Hind foot drumming: Myosin heavy chain muscle fibre distribution in the hind limb muscles of three African mole‐rat species (Bathyergidae)

2021 ◽  
Author(s):  
L. Sahd ◽  
N. Doubell ◽  
N.C. Bennett ◽  
S.H. Kotzé
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fibre ◽  
Heavy Chain ◽  
Hind Limb ◽  
Fibre Distribution ◽  
Mole Rat ◽  
Limb Muscles ◽  
Hind Foot

scholarly journals Four novel myosin heavy chain transcripts define a molecular basis for muscle fibre types inRanapipiens

1998 ◽  
Vol 508 (3) ◽  
pp. 667-680 ◽  
Author(s):  
Gordon J. Lutz ◽  
Denise B. Cuizon ◽  
Allen F. Ryan ◽  
Richard L. Lieber
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fibre ◽  
Heavy Chain ◽  
Molecular Basis ◽  
Fibre Types ◽  
Muscle Fibre Types

Abstract 19086: Myofilament Proteins of the Naked Mole-rat Heart Reflect Low Basal Species Cardiac Function

Circulation ◽  
2014 ◽  
Vol 130 (suppl_2) ◽  
Author(s):  
Kelly M Grimes ◽  
David Barefield ◽  
Mohit Kumar ◽  
Pieter P de Tombe ◽  
Sakthivel Sadayappan ◽  
...  
Keyword(s):  
Cardiac Function ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Troponin I ◽  
Myocardial Contraction ◽  
Myosin Heavy Chain Isoform ◽  
Mole Rat ◽  
Naked Mole Rat ◽  
And Function

The naked mole-rat (NMR) is a mouse-sized rodent with a maximum longevity of >31 years. The species exhibits low basal heart rate (256 bpm) and cardiac output (7 ml/min) for its body size, as well as low fractional shortening (28%) for a rodent. However unlike other well-studied mammals, the NMR maintains cardiac reserve and diastolic function for at least 75% of its maximum lifespan - at ages equivalent to 90 year old humans. We questioned if this low basal cardiac function was due to NMR myofilament composition and function. NMR ventricles are comprised primarily of the β-myosin heavy chain isoform, which is associated with slowed myocardial contraction and increased efficiency. This is in stark contrast to mouse ventricles, which express predominately the α-isoform, and switch to the β-isoform upon experimental induction of heart failure. Compared to mice, NMR myofilament proteins such as cardiac troponin I and cardiac myosin binding protein-C display lower levels of phosphorylation. Such levels are indicative of decreased activation of myofilament proteins and may relate to the species’ low basal cardiac function. Both the NMR’s predominance of β-myosin heavy chain and the low basal level of myofilament phosphorylation present a phenotype much closer to that seen in human ventricles than in those of mice. Intriguingly, maximal force developed by skinned NMR cardiomyocytes is not significantly different to that of mouse cardiomyocytes (NMR: 70.9 ± 9.3mN/mm2 vs. mouse: 87.7 ± 0.6 mN/mm2). This is likely a reflection of the NMR’s ability to enhance cardiac function to the level of a mouse when stimulated, as is evident when both species are treated in vivo with dobutamine (3 μg/g i.p.). Such low basal cardiac function may put less overall strain on the heart over time and could be critical to the NMR’s ability to maintain cardiac function with age.

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.

scholarly journals Hind foot drumming: morphological adaptations of the muscles and bones of the hind limb in three African mole‐rat species

2019 ◽  
Vol 235 (4) ◽  
pp. 811-824 ◽  
Author(s):  
L. Sahd ◽  
N. C. Bennett ◽  
S. H. Kotzé
Keyword(s):  
Hind Limb ◽  
Morphological Adaptations ◽  
Mole Rat ◽  
Hind Foot

Effects of 84-days of bedrest and resistance training on single muscle fibre myosin heavy chain distribution in human vastus lateralis and soleus muscles

2005 ◽  
Vol 185 (1) ◽  
pp. 61-69 ◽  
Author(s):  
P. Gallagher ◽  
S. Trappe ◽  
M. Harber ◽  
A. Creer ◽  
S. Mazzetti ◽  
...  
Keyword(s):  
Resistance Training ◽  
Myosin Heavy Chain ◽  
Muscle Fibre ◽  
Heavy Chain ◽  
Vastus Lateralis ◽  
Single Muscle Fibre ◽  
Single Muscle

Calcineurin differentially regulates fast myosin heavy chain genes in oxidative muscle fibre type conversion

2007 ◽  
Vol 329 (3) ◽  
pp. 515-527 ◽  
Author(s):  
Nuno da Costa ◽  
Julia Edgar ◽  
Peck-Toung Ooi ◽  
Yuhong Su ◽  
Joachim D. Meissner ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fibre ◽  
Heavy Chain ◽  
Fibre Type ◽  
Muscle Fibre Type ◽  
Type Conversion ◽  
Fast Myosin ◽  
Fast Myosin Heavy Chain ◽  
Myosin Heavy Chain Genes

Skeletal muscle fibre type regulation: both MEK1/2 and calcineurin blockade change expression of myosin heavy chain isoforms

2002 ◽  
Vol 30 (1) ◽  
pp. A33-A33
Author(s):  
J. Higginson ◽  
H. Wackerhage ◽  
N. Woods ◽  
P. Schjerling ◽  
A. Ratkevicius ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Muscle Fibre ◽  
Heavy Chain ◽  
Fibre Type ◽  
Skeletal Muscle Fibre ◽  
Myosin Heavy Chain Isoforms ◽  
Muscle Fibre Type

The effect of reinnervation on the distribution of muscle fibre types in the tibialis anterior muscle of the mouse

1990 ◽  
Vol 68 (5) ◽  
pp. 596-602 ◽  
Author(s):  
David J. Parry ◽  
Ross S. Wilkinson
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fibre ◽  
Heavy Chain ◽  
Tibialis Anterior ◽  
Tibialis Anterior Muscle ◽  
Myosin Heavy Chain Isoforms ◽  
Fibre Types ◽  
Muscle Fibre Types ◽  
Muscle Fibres ◽  
Superficial Portion

The distribution of fibre types in the tibialis anterior (TA) muscle of adult mice was examined by means of an immuno-histochemical approach, using monoclonal antibodies that recognize different myosin heavy chain isoforms. As has been reported previously, the superficial portion of TA contains almost exclusively type IIB fibres and is almost entirely glycolytic in nature. Following section of the lateral popliteal nerve and rotation of the proximal stomp to prevent rematching, it was found that the original pattern was virtually restored within 2 months. One possible explanation for this observation is that the activity pattern of peripheral and deep muscle fibres differs and that this aids in specification of muscle fibre type. Alternatively, the muscle fibres of the superficial portion of TA may be inherently resistant to an alteration of their phenotype with regard to expression of myosin heavy chain.Key words: myosin heavy chain, immunohistochemistry, plasticity, self-reinnervation, fibre types.

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