Heterogeneity of myosin heavy-chain expression in fast-twitch fiber types of mature avian pectoralis muscle

1996 ◽  
Vol 74 (5) ◽  
pp. 715-728 ◽  
Author(s):  
B. W. C. Rosser ◽  
D. M. Waldbillig ◽  
M. Wick ◽  
E. Bandman
Keyword(s):  
Monoclonal Antibodies ◽  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Fiber Types ◽  
Pectoralis Muscle ◽  
Western Blots ◽  
Myhc Isoforms ◽  
Fast Twitch ◽  
Myhc Expression

The aims of this study are to investigate the diversity of myosin heavy-chain (MyHC) expression among avian fast-twitch fibers, and to test the hypothesis that dissimilar MyHC isoforms are found in each of the principal avian fast-twitch fiber types. MyHCs within the muscle fibers of the pectoralis of 31 species of bird are characterized using immunocytochemical methods. A library of 11 monoclonal antibodies previously produced against chicken MyHCs is used. The specificity of these antibodies for MyHCs in each of the muscles studied is confirmed by Western blots. The results show that avian fast-twitch glycolytic fibers and fast-twitch oxidative-gylcolytic fibers can contain different MyHCs. Among the species studied, there is also a conspicuous variety of MyHC isoforms expressed. In addition, the results suggest that two epitopes are restricted to chickens and closely allied gallinaceous birds. There are no apparent correlations between MyHC epitope and presupposed contractile properties. However, the presence of different isoforms in different fast-twitch fiber types suggests a correlation between isoform and contractile function.Key words: muscle, fiber, myosin, avian.

scholarly journals Myosin Heavy Chain Expression Can Vary over the Length of Jaw and Leg Muscles

2016 ◽  
Vol 201 (2) ◽  
pp. 130-137 ◽  
Author(s):  
J.A.M. Korfage ◽  
K.E. Kwee ◽  
V. Everts ◽  
G.E.J. Langenbach
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Fiber Type ◽  
Staining Intensity ◽  
Medial Gastrocnemius ◽  
Hybrid Fibers ◽  
Leg Muscles ◽  
Myhc Isoforms ◽  
Myhc Expression

Muscle fiber type classification can be determined by its myosin heavy chain (MyHC) composition based on a few consecutive sections. It is generally assumed that the MyHC expression of a muscle fiber is the same over its length since neural stimulation and systemic influences are supposed to be the same over its length. We analyzed this in detail in three muscle types: the temporalis (closer) and digastricus (opener; both first brachial arch), and the medial gastrocnemius (somite). Sections of the muscles were incubated with monoclonal antibodies against various MyHC isoforms, and the distribution of these isoforms within individual fibers was followed over a distance of approximately 1 mm. The staining intensity of a fiber was measured and compared with the other fibers in the section. In the temporalis, digastricus, and gastrocnemius, 46, 11, and 15%, respectively, of their MyHC-I fibers showed a variation in the staining intensity over the length of their fibers, as well as 47, 87, and 22%, respectively, of their MyHC-IIA fibers. Most variable fibers were found amongst those with an overall relative intermediate staining intensity, which are presumably hybrid fibers. We conclude that different parts of a muscle fiber can have different fiber type compositions and, thus, contractile properties. Some muscle parts might reach their maximum contraction peak sooner or later than a muscle part a few microns further away. Next to stimulation by the nerve and systemic influences, local influences might also have an impact on the MyHC expression of the fiber.

scholarly journals Immunohistochemical Analysis of Myosin Heavy Chain Expression in Laryngeal Muscles of the Rabbit, Cat, and Baboon

2008 ◽  
Vol 56 (10) ◽  
pp. 929-950 ◽  
Author(s):  
Hannah S. Rhee ◽  
Joseph F.Y. Hoh
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fiber Type ◽  
Immunohistochemical Analysis ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Laryngeal Muscles ◽  
Myhc Isoforms ◽  
Posterior Cricoarytenoid ◽  
Myhc Expression

We studied myosin heavy chain (MyHC) expression and fiber type distribution in laryngeal muscles in the rabbit, cat, and baboon using immunohistochemistry with highly MyHC-specific antibodies. Two types of variation in MyHC expression were found: between muscles of different function within species and within specific muscles between species. Within species, thyroarytenoid (Ta), an adductor, had faster MyHCs and fiber type profiles than the abductor, posterior cricoarytenoid (PCA), which expressed faster MyHCs than the vocal fold tensor, cricothyroid (CT). Between species, laryngeal muscles generally expressed faster MyHCs in small animals than in larger ones: extraocular (EO) MyHC was expressed in the Ta and PCA of the rabbit but not in the cat and baboon, whereas 2B MyHC was expressed in these muscles of the cat but not of the baboon. The CT expressed only MyHC isoforms and fiber types found in the limb muscles of the same species. These results are discussed in light of the hypothesis that the between-species variations in laryngeal muscle fiber types are evolutionary adaptations in response to changes in body mass and respiratory frequency. Within-species variations in fiber types ensure that protective closure of the glottis is always faster than movements regulating airflow during respiration.

Myogenic specification in somites: induction by axial structures

Development ◽  
1994 ◽  
Vol 120 (6) ◽  
pp. 1443-1452 ◽  
Author(s):  
N. Buffinger ◽  
F.E. Stockdale
Keyword(s):  
Monoclonal Antibodies ◽  
Chick Embryo ◽  
Myosin Heavy Chain ◽  
Neural Tube ◽  
Heavy Chain ◽  
Muscle Fibers ◽  
Fiber Types ◽  
Early Chick Embryo ◽  
Explant Cultures ◽  
Fast Myhc

Specification of the myogenic phenotype in somites was examined in the early chick embryo using organotypic explant cultures stained with monoclonal antibodies to myosin heavy chain. It was found that myogenic specification (formation of muscle fibers in explants of somites or segmental plates cultured alone) does not occur until Hamburger and Hamilton stage 11 (12-14 somites). At this stage, only the somites in the rostral half of the embryo are myogenically specified. By Hamburger and Hamilton stage 12 (15-17 somites), the three most caudal somites were not specified to be myogenic while most or all of the more rostral somites are specified to myogenesis. Somites from older embryos (stage 13–15, 18–26 somites) showed the same pattern of myogenic specification--all but the three most caudal somites were specified. We investigated the effects of the axial structures, the notochord and neural tube, on myogenic specification. Both the notochord and neural tube were able to induce myogenesis in unspecified somites. In contrast, the neural tube, but not the notochord, was able to induce myogenesis in explants of segmental plate, a structure which is not myogenic when cultured alone. When explants of specified somites were stained with antibodies to slow or fast MyHC, it was found that myofiber diversity (fast and fast slow fibers) was established very early in development (as early as Hamburger and Hamilton stage 11). We also found fiber diversity in explants of unspecified somites (the three most caudal somites from stage 11 to 15) when they were recombined with notochord or neural tube. We conclude that myogenic specification in the embryo results in diverse fiber types and is an inductive process which is mediated by factors produced by the neural tube and notochord.

Architecture of the pectoralis muscle of the Japanese quail (Coturnix japonica): histochemical and ultrastructural characterization, and distribution of muscle fiber types

1987 ◽  
Vol 65 (1) ◽  
pp. 63-71 ◽  
Author(s):  
B. W. C. Rosser ◽  
J. C. George ◽  
S. K. Frombach
Keyword(s):  
Japanese Quail ◽  
Muscle Fiber ◽  
Coturnix Japonica ◽  
Muscle Fiber Types ◽  
Fiber Types ◽  
Pectoralis Muscle ◽  
Motor End Plate ◽  
Ultrastructural Characteristics ◽  
Fast Twitch ◽  
Acid Stable

The muscle fibers in the pectoralis muscle of the Japanese quail (Coturnix japonica) are classified as fast-twitch glycolytic (FG), fast-twitch oxidative-glycolytic (FOG), and slow-tonic on the basis of their histochemical and ultrastructural characteristics. There is an increasing proportion of FOG/FG fibers along a superficial to deep gradient throughout the entire belly of the muscle. Slow-tonic fibers are present in low numbers, and are restricted to a tiny area located in the deepest fasciculi of the cranial third of the muscle. This distribution of muscle fiber types is typical of those vertebrate muscles adapted to a locomotory function. The slow-tonic fibers are alkali-stable and acid-stable when preincubated for myofibrillar adenosine triphosphatase (mATPase) activity. Slow fibers in the chicken pectoralis and mouse soleus muscle, both types previously described as alkali-labile, acid-stable for mATPase activity, cannot be distinguished from each other or Japanese quail slow-tonic fibers on the basis of several ultrastructural characteristics: Z-line width, metabolic differences, or fusion of myofibrils. While mammalian slow fibers have one large motor end plate, all avian slow fibers have small multiple motor end plates. Mammalian slow fibers are slow-twitch, and avian slow fibers are probably slow-tonic. More complex secondary synaptic clefts distinguish mammalian from all avian fiber types.

Geniohyoid muscle properties and myosin heavy chain composition are altered after short-term intermittent hypoxic exposure

2005 ◽  
Vol 98 (3) ◽  
pp. 889-894 ◽  
Author(s):  
Eung-Kwon Pae ◽  
Jennifer Wu ◽  
Daniel Nguyen ◽  
Ryan Monti ◽  
Ronald M. Harper
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Total Duration ◽  
Upper Airway ◽  
Hypoxic Exposure ◽  
Fiber Types ◽  
Short Term ◽  
Fiber Composition ◽  
Obstructive Sleep

Patients with obstructive sleep apnea (OSA) often exhibit fatigued or inefficient upper airway dilator and constrictor muscles; an upper airway dilator, the geniohyoid (GH) muscle, is a particular example. Intermittent hypoxia (IH) is a frequent concomitant of OSA, and it may trigger muscle fiber composition changes that are characteristic of a fatigable nature. We examined effects of short-term IH on diaphragmatic and GH muscle fiber composition and fatigue properties by exposing 24 rats to alternating 10.3% O2-balance N2 and room air every 480 s (240 s duty cycle) for a total duration of 5, 10, 15, 20, or 30 h. Sternohyoid fiber composition was also examined. Control animals were exposed to room air on the same schedule. Single-fiber analyses showed that GH muscle fiber types changed completely from myosin heavy chain (MHC) type 2A to MHC type 2B after 10 h of exposure, and the conversion was maintained for at least 30 h. Sternohyoid muscle fibers showed a delayed transition from MHC type 2A/2B to MHC type 2B. In contrast, major fiber types of the diaphragm were not significantly altered. The GH muscles showed similar tension-frequency relationships in all groups, but an increased fatigability developed, proportional to the duration of IH treatment. We conclude that short-term IH exposure alters GH muscle composition and physical properties toward more fatigable, fast-twitch types and that it may account for the fatigable upper airway fiber types found in sleep-disturbed breathing.

scholarly journals Evidence for myoblast-extrinsic regulation of slow myosin heavy chain expression during muscle fiber formation in embryonic development.

1993 ◽  
Vol 121 (4) ◽  
pp. 795-810 ◽  
Author(s):  
M Cho ◽  
S G Webster ◽  
H M Blau
Keyword(s):  
Embryonic Development ◽  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Fiber Formation ◽  
Slow Myosin ◽  
Slow Myosin Heavy Chain ◽  
Slow Myhc ◽  
Myhc Expression

Vertebrate muscles are composed of an array of diverse fast and slow fiber types with different contractile properties. Differences among fibers in fast and slow MyHC expression could be due to extrinsic factors that act on the differentiated myofibers. Alternatively, the mononucleate myoblasts that fuse to form multinucleated muscle fibers could differ intrinsically due to lineage. To distinguish between these possibilities, we determined whether the changes in proportion of slow fibers were attributable to inherent differences in myoblasts. The proportion of fibers expressing slow myosin heavy chain (MyHC) was found to change markedly with time during embryonic and fetal human limb development. During the first trimester, a maximum of 75% of fibers expressed slow MyHC. Thereafter, new fibers formed which did not express this MyHC, so that the proportion of fibers expressing slow MyHC dropped to approximately 3% of the total by midgestation. Several weeks later, a subset of the new fibers began to express slow MyHC and from week 30 of gestation through adulthood, approximately 50% of fibers were slow. However, each myoblast clone (n = 2,119) derived from muscle tissues at six stages of human development (weeks 7, 9, 16, and 22 of gestation, 2 mo after birth and adult) expressed slow MyHC upon differentiation. We conclude from these results that the control of slow MyHC expression in vivo during muscle fiber formation in embryonic development is largely extrinsic to the myoblast. By contrast, human myoblast clones from the same samples differed in their expression of embryonic and neonatal MyHCs, in agreement with studies in other species, and this difference was shown to be stably heritable. Even after 25 population doublings in tissue culture, embryonic stage myoblasts did not give rise to myoblasts capable of expressing MyHCs typical of neonatal stages, indicating that stage-specific differences are not under the control of a division dependent mechanism, or intrinsic "clock." Taken together, these results suggest that, unlike embryonic and neonatal MyHCs, the expression of slow MyHC in vivo at different developmental stages during gestation is not the result of commitment to a distinct myoblast lineage, but is largely determined by the environment.

scholarly journals Limb myosin heavy chain isoproteins and muscle fiber types in the adult goat (Capra hircus)

2001 ◽  
Vol 264 (3) ◽  
pp. 284-293 ◽  
Author(s):  
Anastasio Argüello ◽  
Juan-Luis López-Fernández ◽  
José-Luis L. Rivero
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Capra Hircus ◽  
Muscle Fiber Types ◽  
Fiber Types

Promoter analysis of the fish gene of slow/cardiac-type myosin heavy chain implicated in specification of muscle fiber types

2018 ◽  
Vol 44 (2) ◽  
pp. 679-691 ◽  
Author(s):  
Shigeharu Kinoshita ◽  
Saltuk Bugrahan Ceyhun ◽  
Asaduzzamann Md ◽  
Bhuiyan Sharmin Siddique ◽  
Dadasaheb B. Akolkar ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Promoter Analysis ◽  
Muscle Fiber Types ◽  
Fiber Types
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