bers tend to exhibit good
meat quality, without signicant differences in muscle mass.
Conversely, selecting for leaner livestock animals can result in
large muscle bers, especially type IIB ber, which seems to
be associated with poorer meat quality (Gentry et al., 2002;
Ryu and Kim, 2006).
Intramuscular fat (IMF) content is an important factor that
inuences eating quality, including tenderness, juiciness, and
avor, and is inuenced by genetic and environmental factors,
such as genotype, gender, feeding system, age etc. However,
IMF content is positively correlated to tenderness (Renand
et al., 2001) and negatively correlated with ber area
(Karlsson et al., 1999). A study using histochemical staining
with Sudan black B and Oil Red O showed that all type I bers
contained neutral lipids, whereas types IIA and IIB bers only
contained 26% and 1%, respectively (Karlsson et al., 1999).
Thus, the percentage of type I ber is positivelycorrelatedwith
IMF content in cattle (Calkins et al., 1981), and a high type I
ber content contributes more to juiciness and avor, whereas
a high content of type IIB ber tends to be associated with
tougher meat. However, although most of these results were
obtained within limited multi-factorial designs, such as
relative to genetic and environmental factors, there is a con-
sensus indicating a correlation between type I ber content
and meat tenderness (Renand et al., 2001).
In living animals, energy production has two main alter-
native routes: the aerobic and anaerobic pathways (Poso and
Puolanne, 2005). However, after exsanguination, when
circulation is stopped, muscles lack the oxygen required for
oxidative metabolism. Therefore, glycolysis is a very impor-
tant pathway in the postmortem period. Rapid postmortem
glycolysis induces an accumulation of lactate, and this lactate
accumulation results in a rapid decline in muscle pH while
muscle temperature is still high (Briskey, 1964). This
combination of low muscle pH and high temperature results
in higher protein denaturation, and generally poorer meat
quality (Joo et al., 1999). Fast-twitch bers mainly carry out
the glycolytic pathway, and their metabolism contributes to a
fast metabolic rate at the early postmortem period. Thus, the
percentage of type IIB ber is negatively related to muscle pH,
and positively related to R-value (adenine/inosine ratio),
allowing for the determination of ATP depletion in the early
postmortem period (Ryu and Kim, 2006). Likewise, muscles
Table 1
Myosin, troponin, and tropomyosin isoforms and their expression patterns in
adult skeletal muscle bers.
Muscle ber types
Type I Type IIA Type IIX Type IIB
Myosin
MHC isoforms MHC 1 MHC 2A MHC 2X MHC 2B
MLC isoforms
ELC ELC 1s ELC 1f, 3f
(higher 1f/
3f ratio)
ELC 1f, 3f ELC 1f, 3f
(higher 3f/
1f ratio)
RLC RLC 2s RLC 2f RLC2f RLC 2f
Troponin
TnC isoforms TnC slow/
cardiac
TnC fast TnC fast TnC fast
TnI isoforms TnI slow TnI fast TnI fast TnI fast
TnT isoforms TnT 1s TnT 3f TnT 4f TnT 2f
TnT 2s (TnT 1f) (TnT 1f) (TnT 1f)
Tropomyosin
TM isoforms TM -slow TM -fast TM -fast TM -fast
TM TM TM
Abbreviations: MHC, myosin heavy chain; MLC, myosin light chain; ELC,
essential light chain; RLC, regulatory light chain; TnC, troponin C; TnI,
troponin I; TnT, troponin T; TM, tropomyosin.
Cited and modied from Schiafno and Reggiani, 1996.
harboring a high glycogen and lactate content at 45 min
postmortem are composed of signicantly higher type IIB
ber and lower type I ber, and also showed rapid
postmortem glycolysis, paler color, higher drip loss than
muscles harboring a high glycogen and low lactate content in
the early postmortemperiod (Choe et al., 2008). In the case of
myosin isoforms, MHC fast isoform content is positively
correlated with lactate content and glycolytic potential, and
negatively correlated with glycogen content and muscle pH.
On the other hand, MHC slow isoform content is positively
correlated with glycogen content and muscle pH, and nega-
tively correlated with lactate content at the early postmortem
period (Choi et al., 2007).
Histochemically, fast-twitch ber has a more extensively
developed sarcoplasmic reticulum, transverse-tubule system,
and thinner Z-band than slow-twitch ber, and proteins that
comprise to the Z-band in fast-twitch ber are more
susceptible to early postmortem proteolytic degradation
than in slow-twitch ber (Xiong, 2004). Thus, the differences
in inherent susceptibility of the various ber types to protein
denaturation may account for the different meat quality
attributes between type red and white muscles (Bowker et al.,
2005). Myosin isoforms also differ in their susceptibility to
protein denaturation, and myosin isoformcontent might have
some bearing on the extent of protein denaturation (Bowker
et al., 2005). Choi et al. (2006) reported that muscles with a
lower MHC slowisoform content exhibited more pronounced
protein denaturation at 24 h postmortem than muscles
possessing a higher MHC slow isoform content. However,
myosin denaturation increases the shrinkage of myobrils
considerably and also causes scattering of light and increasing
drip loss (Bowker et al., 2005), and specic myosin fragment
were observed at 48 h postmortem using 2-dimentional
electrophoresis based proteome analysis, and these fragment
was related to tenderness (Lametsch et al., 2003).
According to the report of Warner et al. (1993), undesir-
able conditions such as pale, soft, and exudative (PSE) pork
are more likely to develop in fast-twitch muscle than in slow-
twitch muscle. Moreover, Ryu and Kim (2005) reported that
the accelerated metabolic rate and poor quality of meat in PSE
are explained by an increase in the percentage of type IIB
ber. For example, drip loss is inversely related to the
percentage of types I and IIA bers, and positively related to
the percentage of type IIB ber. Another important meat
quality parameter is lightness, which is negatively correlated
with type I ber, and the level of heme pigment is positively
correlated with type I ber (Henckel et al., 1997). Moreover,
Whipple et al. (1992) found negative correlations between
the percentage of type IIB ber and both myoglobin content
and visually determined color. In general, since meat is sold
by appearance, this is a very important quality attribute, with
redder color generally preferred. These results suggest that an
increasing percentage of type IIB ber, and decreasing
percentages of types I and IIA bers, are related to increases
in drip loss and lightness, which are deteriorative to pork
quality.
On the other hand, muscles with a higher MHC 1 isoform
content show a higher ultimate muscle pH and a higher level
of oxidative enzyme activity, but a lower glycolytic enzyme
activity level and drip loss and a darker surface than muscles
with a lower MHC 1 isoform content (Gil et al., 2003). Thus,
the MHC slowisoformis a useful indicator for determining the
oxidative capacity of muscle in pigs (Gil et al., 2003), cattle
(Olivan et al., 2004), rabbits (Ramirez et al., 2004), and sheep
(Sazili et al., 2005). MHC isoform content is reected by
differences in the amount and activity of intrinsic muscle
protease. To give a simple example, MHC slowisoformcontent
was positively correlated with calpastatin activity in ovine
longissimus dorsi muscle. In general, calpastatin is closely
related to tenderness in the longissimus dorsi muscles of cattle
(Whipple et al., 1990), lambs (Koohmaraie and Shackelfore,
1991), and pigs (Sensky et al., 1998). These results indicate
that MHC isoform content can inuence meat tenderness in
pigs (Chang et al., 2003) and lambs (Sazili et al., 2005).
Overall, these results also suggest that MHC isoform content
inuences glycolytic rate and protein denaturation, and thus,
also affects the ultimate meat quality.
4.2. Other protein isoforms and meat quality
Muscle diversity is based on the heterogeneity of the
contractile and energetic properties of single muscle bers
that make up muscle, and this in turn is based on the presence
of myobrillar protein isoforms (Bottinelli, 2001). The MLC
isoforms also inuence metabolite content and the glycolytic
rate during the early postmortem period (Choi et al., 2007).
And during this time, muscles with a lower ELC 1s content
showa faster glycolytic rate than muscles with a higher ELC 1s
content. In addition, ELC 1s isoform content is signicantly
correlated with metabolite content; however, the ELC fast/
slow ratio shows an opposite tendency. For example, ELC 1s
isoformcontent is positively correlated with levels of ATP and
G6P, and negatively correlated with lactate and glycolytic
potential. Whereas, the ELC fast/slow ratio is positively cor-
related with lactate and glycolytic potential, and negatively
correlated with pH
45 min
. These results seem to indicate
that MLC isoform content can also inuence the metabolic
properties of muscle. However, MLC isoform content was
found to have only a limited effect on meat quality (Choi et al.,
2007).
In the case of troponin, TnT is a myobrillar protein that is
known to be easily degraded into a 30 kDa peptide during
postmortemmuscle aging (Muroya et al., 2006). Muroya et al.
(2007) reported that TnT fragments can be a useful marker for
examining variations in postmortem beef ageing. TnT degra-
dation shows strong positive correlations with shear force
and tenderness. According to Muroya et al. (2006), protease
susceptibility does not differ among the TnT isoforms;
however, the fast TnT isoforms are degraded differently into
specic fragments, where the TnT-2f and -3f isoforms con-
tribute to 28.3 kDa fragments, and the TnT-1f and -4f isoforms
contributed to 26.0 kDa fragments. Oe et al. (2007) reported
that tropomyosin isoform composition can inuence post-
mortem rigor development and meat quality. However, the
effects of these protein isoforms on ultimate meat quality are
not yet fully understood.
5. Conclusions
Meat quality traits are very complex, and are inuenced by
many factors. This fact makes the prediction and improve-
ment of meat quality traits difcult (Huff-Lonergan et al.,
2002). The histochemical and biochemical characteristics of
skeletal muscles are primarily the result of genetic and
environmental factors such as gender, muscle type, breed,
age, hormones, exercise, etc. However, if the genetic and
environmental factors are both similar, muscle ber char-
acteristics and myobrillar protein isoforms, especially the
MHC isoforms, are very useful indicators for examining
muscle metabolism variations at the postmortem period as
well as ultimate meat quality. Moreover, the histochemical
and biochemical characteristics of live animals can be used to
predict meat quality and then applied in selection programs
to improve and control meat quality. Some recent studies
found heritabilities and genetic correlations between histo-
chemical characteristics and meat quality traits in pigs
(Fiedler et al., 2004), cattle (Shackelford et al., 1994), and
horses (Rivero and Barrey, 2001), and the coefcients of
heritability for the histochemical characteristics and meat
quality traits varied from 0.10 to 0.80.
Although many studies have reported relationships
between histochemical and biochemical characteristics and
meat quality, opinions among scientists on this point remain
divided. For example, although the majority of studies showa
positive correlation between the percentage of type I ber and
tenderness (Strydom et al., 2000; Renand et al., 2001), some
studies showno correlation (Geesink et al., 1995; Vestergaard
et al., 2000), and other studies indicate that tenderness is
negatively correlated with the percentage of type I ber
(Ozawa et al., 2000). Moreover, according to Dingboom and
Weijs (2004), bovine muscles harboring a higher percentage
of type IIB ber showed more rapid ageing, had a lower
concentration of collagen, and offered more tender and
sweeter meat than muscles with a higher percentage of type
I ber. Furthermore, type I ber may be related to the
production of dark cutting beef with high pH, which is caused
by pre-slaughter stress (Ozawa et al., 2000). And still, the
effects of the myobrillar protein isoforms on postmortem
metabolism and ultimate meat quality are not yet fully
understood.
Therefore, more information is needed on how the muscle
ber characteristics and myobrillar protein isoforms affect
meat quality, in order to practically apply this knowledge to
improve and control meat quality, to better understand the
physiological mechanisms of muscle, and to evaluate the
sometimes controversial conclusions regarding the roles of
these traits in practical livestock breeding.
Acknowledgement
This work was supported by a Korea University grant and
the Agricultural R&D Promotion Center of the Republic of
Korea.
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