Atypical Myosin Heavy Chain in Rat Laryngeal Muscle

1995 ◽  
Vol 104 (3) ◽  
pp. 237-245 ◽  
Author(s):  
John M. DelGaudio ◽  
William R. Carroll ◽  
James J. Sciote ◽  
Ramon M. Esclamado
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fiber Type ◽  
Sodium Dodecyl ◽  
Laryngeal Muscles ◽  
Laryngeal Muscle ◽  
Posterior Cricoarytenoid Muscle ◽  
Limb Muscles ◽  
Electrophoretic Techniques ◽  
Posterior Cricoarytenoid

The myosin content of rat posterior cricoarytenoid and thyroarytenoid muscles was described by means of histochemical, immunohistochemical, and electrophoretic techniques. Laryngeal muscles were dissected and frozen, together with other muscles (extraocular, diaphragm, extensor digitorum longus, and soleus) for comparative purposes, then sectioned serially and stained: 1) histochemically for myofibrillar adenosine triphosphatase reactivity and 2) immunohistochemically for myosin heavy chain (MHC) content with six different antibodies. Other portions of the muscle samples were electrophoresed by a glycerol sodium dodecyl sulfatepolyacrylamide gel electrophoresis technique that separates the MHC protein into its specific isoforms. In electrophoretic comparison it limb muscles, the laryngeal muscles contained an additional MHC band we designated as type IIL (type II laryngeal) MHC. On histochemical and immunohistochemical staining, no fibers from the thyroarytenoid muscle and few fibers from the posterior cricoarytenoid muscle could be classified according to the standard fiber type categories established for limb muscles (types I, IIA, IIB, and IIX). These laryngeal muscle fibers appear to represent an atypical fiber type.

Age-Related Alterations in Myosin Heavy Chain Isoforms in Rat Intrinsic Laryngeal Muscles

2002 ◽  
Vol 111 (11) ◽  
pp. 962-967 ◽  
Author(s):  
Tatsutoshi Suzuki ◽  
Diane M. Bless ◽  
Nadine P. Connor ◽  
Charles N. Ford ◽  
Kyungah Lee ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Fiber Type ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Myosin Heavy Chain Isoforms ◽  
Laryngeal Muscles ◽  
Age Related ◽  
Posterior Cricoarytenoid

Deficits in voice and swallowing are found in the elderly, but the underlying neuromuscular mechanisms are unclear. A potential mechanism may be denervation-induced muscle fiber transformation to a slower-contracting type of muscle fiber. This study examined young, old, and denervated rat laryngeal muscles (lateral thyroarytenoid, lateral cricoarytenoid, and posterior cricoarytenoid) to examine differences in myosin heavy chain (MHC) composition. Results of sodium dodecyl sulfate–polyacrylamide gel electrophoresis analyses indicated that all muscles were composed predominately of type IIB MHC. With aging and denervation, type IIB was reduced and type IIX, a slower-contracting isoform, was increased in the lateral thyroarytenoid and lateral cricoarytenoid muscles. In the posterior cricoarytenoid muscle, the MHC composition was relatively unchanged. These findings suggest that aging may affect laryngeal adductory function by altering muscle fiber type composition to a slower-contracting isoform, in a manner similar to that observed with denervation.

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.

Myosin Heavy Chain Expression in Human Laryngeal Muscle Fibers

2000 ◽  
Vol 109 (2) ◽  
pp. 216-220 ◽  
Author(s):  
Sophie Périé ◽  
Onnik Agbulut ◽  
Jean Lacau St Guily ◽  
Gillian Sandra Butler-Browne
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Biochemical Analysis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Laryngeal Muscles ◽  
Immature Development ◽  
Posterior Cricoarytenoid ◽  
Human Limb ◽  
Intrinsic Laryngeal Muscles

Since the intrinsic laryngeal muscles in humans are involved in specialized functions, one may suppose that this would be associated with the expression of specific myosin heavy chain (MHC) isoforms, as has been reported for the rat, dog, and rabbit. In order to determine which MHCs are expressed in the human laryngeal muscles, biochemical analysis using sodium dodecyl sulfate—polyacrylamide gel electrophoresis was performed. Thyroarytenoid and posterior cricoarytenoid muscles were obtained from a 7-month-old infant and 4 adults. In the adult human laryngeal muscles, 3 bands were resolved identical to those previously described in the human limb muscles (I, IIA, and IIB MHCs). In contrast, muscles from the infant also expressed fetal MHC and a novel MHC not observed in other human skeletal muscles. This novel band migrated at the same level as the laryngeal MHC previously described in the rat. Since these 2 isoforms disappear in the adult, the persistence in the infant could be correlated with the immature development of laryngeal functions and, in particular, phonation.

Effect of Deficits in Laryngeal Sensation on Laryngeal Muscle Biochemistry

2005 ◽  
Vol 114 (5) ◽  
pp. 352-360 ◽  
Author(s):  
Hiromi Nagai ◽  
Fumikazu Ota ◽  
Nadine P. Connor
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Sodium Dodecyl ◽  
Biochemical Properties ◽  
Laryngeal Nerve ◽  
Sensory Innervation ◽  
Brown Norway ◽  
Laryngeal Muscles ◽  
Myosin Heavy Chain Isoform ◽  
Thyroarytenoid Muscle

Swallowing deficits in elderly people are significant clinical problems and may be associated with impaired pharyngolaryngeal sensation. However, the extent to which sensory innervation affects the motor system is unclear. Our purpose was to examine differences in biochemical properties of laryngeal muscles following sensory nerve ablation. We used sodium dodecyl sulfate–polyacrylamide gel electrophoresis to evaluate laryngeal muscles of young and old Fischer 344/Brown Norway rats, and rats that underwent sensory ablation via bilateral section of the superior laryngeal nerve, internal branch (SLNi), or mixed sensory-motor nerve ablation via left-sided recurrent laryngeal nerve (RLN) section. In lateral thyroarytenoid muscle, a reduction was found in the proportion of the most rapidly contracting myosin heavy chain isoform (type 2B) with SLNi section, RLN section, and aging. Section of the SLNi did not alter the proportion of any myosin heavy chain isoform within the lateral cricoarytenoid or posterior cricoarytenoid muscles, but RLN section resulted in a reduction in the proportion of type 2B. Accordingly, alteration in biochemical properties of the lateral thyroarytenoid muscle alone was demonstrated following sensory ablation. We conclude that sensory changes may affect properties of laryngeal muscles, and may thus have an impact on motor control during critical functions, such as airway protection during swallowing.

Changes in Myosin Expression in Denervated Laryngeal Muscle

1997 ◽  
Vol 106 (12) ◽  
pp. 1076-1081 ◽  
Author(s):  
John M. Delgaudio ◽  
James J. Sciote
Keyword(s):  
Fiber Type ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Type I ◽  
Type Ii ◽  
Laryngeal Muscle ◽  
Fiber Type Composition ◽  
Neural Input ◽  
Type Composition ◽  
Posterior Cricoarytenoid

The effects of chronic denervation on the myosin heavy chain (MyHC) content and muscle fiber type composition of rat laryngeal muscles are described. The posterior cricoarytenoid (PCA) and thyroarytenoid (TA) muscles were removed 3 weeks, 3 months, and 6 months after recurrent laryngeal nerve sectioning. Myofibrillar adenosine triphosphatase staining of cryostat sections was performed, and fiber type percentages were determined. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to separate MyHC isoforms, and densitometry was subsequently used for quantitative analysis. Unoperated animals served as controls. In the PCA muscle, denervation resulted in a progressive reduction in type I MyHC (the slow-contracting isoform) to an almost complete loss at 6 months, with a concomitant increase in type II MyHCs (fast-contracting isoforms, excluding type IIL). Type IIL MyHC (laryngeal-specific isoform) remained relatively constant up to 6 months after denervation. The myosin expression in the TA muscle, which contained only type II MyHCs, remained relatively constant with denervation. Changes in fiber type composition of the muscles described from tissue staining correlated with MyHC content. These findings in laryngeal muscle confirm the dependence of type I MyHC expression upon neural input, as has been found previously in limb skeletal muscles. Since the expression of all MyHCs except the IIL was modified after denervation in the PCA muscle, it is possible that the IIL isoform is maintained by factors that differ from those in the other skeletal myosins.

Trophic effect of a sciatic nerve extract on fast and slow myosin heavy chain synthesis

1981 ◽  
Vol 241 (5) ◽  
pp. C269-C272 ◽  
Author(s):  
M. C. Thibault ◽  
A. S. Havaranis ◽  
S. M. Heywood
Keyword(s):  
Sciatic Nerve ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Messenger Rna ◽  
Sodium Dodecyl ◽  
Muscle Cells ◽  
Trophic Effect ◽  
Stage Of Development ◽  
Slow Type ◽  
Chain Synthesis

Myosin heavy chain (MHC) synthesis in cultures from chick pectoralis muscle cells was determined by [35S]methionine incorporation. Two types of MHC, migrating as 200,000-dalton components on sodium dodecyl sulfate polyacrylamide gels, were distinguished with antibodies against adult fast and slow MHC. Their synthesis was revealed by autoradiography. The effect of a sciatic nerve extract on the synthesis of the two types of MHC was also determined. Control experiments show that fast MHC is primarily synthesized in 48-h cultures. At a later stage of development (5- to 7-day cultures), slow MHC is also produced. The nerve extract promotes muscle cell differentiation and stimulates the synthesis of the slow type of MHC at an earlier stage of development (i.e., at 48 h as compared with 5-7 day in controlled cultures). It is concluded therefore that presumptive fast muscle cells in culture synthesize initially fast MHC and later both types of MHC (slow and fast). These results also suggest that the sciatic nerve extract is capable either of activating the transcription of the structural gene for slow MHC or of activating the translation of preexisting messenger RNA coding for this protein.

Reinnervation of the Canine Posterior Cricoarytenoid Muscle with Sympathetic Preganglionic Neurons

1990 ◽  
Vol 99 (3) ◽  
pp. 167-174 ◽  
Author(s):  
Ian N. Jacobs ◽  
Bei-Lian Wu ◽  
Ira Sanders ◽  
Hugh F. Biller
Keyword(s):  
Vocal Cord Paralysis ◽  
Fiber Type ◽  
Electromyographic Activity ◽  
Glycogen Depletion ◽  
Bilateral Vocal Cord Paralysis ◽  
Preganglionic Neurons ◽  
Posterior Cricoarytenoid Muscle ◽  
Posterior Cricoarytenoid ◽  
The Right ◽  
Stimulation Of

This experiment investigated the reinnervation of the canine posterior cricoarytenoid (PCA) muscle with preganglionic neurons of the sympathetic nervous system. Six dogs had their right recurrent laryngeal nerve (RLN) sectioned. Four of these dogs had the sympathetic cervical trunk (SCT) implanted into the right PCA muscle, and the two remaining dogs served as denervated controls. Four months later all dogs underwent videolaryngoscopy, electromyography, and electrical stimulation of the SCT. The PCA muscles were excised, sectioned, and stained for glycogen and ATPase. All four experimental PCA muscles demonstrated electrically evoked abduction and tonic electromyographic activity. In two of the specimens, staining (ATPase and PAS) revealed areas of reinnervation with fiber type grouping and glycogen depletion. These results are consistent with the successful reinnervation of the PCA muscle. Further refinement of this technique could be of benefit to patients with bilateral vocal cord paralysis.

scholarly journals ProNGF/p75NTR Axis Drives Fiber Type Specification by Inducing the Fast-Glycolytic Phenotype in Mouse Skeletal Muscle Cells

Cells ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 2232
Author(s):  
Valentina Pallottini ◽  
Mayra Colardo ◽  
Claudia Tonini ◽  
Noemi Martella ◽  
Georgios Strimpakos ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myogenic Differentiation ◽  
Fiber Type ◽  
Pcr Analysis ◽  
Mdx Mouse ◽  
Mdx Mice ◽  
Muscle Physiology

Despite its undisputable role in the homeostatic regulation of the nervous system, the nerve growth factor (NGF) also governs the relevant cellular processes in other tissues and organs. In this study, we aimed at assessing the expression and the putative involvement of NGF signaling in skeletal muscle physiology. To reach this objective, we employed satellite cell-derived myoblasts as an in vitro culture model. In vivo experiments were performed on Tibialis anterior from wild-type mice and an mdx mouse model of Duchenne muscular dystrophy. Targets of interest were mainly assessed by means of morphological, Western blot and qRT-PCR analysis. The results show that proNGF is involved in myogenic differentiation. Importantly, the proNGF/p75NTR pathway orchestrates a slow-to-fast fiber type transition by counteracting the expression of slow myosin heavy chain and that of oxidative markers. Concurrently, proNGF/p75NTR activation facilitates the induction of fast myosin heavy chain and of fast/glycolytic markers. Furthermore, we also provided evidence that the oxidative metabolism is impaired in mdx mice, and that these alterations are paralleled by a prominent buildup of proNGF and p75NTR. These findings underline that the proNGF/p75NTR pathway may play a crucial role in fiber type determination and suggest its prospective modulation as an innovative therapeutic approach to counteract muscle disorders.

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