Enzyme activity patterns of myosin ATPase, α-glycerophosphate dehydrogenase and succinate dehydrogenase within different muscle fibre types

Wank, Veit; Bauer, Reinhard; Punkt, Karla; Ziegan, J

doi:10.1016/s0065-1281(11)80181-9

Cited by 12 publications

(6 citation statements)

References 12 publications

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“…4) and therefore higher mitochondrial densities. This is in agreement with a previous study using the rat tibialis anterior muscle [78]. Type IIB fibers in the deep regions of the plantaris, extensor digitorum longus, and tibialis anterior muscles have lower oxidative enzyme activities than type I and type IIA fibers in the respective muscle regions.…”

Section: Fiber Type and Oxidative Enzyme Activity In Hindllimb Mussupporting

confidence: 93%

Cell Size and Oxidative Enzyme Activity of Type-Identified Fibers in Rat Hindlimb Muscles: a Review

Nakatani

Nakashima

Kita

et al. 2003

Acta Histochem. Cytochem

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Mammalian skeletal muscles are comprised of heterogeneous types of fibers based on their enzyme histochemical or immunohistochemical properties. Regardless of the muscle type, muscle region, or fiber type, an inverse relationship between cross-sectional area and oxidative enzyme activity of fibers is observed in the rat hindlimb muscles including the soleus, plantaris, extensor digitorum longus, and tibialis anterior muscles. This indicates that smallersized fibers have higher oxidative enzyme activities than larger-sized fibers even within the same fiber type. In addition, there is a matching of cell sizes and oxidative enzyme activities of spinal motoneurons and the muscle fibers that they innervate, which is important for maintaining their functional and metabolic properties.

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Section: Fiber Type and Oxidative Enzyme Activity In Hindllimb Mussupporting

confidence: 93%

Cell Size and Oxidative Enzyme Activity of Type-Identified Fibers in Rat Hindlimb Muscles: a Review

Nakatani

Nakashima

Kita

et al. 2003

Acta Histochem. Cytochem

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“…This result contrasts with previous studies [11][12][13] where large variations in SDH activity were observed in fibers within the same fiber types in the tibialis anterior muscle of mice and rats, but it is in agreement with another study using the tibialis anterior muscle of rats [14] although that study [14] did not examine the enzyme activity of fibers in different muscle regions.…”

Section: Discussionsupporting

confidence: 56%

Cell Size and Oxidative Enzyme Activity of Different Types of Fibers in Different Regions of the Rat Plantaris and Tibialis Anterior Muscles.

Nakatani

Nakashima²,

Kita³

et al. 2000

JJP

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Skeletal muscle fibers are classified into slow-twitch type I and fast-twitch type IIA and type IIB according to their myosin-based enzyme histochemical profiles [1,2]. Previous studies [3,4] have reported relationships among fiber types, and morphological (cell size) and metabolic (oxidative and glycolytic enzyme activities) features in the muscle. Muscle fibers have wide variations in their cell sizes [5], and large muscles (i.e., the gastrocnemius, tibialis anterior, and vastus lateralis muscles) show an increasing gradient of fibers having a small cell size proceeding from the superficial to deep region [6,7]. Therefore, it would be expected that smaller-sized fibers have higher oxidative enzyme activity than larger-sized fibers in the muscle even within the same fiber type because supplies of oxygen and substrates for oxidative energy metabolism from capillaries which are located close to the membrane are more plentiful in smaller-sized fibers. In the present study, we examined the cell size and oxidative enzyme activity of different types of fibers in different regions of the fast plantaris and tibialis anterior muscles in rats. MATERIALS AND METHODSExperimental animals. Five ten-week-old Wistar male rats (body weight, 293-322 g) were used in the present study. All experiments were approved by the Institutional Animal Care Committee at the university and conducted under the Guide for the Care and Use of Laboratory Animals published by the Office of Science and Health Reports of the USA National Institutes of Health, Bethesda, Maryland, USA.Tissue processing. The right plantaris and tibialis anterior muscles were removed under sodium pentobarbital anesthesia (50 mg/kg body weight, i.p.). Japanese Journal of Physiology Vol. 50, No. 4, 2000 413Japanese Journal of Physiology, 50, 413-418, 2000 Key words: cross-sectional area, muscle fiber, plantaris muscle, succinate dehydrogenase activity, tibialis anterior muscle. Abstract:The cross-sectional areas and succinate dehydrogenase activities of different types of fibers in different regions of the plantaris and tibialis anterior muscles in 10-week-old male rats were determined using quantitative histochemistry. The muscle fibers were classified as type I, type IIA, or type IIB according to their adenosine triphosphatase activities. There were no regional differences in either the mean cross-sectional area or the mean succinate dehydrogenase activity of type IIA fibers in both muscles. In contrast, type IIB fibers in the deep region of both muscles had smaller cross-sectional areas and higher succinate dehydrogenase activities than those in the superficial and middle regions. These data suggest the presence of regional differences in the cross-sectional area and succinate dehydrogenase activity of type IIB fibers in the muscle.

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“…In contrast, myofibers in skeletal muscles can be classified as MHC-1, MHC-2A, MHC-2X/2D, and MHC-2B based on differences in myosin heavy chain (MHC) isoforms using methods such as electrophoresis and immunohistological staining 28 , 29 ) and as types I, IIA, IIB, and IID (X), depending on the difference in myosin ATPase activity, using the myosin ATPase staining method 30 , 31 , 32 , 33 ) . Moreover, succinate dehydrogenase staining and nicotinamide tetrazolium reductase staining are known to classify myofibers as types I and II 34 , 35 ) . These identification methods are based on differences in MHC isoforms or mitochondrial enzyme activity, and no other method that identifies the type of myofibers has previously been established.…”

Section: Discussionmentioning

confidence: 99%

Alteration of cathepsin-D expression in atrophied muscles and apoptotic myofibers by hindlimb unloading in a low-temperature environment

Nagano

2015

J Phys Ther Sci

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[Purpose] The purpose of this study was to elucidate the cathepsin-D involvement in signaling pathways for the survival and apoptosis of myofibers in rats with hindlimb-unloading in a low-temperature environment. [Subjects and Methods] Wistar rats were divided into two groups: a control group and a group that underwent hindlimb unloading in a low-temperature environment to induce muscle apoptosis. Cathepsin-D localization in the soleus and extensor digitorum longus muscles, along with the expression of cathepsin-D in apoptotic myofibers, was examined. Expression of the active and inactive forms of cathepsin-D was also analyzed. [Results] Cathepsin-D was mainly expressed in type I myofibers and was observed to have punctate patterns in the control group. In the hindlimb unloading in a low-temperature environment group, the type I myofiber composition ratio decreased, and caspase-3 activation and TUNEL-positive apoptotic myofibers were observed. In caspase-3-activated myofibers, cathepsin-D overexpression and leakage of it into the cytoplasm were observed. In the hindlimb unloading in a low-temperature environment group, the amount of inactive cathepsin-D decreased, whereas that of the active form increased. [Conclusion] Cathepsin-D was deduced to be indicative of a myofiber-type classification and a factor related to myofiber type maintenance. In addition, cathepsin-D leakage into the cytoplasm was appeared to be involved in caspase-3 activation in the hindlimb unloading in a low-temperature environment group.

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Enzyme activity patterns of myosin ATPase, α-glycerophosphate dehydrogenase and succinate dehydrogenase within different muscle fibre types

Cited by 12 publications

References 12 publications

Cell Size and Oxidative Enzyme Activity of Type-Identified Fibers in Rat Hindlimb Muscles: a Review

Cell Size and Oxidative Enzyme Activity of Type-Identified Fibers in Rat Hindlimb Muscles: a Review

Cell Size and Oxidative Enzyme Activity of Different Types of Fibers in Different Regions of the Rat Plantaris and Tibialis Anterior Muscles.

Alteration of cathepsin-D expression in atrophied muscles and apoptotic myofibers by hindlimb unloading in a low-temperature environment

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