Differential Expression of Myosin Heavy Chain Isoforms between Abductor and Adductor Muscles in the Human Larynx

Li, Zhao Bo; Lehar, Mohamed; Nakagawa, Hideki; Hoh, Joseph F. Y.; Flint, Paul W.

doi:10.1016/j.otohns.2003.09.009

Cited by 48 publications

(56 citation statements)

References 22 publications

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“…The identification of MyHC isoforms in Adreani et al (2006) relied on a comparison of the electrophoretic mobilities of equine and murine MyHCs in SDS-PAGE gels, under the as- sumption that the mobility of each MyHC isoform is independent of species, which clearly cannot be relied upon (Galler et al 1997;Reiser and Kline 1998;Zhong et al 2001). The absence of 2B and EO MyHCs in horse laryngeal muscles is consistent with findings in other large animals-humans (Li et al 2004), baboons (Rhee and Hoh 2008), and cattle (Toniolo et al 2005). These results reflect the notion that variations in fiber types in laryngeal muscles among species represent an adaptation to optimize the control of airway resistance in relation to the respiratory frequency and metabolic rate of the animal (Rhee and Hoh 2008).…”

Section: Isoforms Of Myhc Expressed In Equine Laryngeal Musclesmentioning

confidence: 54%

Immunohistochemical Analysis of Laryngeal Muscles in Normal Horses and Horses With Subclinical Recurrent Laryngeal Neuropathy

Rhee

Steel

Derksen

et al. 2009

J Histochem Cytochem.

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Michigan (FJD,NER)S U M M A R Y We used immunohistochemistry to examine myosin heavy-chain (MyHC)-based fiber-type profiles of the right and left cricoarytenoideus dorsalis (CAD) and arytenoideus transversus (TrA) muscles of six horses without laryngoscopic evidence of recurrent laryngeal neuropathy (RLN). Results showed that CAD and TrA muscles have the same slow, 2a, and 2x fibers as equine limb muscles, but not the faster contracting fibers expressing extraocular and 2B MyHCs found in laryngeal muscles of small mammals. Muscles from three horses showed fiber-type grouping bilaterally in the TrA muscles, but only in the left CAD. Fiber-type grouping suggests that denervation and reinnervation of fibers had occurred, and that these horses had subclinical RLN. There was a virtual elimination of 2x fibers in these muscles, accompanied by a significant increase in the percentage of 2a and slow fibers, and hypertrophy of these fiber types. The results suggest that multiple pathophysiological mechanisms are at work in early RLN, including selective denervation and reinnervation of 2x muscle fibers, corruption of neural impulse traffic that regulates 2x and slow muscle fiber types, and compensatory hypertrophy of remaining fibers. We conclude that horses afflicted with mild RLN are able to remain subclinical by compensatory hypertrophy of surviving muscle fibers. (J Histochem Cytochem 57:787-800, 2009)

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Section: Isoforms Of Myhc Expressed In Equine Laryngeal Musclesmentioning

confidence: 54%

Immunohistochemical Analysis of Laryngeal Muscles in Normal Horses and Horses With Subclinical Recurrent Laryngeal Neuropathy

Rhee

Steel

Derksen

et al. 2009

J Histochem Cytochem.

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“…To be effective, the adductor needs to be faster relative to the abductor, which is active during inspiration. Thus, it is not surprising that the Ta-X was found to express the fastest fiber type profile among the laryngeal muscles in all species studied here, as well as in the rat (Rhee et al 2004) and in humans (Li et al 2004). This may represent an evolutionary adaptation to ensure that protective closure of the glottis is always faster than movements regulating airflow during respiration.…”

Section: Myhc Expression In the Thyroarytenoid And Its Functional Sigmentioning

confidence: 55%

“…These muscles have distinct developmental origins; the CT is derived from the fourth branchial arch, whereas the RLN-innervated muscles are from the sixth arch (Sperber 1989). However, as pointed out above, baboon (this study) and human (Li et al 2004) Ta and PCA muscles do not express EO or 2B MyHC, making them allotypically indistinguishable from the CT and limb muscles using MyHC expression as a criterion. An alternative hypothesis for the fact that the CT does not express EO and/or 2B isoforms in these species is simply that it is the slowest of the laryngeal muscles and consequently has the slowest MyHC profile relative to other laryngeal muscles and thus excludes these fast isoforms.…”

Section: Myhc Expression In the Ct And Its Functional Significancementioning

confidence: 59%

“…Lucas and J.F.Y. Hoh, unpublished data), and humans (PedrosaDomellof et al 2000;Li et al 2004). The secondary antibodies used were HRP-labeled goat anti-mouse IgM (Sigma; St. Louis, MO) for MAbs 6H1 and 10F5 and HRP-labeled rabbit anti-mouse immunoglobulin antibody (Dako Corp.; Carpinteria, CA) for the other MAbs.…”

Section: Ihcmentioning

confidence: 95%

“…These studies have shown considerable variations in MyHC expression in laryngeal muscle fibers between species, as well as in different laryngeal muscles within species. EO MyHC is expressed in the rabbit (Lucas et al 1995) and the rat (Rhee et al 2004) but not in the dog (Wu et al 2000c) or humans (Wu et al 2000b;Li et al 2004), whereas 2B MyHC is found in dog laryngeal muscles but not in humans. In rats, dogs, and humans, the profile of fiber types in the Ta is faster than that of the PCA, which is faster than that of the CT, reflecting differences in isometric contraction times of these muscles in rats and dogs (Hoh 2005), and suggests that similar relationships hold for the contraction times of these muscles in human.…”

mentioning

confidence: 99%

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

Rhee

Hoh

2008

J Histochem Cytochem.

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S U M M A R Y 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. (J Histochem Cytochem 56:929-950, 2008)

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Novel application of flow cytometry: Determination of muscle fiber types and protein levels in whole murine skeletal muscles and heart

Jackaman

Nowak

Ravenscroft

et al. 2007

Cell Motil. Cytoskeleton

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Conventional methods for measuring proteins within muscle samples such as immunohistochemistry and western blot analysis can be time consuming, labor intensive and subject to sampling errors. We have developed flow cytometry techniques to detect proteins in whole murine heart and skeletal muscle. Flow cytometry and immunohistochemistry were performed on quadriceps and soleus muscles from male C57BL/6J, BALB/c, CBA and mdx mice. Proteins including actins, myosins, tropomyosin and alpha-actinin were detected via single staining flow cytometric analysis. This correlated with immunohistochemistry using the same antibodies. Muscle fiber types could be determined by dual labeled flow cytometry for skeletal muscle actin and different myosins. This showed similar results to immunohistochemistry for I, IIA and IIB myosins. Flow cytometry of heart samples from C57BL/6J and BALB/c mice dual labeled with cardiac and skeletal muscle actin antibodies demonstrated the known increase in skeletal actin protein in BALB/c hearts. The membrane-associated proteins alpha-sarcoglycan and dystrophin could be detected in C57BL/6J mice, but were decreased or absent in mdx mice. With the ability to label whole muscle samples simultaneously with multiple antibodies, flow cytometry may have advantages over conventional methods for certain applications, including assessing the efficacy of potential therapies for muscle diseases.

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Differential Expression of Myosin Heavy Chain Isoforms between Abductor and Adductor Muscles in the Human Larynx

Cited by 48 publications

References 22 publications

Immunohistochemical Analysis of Laryngeal Muscles in Normal Horses and Horses With Subclinical Recurrent Laryngeal Neuropathy

Immunohistochemical Analysis of Laryngeal Muscles in Normal Horses and Horses With Subclinical Recurrent Laryngeal Neuropathy

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

Novel application of flow cytometry: Determination of muscle fiber types and protein levels in whole murine skeletal muscles and heart

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