Pattern of Myosin Heavy Chain Isoforms in Different Fibre Types of Canine Trunk and Limb Skeletal Muscles

Štrbenc, Malan; Smerdu,; Zupanc, Marianne M.; Tozon, Nataša; Fazarinc, Gregor

doi:10.1159/000077034

Cited by 20 publications

(38 citation statements)

References 68 publications

(47 reference statements)

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“…However, in the muscles that contained only a weak MHC-IIx band ( fi g. 1 e), no type IIX fi bres could be demonstrated immunohistochemically. Since BF-35 recognizes MHC-IIa, only pure IIX and hybrid IIAX fi bres with the predominant MHC-IIx isoform can be demonstrated with this antibody [Smerdu and Eržen, 2001;Štrbenc et al, 2004]. It implies that in these muscles, the MHC-IIx isoform was obviously co-expressed with MHC-IIa in type IIA fi bres (or more precisely type IIAX fi bres), but its content was too low to be detected by BF-35.…”

Section: Discussionmentioning

confidence: 99%

Identification of Myosin Heavy Chain I, IIa and IIx in Canine Skeletal Muscles by an Electrophoretic and Immunoblotting Study

Smerdu¹,

Štrbenc

Meznarič³

et al. 2005

Cells Tissues Organs

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To determine which myosin heavy chain (MHC) isoforms are expressed in canine skeletal muscles, different muscle samples of five mixed-breed dogs were analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The separated MHC isoforms were identified by immunoblotting technique using a set of specific monoclonal antibodies. To compare the results of the electrophoretic and immunoblotting study, the pattern of MHC isoform expression and histochemical profiles of canine fibres were additionally demonstrated on serial muscle sections by immunohistochemistry and myofibrillar adenosine triphosphatase (mATPase) histochemistry. Not more than three MHC isoforms were demonstrated by SDS-PAGE in the analysed canine muscles. By the immunoblotting technique, the fastest migrating MHC band was identified as slow or MHC-I, the intermediate one as MHC-IIx and the slowest migrating band as MHC-IIa isoform. Since none of the three MHC bands and none of the analysed fibres were recognized by the antibody specific to MHC-IIb of rats, we concluded that MHC-IIb is not expressed in large skeletal muscles of dogs. Similarly, only three major fibre types, i.e. I, IIA and IIX, were revealed according to the pattern of MHC immunohistochemistry and mATPase reaction. Type IIA fibres were more alkali- and acid-stable than type IIX fibres after mATPase histochemistry; hence, the latter corresponded to type IIDog fibres. However, beside the three major fibre types, scarce hybrid fibres co-expressing two MHC isoforms (I/IIA and IIA/IIX) were demonstrated by immunohistochemistry.

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Section: Discussionmentioning

confidence: 99%

Identification of Myosin Heavy Chain I, IIa and IIx in Canine Skeletal Muscles by an Electrophoretic and Immunoblotting Study

Smerdu¹,

Štrbenc

Meznarič³

et al. 2005

Cells Tissues Organs

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“…Type IIX fibers are histochemically very similar to Type IIB fibers and MHC IIx has been shown to be expressed in fibers histochemically identified as Type IIB, but both types differ in their contractile properties (Pette et al, 1999;Smerdu et al, 2009). In contrast to small mammals, results on larger species have shown that only MHC IIa and IIx were expressed but not MHC IIb (e.g., cat: Talmadge et al, 1996;dog: Snow et al, 1982;Š trbenc et al, 2004;goat: Argü ello et al, 2001;sheep: Maier et al, 1992;human: Smerdu et al, 1994;Ennion et al, 1995;horse: Rivero et al, 1996;Eizema et al, 2003;cattle: Tanabe et al, 1998;brown bear: Smerdu et al, 2009). However, Type IIB and IIX fibers are not distinguishable with the Ziegan protocol used in this study.…”

Section: Histochemistrymentioning

confidence: 99%

Distribution Pattern of Muscle Fiber Types in the Perivertebral Musculature of Two Different Sized Species of Mice

Hesse

Fischer

Schilling

2010

The Anatomical Record

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Many physiological parameters scale with body size. Regarding limb muscles, it has been shown that the demands for relatively faster muscles, less postural work, and greater heat production in small mammals are met by lower proportions of Type I and conversely higher proportions of Type II fibers. To investigate possible adaptations of the perivertebral musculature, we investigated the proportion, spatial distribution, and cross-sectional area (csa) of the different muscle fiber types in the laboratory and harvest mouse. Serial cross sections from the posterior thoracic to the lumbo-sacral region were prepared and Type I, IIA, and IIB fibers identified using enzymehistochemistry. The general distribution of Type I and IIB fibers, as well as the more or less equal distribution of IIA fibers, resembles the pattern found in other mammals. However, the overall proportion of Type I fibers was very low in the laboratory mouse and particularly low in the harvest mouse. Muscular adaptations to a small body size were met primarily by increased Type IIA fiber proportions. Thereby, not all muscles or muscle regions similarly reflected the expected scaling effects. However, our results clearly show that body size is a critical factor when fiber-type proportions are compared among different sized mammals. Anat Rec, 293:446-463, 2010. V V C 2010 Wiley-Liss, Inc.

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“…muscles from adult animals and muscles that have not been subjected to 'transforming conditions', such as changes in the neural impulse pattern or hormone levels [Stephenson, 2001]. For instance, it was found that hybrid fibers were common among fast fibers expressing MyHC-IIX [Strbenc et al, 2004]. Muscle fibers have a length of a few millimeters to several centimeters.…”

Section: Introductionmentioning

confidence: 99%

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

Korfage¹,

Kwee²,

Everts³

et al. 2016

Cells Tissues Organs

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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.

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Pattern of Myosin Heavy Chain Isoforms in Different Fibre Types of Canine Trunk and Limb Skeletal Muscles

Cited by 20 publications

References 68 publications

Identification of Myosin Heavy Chain I, IIa and IIx in Canine Skeletal Muscles by an Electrophoretic and Immunoblotting Study

Identification of Myosin Heavy Chain I, IIa and IIx in Canine Skeletal Muscles by an Electrophoretic and Immunoblotting Study

Distribution Pattern of Muscle Fiber Types in the Perivertebral Musculature of Two Different Sized Species of Mice

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

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