Differential Expression of Equine Myosin Heavy-chain mRNA and Protein Isoforms in a Limb Muscle

Eizema, Karin; Burg, Maarten van den; Kiri, Arpna; Dingboom, Elizabeth G.; Oudheusden, H. van; Goldspink, Geoffrey; Weijs, W.A.

doi:10.1177/002215540305100911

Cited by 41 publications

(45 citation statements)

References 52 publications

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“…First, muscle fibers are isotyped by the myosin isoform they express, but quantification of MyHC mRNA demonstrated that transcripts for several isoforms are present in a fiber, and that both isoform mRNA and protein levels can vary longitudinally along a single fiber (34). While these isoforms may be undetectable at the resolution of SDS-PAGE, it is possible that a small percentage of another isoform may influence biochemical and biophysical experiments (35)(36)(37). The second caveat associated with whole fiber analysis is the number of variables that may exist among fibers beyond myosin isoform expression.…”

mentioning

confidence: 99%

Functional diversity among a family of human skeletal muscle myosin motors

Resnicow

Deacon

Warrick

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

100

130

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Human skeletal muscle fibers express five highly conserved type-II myosin heavy chain (MyHC) genes in distinct spatial and temporal patterns. In addition, the human genome contains an intact sixth gene, MyHC-IIb, which is thought under most circumstances not to be expressed. The physiological and biochemical properties of individual muscle fibers correlate with the predominantly expressed MyHC isoform, but a functional analysis of homogenous skeletal muscle myosin isoforms has not been possible. This is due to the difficulties of separating the multiple isoforms usually coexpressed in muscle fibers, as well as the lack of an expression system that produces active recombinant type II skeletal muscle myosin. In this study we describe a mammalian muscle cell expression system and the functional analysis of all six recombinant human type II skeletal muscle myosin isoforms. The diverse biochemical activities and actin-filament velocities of these myosins indicate that they likely have distinct functions in muscle. Our data also show that ATPase activity and motility are generally correlated for human skeletal muscle myosins. The exception, MyHC-IIb, encodes a protein that is high in ATPase activity but slow in motility; this is the first functional analysis of the protein from this gene. In addition, the developmental isoforms, hypothesized to have low ATPase activity, were indistinguishable from adult-fast MyHC-IIa and the specialized MyHC-Extraocular isoform, that was predicted to be the fastest of all six isoforms but was functionally similar to the slower isoforms.

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mentioning

confidence: 99%

Functional diversity among a family of human skeletal muscle myosin motors

Resnicow

Deacon

Warrick

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

100

130

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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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“…Three fast MHC isoforms have been demonstrated in large mammals, such as domestic pigs and llamas [Lefaucheur et al, 1998;Graziotti et al, 2001]. On the contrary, only two fast MHC isoforms (MHC-IIa and -IIx) are expressed in skeletal muscles of humans [Smerdu et al, 1994;Ennion et al, 1995] and several domestic animal species, like cats , cattle [Tanabe et al, 1998], goats [Argüello et al, 2001] and horses [Rivero et al, 1996;Eizema et al, 2003].…”

Section: Introductionmentioning

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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Differential Expression of Equine Myosin Heavy-chain mRNA and Protein Isoforms in a Limb Muscle

Cited by 41 publications

References 52 publications

Functional diversity among a family of human skeletal muscle myosin motors

Functional diversity among a family of human skeletal muscle myosin motors

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

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

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