Orthologous myosin isoforms and scaling of shortening velocity with body size in mouse, rat, rabbit and human muscles

Pellegrino, Maria Antonietta; Canepari, Monica; Rossi, R.; D’Antona, Giuseppe; Reggiani, Carlo; Bottinelli, Roberto

doi:10.1113/jphysiol.2002.027375

Cited by 194 publications

(287 citation statements)

References 54 publications

(86 reference statements)

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“…Hill (1950) predicted that shortening velocity should scale as an allometric function of the body mass, with small animals possessing faster, more powerful muscles. Toniolo et al (2004) showed the scaling relation between V o and body mass and they showed that pig slow fibres conform to the values expected from the scaling equation obtained with other animal species (Pellegrino et al 2003). The resulting values concerning fast fibres were higher in the pig than those obtained in human fibres and similar to those of rabbit fibres (Pellegrino et al 2003).…”

Section: Discussionsupporting

confidence: 66%

“…The values of P o and V o obtained for the muscle fibres can be compared with published data obtained in other animal species (Pellegrino et al 2003). We found that isometric tension of FOG fibres was not significantly different from that measured in corresponding fibres of other animal species; both slow fibres and fast twitch glycolytic fibres exhibit lower tension values.…”

Section: Discussionsupporting

confidence: 59%

“…Segments of 1-2 mm length were then cut from the fibres and light aluminium clips were applied at both ends. Skinning, relaxing, preactivating and activating solutions employed for mechanical experiments with single fibres were prepared as previously described (Pellegrino et al 2003). Protease inhibitors (E64 10 mol·l -1 and leupeptin 40 mol·l ) were added to all solutions.…”

Section: Single Fibre Mechanicsmentioning

confidence: 99%

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New Insights into Muscle Fibre Types in Casertana Pig

et al. 2010

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Little is known about the Casertana pig. The aim of this study was to evaluate the effect of sex on histochemical and morphometrical characteristics of muscle fibres (myocytes) in this pure breed and to verify the presence of giant fibres as well as vascularity of the muscle. Finally, maximum shortening velocity and isometric tension were measured in single muscle fibres.Sixteen Casertana pigs (8 males, 8 females) from a farm in Campania (Italy) were slaughtered at one year of age. Muscle tissues were obtained from psoas minor, rhomboideus and longissimus dorsi. Myofibres were stained for myosin adenosine triphosphatase, succinic dehydrogenase, and α-amylase-periodic acid schiff. For all fibre types, the area and perimeter were measured. Slowtwitch oxidative fibres, fast-twitch glycolytic fibres and fast-twitch oxidative-glycolytic fibres were histochemically differentiated; an image-analyzing system was used. The results showed significant differences between the sexes in the size of all three fibre types. The psoas minor muscle had a high percentage of slow-twitch oxidative fibres and contained more capillaries per fibre and per mm 2 than rhomboideus and longissimus dorsi, in which fast-twitch glycolytic fibres dominated. The cross-sectional area of all fibre types was larger in longissimus dorsi than in rhomboideus and psoas minor muscles; the giant fibres were present in the longissimus dorsi muscle only. Besides, isometric tension values were higher in fast-twitch glycolytic fibres than in the other ones. Variations in fibre type composition may contribute to meat quality. Giant fibres, myosin adenosine triphosphatase, succinic dehydrogenase, capillaries, shortening velocity, isometric tensionThe Casertana breed is an autochthonous pig breed of ancient origin, now threatened with extinction. In the past it was considered a very fine breed, raised in the Campania region and the surrounding area in South Italy. It was valued for its productive performance particularly regarding the fattening tendency. It is characterized by slow growth and massive accumulation of backfat; its coat is bright black and hairless. The purpose of this study was to complete the knowledge regarding the Casertana pig in order to valorise this breed and to study its meat quality characteristics. Porcine meat quality can be affected by variation in muscle fibre type composition (Depreux 2000). Muscle fibre types may be classified based on enzymatic activity; in this study the following nomenclature was used for myofibre types: FG (fast-contracting with glycolytic metabolism), FOG (fast contracting with glycolytic-oxidative metabolism) and SO (slow-contracting with oxidative metabolism). The aim of this study was to evaluate the effect of sex on the histochemical and morphometric characteristics of muscle fibres on the basis of myosin adenosine triphosphatase (myosin ATPase), succinic dehydrogenase (SDH), to analyse the contractile properties of pig muscle fibres and to determine the presence of giant fibres in the muscles consi...

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Section: Discussionsupporting

confidence: 66%

Section: Discussionsupporting

confidence: 59%

Section: Single Fibre Mechanicsmentioning

confidence: 99%

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New Insights into Muscle Fibre Types in Casertana Pig

et al. 2010

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“…The amino acid sequence for MHC-1 of mammals is ϳ80% identical to MHC-2 within the motor domain and for a discussion of the structural and functional differences between MHC-1 and MHC-2 see Ref. 41. The myosin light chains also differ between fast and slow muscle myosins but are generally regarded as having a modulatory role on the properties of the MHC (42).…”

Section: Discussionmentioning

confidence: 99%

The Slow Skeletal Muscle Isoform of Myosin Shows Kinetic Features Common to Smooth and Non-muscle Myosins

Iorga

Adamek

Geeves

2007

Journal of Biological Chemistry

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Fast and slow mammalian muscle myosins differ in the heavy chain sequences (MHC-2, MHC-1) and muscles expressing the two isoforms contract at markedly different velocities. One role of slow skeletal muscles is to maintain posture with low ATP turnover, and MHC-1 expressed in these muscles is identical to heavy chain of the ␤-myosin of cardiac muscle. Few studies have addressed the biochemical kinetic properties of the slow MHC-1 isoform. We report here a detailed analysis of the MHC-1 isoform of the rabbit compared with MHC-2 and focus on the mechanism of ADP release. We show that MHC-1, like some non-muscle myosins, shows a biphasic dissociation of actin-myosin by ATP. Most of the actinmyosin dissociates at up to ϳ1000 s ؊1, a very similar rate constant to MHC-2, but 10 -15% of the complex must go through a slow isomerization (ϳ20 s ؊1 ) before ATP can dissociate it. Similar slow isomerizations were seen in the displacement of ADP from actinmyosin⅐ADP and provide evidence of three closely related actinmyosin⅐ADP complexes, a complex in rapid equilibrium with free ADP, a complex from which ADP is released at the rate required to define the maximum shortening velocity of slow muscle fibers (ϳ20 s ؊1 ), and a third complex that releases ADP too slowly (ϳ6 s ؊1 ) to be on the main ATPase pathway. The role of these actin-myosin⅐ADP complexes in the mechanochemistry of slow muscle contraction is discussed in relation to the load dependence of ADP release.Myosins comprise a family of ATP-dependent motor proteins and are best known for their role in muscle contraction and their involvement in a wide range of other eukaryotic motility processes (1-6). During the myosin ATPase cycle, the myosin motor domain (or cross-bridge) undergoes a series of conformational changes coupled to the binding of nucleotide and actin, which results in a translocation of the myosin cargo domain relative to the actin track (7). The sequence of molecular events in the actin-myosin cross-bridge cycle appears essentially the same for all myosins so far studied. The different mechanochemical properties of each myosin are attributed to a modulation of the rates and equilibrium constants of individual molecular events to match each myosin to its physiological role.The most widely studied myosins are the vertebrate, striatedmuscle myosins, which define the class II myosins. This class of myosins have a dimerization domain that forms a long coiled-coil and which can assemble further to form the backbone of the bipolar thick myosin filament. Of the class II myosin, the myosin heavy chain 2 (MHC-2) 4 isoform found primarily in white, anaerobic, fast-contracting, skeletal muscle has been most thoroughly described at both the molecular and physiological levels. In adult, mammalian, muscle tissue the MHC-2 is found as various isoforms (e.g. 2a, 2b, 2x) and it has been established that the essential mechanical properties of the muscle fiber contraction (e.g. maximum velocity of shortening, force per cross-bridge) are properties of the MHC present in the t...

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“…In the region of MHC isoforms, four bands were separated that corresponded, in order of migration from the fastest to the slowest, to MHC-1 (or slow), MHC-2B, MHC-2X and MHC-2A (or fast). Densitometric analysis of these isoforms were performed to establish the relative proportion of the MHC isoforms identified in the sample [38].…”

Section: Analysis Of Mhc Isoforms Contentmentioning

confidence: 99%

Statin or fibrate chronic treatment modifies the proteomic profile of rat skeletal muscle

Camerino

Pellegrino

Brocca

et al. 2011

Biochemical Pharmacology

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Statins and fibrates can cause myopathy. To further understand the causes of the damage we performed a proteome analysis in fast-twitch skeletal muscle of rats chronically treated with different hypolipidemic drugs. The proteomic maps were obtained from extensor digitorum longus (EDL) muscles of rats treated for 2-months with 10mg/kg atorvastatin, 20mg/kg fluvastatin, 60mg/kg fenofibrate and control rats. The proteins differentially expressed were identified by mass spectrometry and further analysed by immunoblot analysis. We found a significant modification in 40 out of 417 total spots analysed in atorvastatin treated rats, 15 out of 436 total spots in fluvastatin treated rats and 21 out of 439 total spots in fenofibrate treated rats in comparison to controls. All treatments induced a general tendency to a down-regulation of protein expression; in particular, atorvastatin affected the protein pattern more extensively with respect to the other treatments.Energy production systems, both oxidative and glycolytic enzymes and creatine kinase, were downregulated following atorvastatin administration, whereas fenofibrate determined mostly alterations in glycolytic enzymes and creatine kinase, oxidative enzymes being relatively spared. Additionally, all treatments resulted in some modifications of proteins involved in cellular defenses against oxidative stress, such as heat shock proteins, and of myofibrillar proteins. These results were confirmed by immunoblot analysis. In conclusions, the proteomic analysis showed that either statin or fibrate administration can modify the expression of proteins essential for skeletal muscle function suggesting potential mechanisms for statin myopathy.

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Orthologous myosin isoforms and scaling of shortening velocity with body size in mouse, rat, rabbit and human muscles

Cited by 194 publications

References 54 publications

New Insights into Muscle Fibre Types in Casertana Pig

New Insights into Muscle Fibre Types in Casertana Pig

The Slow Skeletal Muscle Isoform of Myosin Shows Kinetic Features Common to Smooth and Non-muscle Myosins

Statin or fibrate chronic treatment modifies the proteomic profile of rat skeletal muscle

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