Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition.

Reiser, Peter J.; Moss, Richard L.; Giulian, G G; Greaser, M L

doi:10.1016/s0021-9258(17)39330-4

Cited by 359 publications

(37 citation statements)

References 25 publications

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“…The expression and distribution patterns of the MHC isoforms in a muscle highly correlate with the functional demands of the muscle. Electrophysiological studies have demonstrated that the maximal velocity of shortening of muscle fibers is largely determined by and highly dependent on their MHC isoform composition (Reiser et al 1985;Larsson and Moss 1993). In addition to the major MHC isoforms (i.e., MHCI, IIa, IIx, and IIb), the unique (i.e., MHC-␣ and MHC-ton) and developmental (i.e., neonatal and embryonic) MHC isoforms could be found in restricted cranial muscles, and the tissue-specific superfast MHC isoform was found in extraocular and masticatory muscles (Rowlerson et al 1982;Sartore et al 1987).…”

Section: Discussionmentioning

confidence: 99%

Expression of Unique and Developmental Myosin Heavy Chain Isoforms in Adult Human Digastric Muscle

Wang

Han

et al. 2004

J Histochem Cytochem.

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Digastric muscle (DGM) is a powerful jaw-opening muscle that participates in chewing, swallowing, breathing, and speech. For better understanding of its contractile properties, five pairs of adult human DGMs were obtained from autopsies and processed with immunocytochemistry and/or immunoblotting. Monoclonal antibodies against alpha-cardiac, slow tonic, neonatal, and embryonic myosin heavy chain (MHC) isoforms were employed to determine whether the DGM fibers contain these MHC isoforms, which have previously been demonstrated in restricted specialized craniocervical skeletal muscles but have not been reported in normal adult human trunk and limb muscles. The results showed expression of all these MHC isoforms in adult human DGMs. About half of the fibers reacted positively to the antibody specific for the alpha-cardiac MHC isoform in DGMs, and the number of these fibers decreased with age. Slow tonic MHC isoform containing fibers accounted for 19% of the total fiber population. Both the alpha-cardiac and slow tonic MHC isoforms were found to coexist mainly with the slow twitch MHC isoform in a fiber. A few DGM fibers expressed the embryonic or neonatal MHC isoform. The findings suggest that human DGM fibers may be specialized to facilitate performance of complex motor behaviors in the upper airway and digestive tract.

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Section: Discussionmentioning

confidence: 99%

Expression of Unique and Developmental Myosin Heavy Chain Isoforms in Adult Human Digastric Muscle

Wang

Han

et al. 2004

J Histochem Cytochem.

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“…In general terms, MHC-I-expressing fibers are small, rich in oxidative enzymes, slow in contraction, and have a greater resistance to fatigue, while MHC-IIb-expressing fibers are large, rich in glycolytic enzymes, and fast in contraction due to the developed sarcoplasmic reticulum that allows the rapid release of calcium ions, and a predominantly anaerobic metabolism [40,41]. Specifically, fiber contraction correlates with myosin ATPase activity with relative velocities of I < IIa < IIx < IIb [42,43]. Furthermore, skeletal muscle can be classified as postural or non-postural according to its function and the percentage of each fiber-type [44].…”

Section: Fiber-types Of Skeletal Muscle and Its Adaptation To Physicamentioning

confidence: 99%

Function and Fiber-Type Specific Distribution of Hsp60 and αB-Crystallin in Skeletal Muscles: Role of Physical Exercise

D’Amico

Fiore

Caporossi

et al. 2021

Biology

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Skeletal muscle is a plastic and complex tissue, rich in proteins that are subject to continuous rearrangements. Skeletal muscle homeostasis can be affected by different types of stresses, including physical activity, a physiological stressor able to stimulate a robust increase in different heat shock proteins (HSPs). The modulation of these proteins appears to be fundamental in facilitating the cellular remodeling processes related to the phenomenon of training adaptations such as hypertrophy, increased oxidative capacity, and mitochondrial activity. Among the HSPs, a special attention needs to be devoted to Hsp60 and αB-crystallin (CRYAB), proteins constitutively expressed in the skeletal muscle, where their specific features could be highly relevant in understanding the impact of different volumes of training regimes on myofiber types and in explaining the complex picture of exercise-induced mechanical strain and damaging conditions on fiber population. This knowledge could lead to a better personalization of training protocols with an optimal non-harmful workload in populations of individuals with different needs and healthy status. Here, we introduce for the first time to the reader these peculiar HSPs from the perspective of exercise response, highlighting the control of their expression, biological function, and specific distribution within skeletal muscle fiber-types.

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“…IIA . I (Reiser et al 1985a;Bottinelli et al 1991;Galler et al 1994). However, there are no pure fibers in the adult human UES.…”

Section: The Journal Of Histochemistry and Cytochemistrymentioning

confidence: 99%

Adult Human Upper Esophageal Sphincter Contains Specialized Muscle Fibers Expressing Unusual Myosin Heavy Chain Isoforms

Wang

et al. 2006

J Histochem Cytochem.

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New Jersey (IS)S U M M A R Y The functional upper esophageal sphincter (UES) is composed of the cricopharyngeus muscle (CP), the most inferior part of the inferior pharyngeal constrictor (iIPC), and the upper esophagus (UE). This sphincter is collapsed and exhibits sustained muscle activity in the resting state; it only relaxes and opens during swallowing, vomiting, and belching. The tonic contractile properties of the UES suggest that the skeletal muscle fibers in this sphincter differ from those in the limb and trunk muscles. In this study, myosin heavy chain (MHC) composition in the adult human UES muscles obtained from autopsies was investigated using immunocytochemical and immunoblotting techniques. Results showed that the adult human UES muscle fibers expressed unusual MHC isoforms such as slow-tonic (MHC-ton), a-cardiac (MHC-a), neonatal (MHC-neo), and embryonic (MHC-emb), which coexisted with the major MHCs (i.e., MHCI, IIa, and IIx). MHC-ton and MHC-a were coexpressed predominantly with slow-type I MHC isoform, whereas MHC-neo and MHC-emb coexisted mainly with fast-type IIa MHC. A slow inner layer (SIL) and a fast outer layer (FOL) in the iIPC and CP were identified immunocytochemically. MHC-ton-and MHC-a-containing fibers were concentrated mainly in the SIL, whereas MHC-neo-and MHC-emb-containing fibers were distributed primarily to the FOL. Identification of the specialized muscle fibers and their distribution patterns in the adult human UES is valuable for a better understanding of the physiological and pathophysiological behaviors of the sphincter.(J Histochem Cytochem

show abstract

Shortening velocity in single fibers from adult rabbit soleus muscles is correlated with myosin heavy chain composition.

Cited by 359 publications

References 25 publications

Expression of Unique and Developmental Myosin Heavy Chain Isoforms in Adult Human Digastric Muscle

Expression of Unique and Developmental Myosin Heavy Chain Isoforms in Adult Human Digastric Muscle

Function and Fiber-Type Specific Distribution of Hsp60 and αB-Crystallin in Skeletal Muscles: Role of Physical Exercise

Adult Human Upper Esophageal Sphincter Contains Specialized Muscle Fibers Expressing Unusual Myosin Heavy Chain Isoforms

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