Postnatal transitions in myosin heavy chain isoforms of the rabbit superficial masseter and digastric muscle (original) (raw)
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The Anatomical Record Part A: Discoveries in Molecular, Cellular, and Evolutionary Biology, 2006
Postnatal changes in the fiber type composition and fiber crosssectional area were investigated in the superficial (TEM1) and deep (TEM23) temporalis of male rabbits. It was hypothesized that, due to the transition from suckling to chewing during early postnatal development, the proportion of fast fiber types would decrease, while the proportion of fibers positive for myosin heavy chain (MyHC) cardiac a would increase, and that, due to the influence of testosterone during late postnatal development, the proportion of these a fibers would decrease again. Classification of the fibers types was performed by immunohistochemistry according to their MyHC content. The proportion of a fiber types significantly increased in both muscle portions from 2% and 8% for TEM1 and TEM23 at week 1 to 29% and 54% at week 8, respectively,. While in TEM1 the proportion of this fiber type did not change thereafter, it decreased again to 27% in TEM23 at week 20. The change for the fast fiber types was opposite to that of the a fiber types. Significantly more MyHC IIX fibers were found in TEM1 than in TEM23 in adult rabbits. In the first 8 weeks, the cross-sectional areas of all fibers increased. After this period, only MyHC cardiac a þ I fibers continued to increase significantly. It was concluded that there are developmental differences in the myosin heavy chain transitions of the two portions of the temporalis muscle.
Cells Tissues Organs, 1999
The myosin heavy chain (MyHC) isoform composition of six adult (>7 months old) male and female rabbit masseter muscles was studied using seven monoclonal antibodies. In matched serial tissue sections, muscle fibers in 10 different neuromuscular compartments were analyzed. Nearly all fibers were found to express one of five phenotypes. They either contained one of four different slow/beta MyHC phenotypes (I1–I4), nearly all of which co-express cardiac alpha MyHC, or they contained type IIa MyHC. Very few fibers contained slow/beta or cardiac alpha MyHC only or both the alpha/slow/beta and IIa isoforms. Most, but not all, of the compartments studied contained similar proportions of fibers of the five major phenotypes, at least within sex. For 7 of the 10 compartments studied, significant sex differences in the proportion of I1 and IIa fibers were found. Males contained more IIa fibers and fewer I1 fibers than females. Fibers of the IIa phenotype were significantly larger than fiber...
Journal of Muscle Research and Cell Motility, 1988
Changes in myosin synthesis during the postnatal development of the fast extensor digitorum longus (EDL) and the slow soleus muscles of the kitten were examined using immunocytochemical techniques supplemented by pyrophosphate gel electrophoresis and gel electrophoresis-derived enzyme linked immunosorbent assay (GEDELISA) of myosin isoforms. The antibodies used were monoclonals against heavy chains of slow and fast myosins and a polyclonal against foetal/embryonic myosin. In both muscles in the newborn kitten, there was a population of more mature fibres which stained strongly for slow but weakly for foetal/embryonic myosin. These fibres were considered to be primary fibres. They formed 4.8% of EDL fibres and 26.% of soleus fibres at birth, and continued to express slow myosin in adult muscles. The less mature secondary fibres stained strongly for foetal/embryonic myosin, and these could be divided into two subpopulations; fast Secondaries in which foetal/embryonic myosin was replaced by fast myosin, and slow secondaries in which the myosin was replaced by slow myosin. At 50 days the EDL had a large population of fast secondaries (83% of total fibres) and a small population of slow secondaries which gradually transformed into fast fibres with maturity. The vast majority of secondary fibres in the soleus were slow secondaries, in which slow myosin synthesis persisted in adult life. There was a restricted zone of fast secondaries in the soleus, and these gradually transformed into slow fibres in adult life. It is proposed that the emergence of primary fibres and the two populations of secondary fibres is myogenically determined.
Journal of Experimental Biology, 2004
SUMMARY Little is known about the influence of Myosin Heavy Chain (MHC) isoforms on the contractile properties of single muscle fibres in large animals. We have studied MHC isoform composition and contractile properties of single muscle fibres from the pig. Masseter, diaphragm, longissimus, semitendinosus,rectractor bulbi and rectus lateralis were sampled in female pigs (aged 6 months, mass 160 kg). RT-PCR, histochemistry, immunohistochemistry and gel electrophoresis were combined to identify and separate four MHC isoforms:MHC-slow and three fast MHC (2A, 2X, 2B). Maximum shortening velocity (Vo) and isometric tension(Po) were measured in single muscle fibres with known MHC isoform composition. Six groups of fibres (pure: slow, 2A, 2X and 2B, and hybrid: 2A-2X and 2X-2B) with large differences in Vo and Po were identified. Slow fibres had mean Vo=0.17±0.01 length s-1 and Po=25.1±3.3 mN mm-2. For fast fibres 2A,2X and 2B, mean Vo values were 1.86±0.18,2.55±0.19 and 4.06±0.33 length s...
Expression of myosin heavy chain isoforms in the postnatal mouse masseter muscle
Okajimas Folia Anatomica Japonica, 2009
We investigated the properties of the masseter muscle in mice from five to seven weeks of age. Myosin heavy chain (MyHC) isoforms were measured in the masseter muscle. The three types of muscle fibers (Type I, strong reaction; Type IIA, intermediate reaction; and Type IIB, weak reaction) were all present in the masseter muscle in five-weeks-old mice and seven-weeks-old mice, the three types could be clearly distinguished by their enzyme activity. The percentage of Type IIB fibers (above 50%) was the highest among all fiber types both 5-and 7-weeks-old mice. The mRNA levels for myosin slow and myosin IIb increased significantly between 5 and 7 weeks. These observations suggest that muscle fiber size, muscle fiber types and mRNA levels of the MyHC isoforms all contribute to the diminished functional adaptability of enzyme activity in the masseter muscle.
Heterogeneity of fiber characteristics in the rat masseter and digastric muscles
Journal of Anatomy, 2007
The functional requirements in muscle use are related to the fiber type composition of the muscles and the crosssectional area of the individual fibers. We investigated the heterogeneity in the fiber type composition and fiber cross-sectional area in two muscles with an opposing function, namely the digastric and masseter muscles ( n = 5 for each muscle) of adult male rats, by means of immunohistochemical staining according to their myosin heavy chain (MyHC) content. The digastric and masseter muscles were taken from Wistar strain male rats 10 weeks old. In the masseter six predefined sample locations were examined; in the digastric four. Most regions showed dominant proportions of type IIA and IIX fibers. However, both muscles also revealed a regional heterogeneity in their fiber type distribution. In the digastric, type I fibers were detected only at the central and deep areas of the anterior and posterior belly, respectively. Meanwhile, the peripheral area of the anterior belly contained a higher proportion of type IIB fibers. In the masseter, the type I fibers were absent. In the superficial masseter the distribution of IIA and IIB fibers was significantly different between the superior and inferior regions. In the deep masseter, regional differences were observed among all four examined areas, of which the posterolateral region contained the highest proportion of type IIB fibers. The cross-sectional areas of type IIB fibers were always the largest, followed by the type IIX and IIA fibers. Only a few differences in cross-sectional area of corresponding fiber types were detected between the various sites. In conclusion, the masseter and digastric muscles showed an obvious heterogeneity of fiber type composition and fiber cross-sectional area. Their heterogeneity reflects the complex role of the both muscles during function. This detailed description of the fiber type composition can serve as a reference for future studies examining the muscular adaptations after the onset of various diseases in the masticatory system.
A developmentally regulated disappearance of slow myosin in fast-type muscles of the mouse
FEBS Letters, 1984
Histochemistry and immunocytochemistry using an antibody to adult rat slow-type myosin demonstrated that about 10% of the fibers in the mouse extensor digitorum longus and semimembranosus muscles contain slow myosin during the first month after birth. In adult animals, these muscles have only t&0.8% slow myosin-containing fibers. These results demonstrate a developmentally linked disappearance of an adult-type myosin, and show that the adult phenotype of muscle fibers is not necessarily determined before birth as previously suggested.
Distinct Myosin Heavy Chain Isoform Transitions in Developing Slow and Fast Cat Hindlimb Muscles
Cells Tissues Organs, 2000
The expression of myosin heavy chain (MHC) isoforms leading to adult fiber phenotypes in the tibialis anterior (TA) and soleus muscles of the cat were investigated from embryonic day 35 to 1 year after birth. Electrophoresis and immunoblotting of myofibrils demonstrated the expression of 5 different MHC isoforms, i.e. I, IIa, IIx, embryonic, and neonatal, during development. Based on electrophoresis, the adult-like MHC composition of the soleus and TA were not observed until postnatal day 40 (P40) and 120 (P120), respectively. In contrast, immunohistochemical analyses revealed that the adult-like fiber phenotype composition was attained much later (P120) in the soleus. The existence of multiple MHC isoforms in individual fibers suggested that transitions occurred until P120 in both muscles. Adult type I fibers were first observed at P1. Adult IIA fibers were first observed at P30 in the TA and P40 in the soleus. IIX fibers were not identified until P40 in the TA. The transition to the predominantly slow phenotype of the soleus involved a gradual loss of embryonic and fast isoforms accompanied by an accumulation of slow MHC. In contrast, the expression of slow and fast MHC in the fast TA muscle was relatively unchanged throughout development. These results show that the establishment of a given MHC-based fiber phenotype varies significantly between slow and fast muscles in the kitten.
Pattern of muscle fiber type formation in the pig
Developmental Dynamics, 1995
The aim of this study was to analyze the temporal sequence of expression of the myosin isoforms in the populations of muscle fibers in the pig and to bring more information on the origin of the strikingly different pattern of fiber composition and distribution between the deep medial red (oxido-glycolytic) and superficial white (glycolytic) portions of semitendinosus (ST) muscle. Muscle samples were taken from 49-, 55-, 75-, 90-, 103-, and 113- (birth) day-old fetuses, from 6-, 11-, 21-, 35-, 50-, and 80-day-old piglets, and from a 3-year-old pig. Our results confirm the sequential formation of primary and secondary generation fibers. The use of immunohistochemistry and heterologous monoclonal antibodies (mAb) directed against specific myosin heavy chain (MHC) isoforms revealed a different pattern of gene expression between the two portions of the ST muscle for both generations of fibers. By 75 days of gestation (dg), primary myotubes from the deep medial portion stained positively for the anti-slow MHC mAb and negatively for the adult anti-fast MHC, whereas the opposite was observed in the superficial portion. Secondary fibers never expressed slow MHC until late gestation. Instead, they expressed an adult fast MHC isoform as soon as they formed in the deep medial portion and later on in the superficial portion. From late gestation to the first 3 postnatal weeks, slow MHC began to be expressed in a subpopulation of secondary fibers. These fibers were in the direct vicinity of primary myotubes in the deep medial portion, whereas their location could not be established in the superficial portion. The remaining secondary fibers matured to type IIA in the direct vicinity of these type I fibers and to type IIB at the periphery of the islets. In both portions of the muscle, a subpopulation of secondary fibers, the first ones to express slow MHC, also transitorily expressed a MHC that was identical or closely related to the alpha-cardiac MHC during the early postnatal period. A third generation of small diameter fibers was observed shortly after birth and reacted with the anti-fetal MHC mAb; their destiny remains to be established.(ABSTRACT TRUNCATED AT 400 WORDS)
Journal of Muscle Research and Cell Motility, 1994
Immunohistochemistry was used to determine the myosin composition of defined fibre types of three embryologically different adult muscles, the oro-facial, masseter and limb muscles. In addition, the myosin composition in whole muscle specimens was analysed with biochemical methods. Both similarities and differences between muscles in the content of myosin heavy chains and myosin light chains were found. Nevertheless, each muscle had its own distinct identity. Our results indicated the presence of a previously undetected fast myosin heavy chain isoform in the oro-facial type II fibre population, tentatively termed 'fast F'. The masseter contained aberrant myosin isoforms, such as foetal myosin heavy chain and s-cardiac myosin heavy chain and unique combinations of myosin heavy chain isoforms which were not found in the limb or oro-facial muscles. The type IM and IIC fibres coexpressed slow and fast A myosin heavy chains in the oro-facial and limb muscles but slow and a fast B like myosin heavy chain in the masseter. While single oro-facial and limb muscle fibres contained one or two myosin heavy chain types, single masseter fibres coexpressed up to four different myosin heavy chain isoforms. Describing the fibres according to their expression of myosin heavy chain isozymes, up to five fibre types could be distinguished in the oro-facial and limb muscles and eight in the masseter. Oro-facial and limb muscles expressed five myosin light chains, MLCls, MLC2s, MLCIF, MLC2F and MLC3F, and the masseter four, MLCls, MLC2s, MLC~F, and, in addition, an embryonic myosin light chain, MLCiemb, which is usually not present in normal adult skeletal muscle. These results probably reflect the way the muscles have evolved to meet the specialized functional requirements imposed upon them and are in agreement with the previously proposed concept that jaw and limb muscles belong to two distinct allotypes.