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In situ hybridization (ISH) of myosin heavy chain (MHC) mRNA, immunofluorescent detection of MHC protein, and oxidative enzyme histochemistry were performed on the same fibers in serially sectioned rabbit skeletal muscle. By combining these three techniques quantitatively, on a fiber-by-fiber basis, fibers that expressed mRNA complementary to a fast MHC cDNA pMHC24-79 of unknown subtype (Maeda et al., 1987) were classified into fiber types with respect to slow myosin expression and oxidative capacity. As expected, slow fibers had low hybridization to pMHC24-79. Fast fibers were divided into three subtypes. mRNA from the low oxidative fibers (fast-glycolytic, IIB) did not hybridize with pMHC24-79. Fast fibers whose mRNA hybridized best to pMHC24-79 were mainly in the intermediate range of oxidative capacity (probably IIX). The fast fibers with the highest oxidative capacity had low hybridization to this MHC mRNA (probably IIA). Thus, pMHC24-79 was identified as a clone of a fast isomyosin, tentatively designated as the fast IIX with intermediate oxidative capacity. The expression of more than a single species of fast and slow isomyosin mRNAs in classically defined fiber type was considered in interpreting these results.
Anat Rec 1991 May
PMID:Expression of a fast myosin heavy chain mRNA in individual rabbit skeletal muscle fibers with intermediate oxidative capacity. 182 91

An immunohistochemical study of cardiac alpha and beta myosin heavy chain (MHC) expression during rat heart morphogenesis was performed. In tubular hearts (embryonic days, ED10-11) coexpression of both cardiac alpha and beta MHC was found throughout the heart, except for the left free wall of the atrium, where only cardiac alpha MHC is detected. A transition of coexpression to single expression of either cardiac alpha or beta MHC begins at the same time in both atria and ventricles but requires a longer time for completion in the ventricules; in the atria transition takes place during the period ED 12-13 and in the ventricles during ED12-15. Furthermore, expression of cardiac alpha and beta MHC was detected in the sinus venosus, and cardiac alpha MHC expression was detected in the pulmonary veins. A comparison of the results obtained in chicken embryos revealed that in tubular hearts the expression pattern is similar, whereas in later developmental stages two major differences were observed: 1) transition of coexpression to single expression in rat ventricles appears to take a longer developmental period; 2) the persistence of areas of coexpression in the sinoatrial junction, dorsal mesocardium, atrioventricular junction, and outflow tract, as found in the chicken embryo in later developmental stages, is not found in the rat heart.
Anat Rec 1989 Jul
PMID:Isomyosin expression patterns during rat heart morphogenesis: an immunohistochemical study. 278 21

The diaphragm of neonatal horses is significantly different from the diaphragm of adult horses in terms of histochemical fiber type composition, myosin heavy chain isoform, and native myosin isoform composition. There is a significant increase in the percentage of type I fibers present in the diaphragm with increasing age from birth through about seven months postnatal age. A possible lack of postural tone in the hiatal region of the neonatal diaphragm is suggested to account for increased incidence of vomiting or aspiration pneumonia in younger horses. The isoform data lead to rejection of the hypothesis that the diaphragm of the horse should, as an ungulate, be relatively precocial in its rate of maturation relative to other non-ungulate mammals that have been studied.
Anat Rec 1994 Mar
PMID:Neonatal development of the diaphragm of the horse, Equus caballus. 817 12

The horse provides an interesting model for study of the structure and function of the mammalian diaphragm. Multiple regions of diaphragm from seven adult horses were prepared for histochemistry, immunocytochemistry, myosin heavy chain electrophoresis, and native myosin electrophoresis. Two additional adults were dissected to demonstrate myofiber and central tendon morphology and stained for acetylcholinesterase to demonstrate motor endplates. All regions of the adult diaphragm were histochemically characterized by a preponderance of type I fibers with some type IIa fibers. Type IIb fibers were absent in all adult specimens. Myosin heavy chain electrophoresis supported the histochemical study: two isoform bands were present on SDS gels that comigrated at the same rate as rat type I and IIa myosin heavy chain isoforms. No isoform was determined to comigrate with rat type IIb heavy chain isoforms. Native myosin isoform analysis revealed two isoforms that comigrated with rat FM-4 and FM-3 (FM = fast myosin) and two isoforms that comigrated with rat SM-1 and SM-2 (SM = slow myosin) isoforms. In some samples, a third slow native myosin isoform was observed that comigrated at the same rate as the SM-3 of the equine biceps brachii muscle. This doublet (or "triplet") of slow isoforms is unique to some horse muscles compared with other adult animals studied. It is not known if these multiple slow native myosin isoforms confer some functional advantage to the equine muscles. The adult equine diaphragm also differs in its morphology by having a large central tendon compared to that in other mammals, and is predominantly slow in fiber type and myosin isoform composition.
Anat Rec 1994 Mar
PMID:Morphological, histochemical, and myosin isoform analysis of the diaphragm of adult horses, Equus caballus. 817 13

The effects of a chronic (up to 360 days) reduction in neuromuscular activity (defined as electrical activation and loading) on myosin heavy chain (MHC) isoform expression in the rat soleus muscle were studied. A complete mid-thoracic (T7-T8) spinal cord transection (ST) was used to induce a reduction in soleus muscle neuromuscular activity. Electrophoretic analyses revealed that MHC-I was progressively decreased after ST, accounting for approx. 90% of the total soleus MHC in controls and only approx. 12% 1 year after ST. The reductions in the proportion of MHC-I were countered by increases in MHC-IIa and MHC-IIx with the increase in MHC-IIx preceding the increase in MHC-IIa. Curiously, MHC-IIb was expressed only at very low levels. Thus, a complete transformation from predominantly MHC-I to MHC-IIb did not occur. Many fibers (up to approx. 80%) contained multiple MHCs (hybrid fibers) after ST. The proportion of hybrid fibers was maintained at a high level (approx. 50%) 1 year after ST. These data suggest that: 1) a prolonged reduction in neuromuscular activity was not sufficient to induce high level MHC-IIb expression by the soleus muscle; and 2) hybrid fibers were not simply transitional fibers. Thus, it appears that under appropriate conditions hybrid fibers may represent a "stable" fiber phenotype.
Anat Rec 1999 06 01
PMID:Persistence of hybrid fibers in rat soleus after spinal cord transection. 1035 20

Most of the sounds of human speech are produced by vibration of the vocal folds, yet the biomechanics and control of these vibrations are poorly understood. In this study the muscle within the vocal fold, the thyroarytenoid muscle (TA), was examined for the presence and distribution of slow tonic muscle fibers (STF), a rare muscle fiber type with unique contraction properties. Nine human TAs were frozen and serially sectioned in the frontal plane. The presence and distribution pattern of STF in each TA were examined by immunofluorescence microscopy using the monoclonal antibodies (mAb) ALD-19 and ALD-58 which react with the slow tonic myosin heavy chain (MyHC) isoform. In addition, TA muscle samples from adjacent frozen sections were also examined for slow tonic MyHC isoform by electrophoretic immunoblotting. STF were detected in all nine TAs and the presence of slow tonic MyHC isoform was confirmed in the immunoblots. The STF were distributed predominantly in the medial aspect of the TA, a distinct muscle compartment called the vocalis which is the vibrating part of the vocal fold. STF do not contract with a twitch like most muscle fibers, instead, their contractions are prolonged, stable, precisely controlled, and fatigue resistant. The human voice is characterized by a stable sound with a wide frequency spectrum that can be precisely modulated and the STF may contribute to this ability. At present, the evidence suggests that STF are not presented in the vocal folds of other mammals (including other primates), therefore STF may be a unique human specialization for speech.
Anat Rec 1999 10 01
PMID:Slow tonic muscle fibers in the thyroarytenoid muscles of human vocal folds; a possible specialization for speech. 1048 12

The primary focus of this study was the accurate classification of limb skeletal muscle fiber types in adult goats (Capra hircus) according to the myosin heavy chain (MHC) isoform they express. Combined methodologies of gel electrophoresis, immunoblotting, immunohistochemistry, myofibrillar ATPase (mATPase), and quantitative metabolic enzyme histochemistry of M. semitendinosus samples were developed. Three MHCs were identified and tentatively designated as types I, IIA, and IIX. Five fiber types were defined immunohistochemically according to their MHC content: I, I+IIA, IIA, IIAX, and IIX. The hybrid fast-twitch fibers (IIAX) totaled 21% of the fiber population analyzed. The three major pure fibers (I, IIA, and IIX) could be objectively separated upon the basis of their mATPase activities after acid and alkaline preincubations. The prominent number of hybrid fibers, however, could not be delineated with these mATPase methods. Metabolic and size properties of muscle fibers varied according to their MHC content, but overlapped the full range of muscle fiber phenotypes. These integrated data demonstrate that type II skeletal muscle fibers of small ruminants have been misclassified in previous studies. The immunohistochemical approach developed in the present study offers new prospects for muscle fiber typing in caprine experimental studies and meat production technologies.
Anat Rec 2001 11 01
PMID:Limb myosin heavy chain isoproteins and muscle fiber types in the adult goat (Capra hircus). 1159 10

Key morphogenetic events during heart ontogenesis are similar in different vertebrate species. We report that in primitive vertebrates, i.e., cartilaginous fishes, both the embryonic and the adult heart show a segmental subdivision similar to that of the embryonic mammalian heart. Early morphogenetic events during cardiac development in the dogfish are long-lasting, providing a suitable model to study changes in pattern of gene expression during these stages. We performed a comparative study among dogfish, chicken, rat, and mouse to assess whether species-specific qualitative and/or quantitative differences in myosin heavy chain (MyHC) distribution arise during development, indicative of functional differences between species. MyHC RNA content was investigated by means of in situ hybridisation using an MyHC probe specific for a highly conserved domain, and MyHC protein content was assessed by immunohistochemistry. MyHC transcripts were found to be homogeneously distributed in the myocardium of the tubular and embryonic heart of dogfish and rodents. A difference between atrial and ventricular MyHC content (mRNA and protein) was observed in the adult stage. Interestingly, differences in the MyHC content were observed at the tubular heart stage in chicken. These differences in MyHC content illustrate the distinct developmental profiles of avian and mammalian species, which might be ascribed to distinct functional requirements of the myocardial segments during ontogenesis. The atrial myocardium showed the highest MyHC content in the adult heart of all species analysed (dogfish (S. canicula), mouse (M. musculus), rat (R. norvegicus), and chicken (G. gallus)). These observations indicate that in the adult heart of vertebrates the atrial myocardium contains more myosin than the ventricular myocardium.
Anat Rec 2002 Sep 01
PMID:Species-specific differences of myosin content in the developing cardiac chambers of fish, birds, and mammals. 1220 62

This short review discusses changes in the fibre type distribution, myosin heavy chain isoform composition and histological appearance of the very elderly human skeletal muscle. Point of origin of the discussion comes from data that we have obtained from muscle biopsies from the vastus lateralis muscle of a group of frail very elderly subjects (age: 88 +/- 3 years, range 85-97). Myosin heavy chain composition of muscle homogenates and single fibres, fibre type distribution, fibre size and capillary density were examined and compared with muscle biopsies from the young vastus lateralis muscle. Histological preparations of the muscle biopsies from our elderly subjects showed extended "grouping" (Nygaard & Sanchez, Anat Rec 1992: 202: 451-459) of the fibre types as well as significant changes in the appearance and size of the individual muscle fibres. On average, the fibre type composition of our very elderly subjects do not seem to be different to what is observed in a corresponding young group when examined with ATPase histochemistry. Likewise, the MHC composition of the muscle homogenates is comparable to what is observed in young subjects. Nevertheless, a detailed examination of the MHC composition of single fibres from the old subjects revealed that the most prominent phenotype was fibres co-expressing MHC I and MHC IIA. This is very different from what is observed in the young muscle. Detailed investigation of longitudinally cut fibres indicated that some fibres in the very old muscle, in contrast to the young muscle, switch fibre type along the length of the fibre or contain areas or nuclear domains in which the MHC expression is different from the remaining part of the fibre.
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PMID:Muscle fibre type adaptation in the elderly human muscle. 1253 16

Our knowledge of the temporal expression of postnatal (adult) fast myosin heavy chain (MyHC) isoforms (2a, 2x, and 2b) in prenatal muscles is limited. Using the pig as a target species and large-animal model, we report on the qualitative and quantitative expression of the major post- and prenatal MyHC isoforms during gestation, as determined by TaqMan real-time PCR and immunohistochemistry. We found that postnatal fast MyHC mRNAs and proteins were expressed much earlier in the pig (gestation day 35) than was previously reported in small mammals. There was a high degree of coexpression and colocalisation of pre- and postnatal MyHC mRNAs and proteins in prenatal muscles. During a period of prenatal muscle growth (gestation days 35-77), relative expression of MyHC isoforms (embryonic > 2a > 2x > 2b) correlated with the gene order in the skeletal MyHC cluster, which suggests the possible presence of cis-acting elements on the same side as the MyHC embryonic gene associated with temporal regulation.
Anat Rec A Discov Mol Cell Evol Biol 2003 Aug
PMID:Postnatal myosin heavy chain isoforms in prenatal porcine skeletal muscles: insights into temporal regulation. 1284 9


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