Enzyme histochemistry of the mesocoxal muscles of Periplaneta americana

Stokes, Darrell R.; Vitale, Anthony J.; Morgan, C. R.

doi:10.1007/bf00234844

Cited by 110 publications

(17 citation statements)

References 41 publications

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“…Their smaller counterparts, d and e, insert more proximally on opposite sides of the apodeme. Histochemical analysis of muscle 135d (the mesothoracic homolog of 177d) has revealed two distinct fiber bundles (Stokes, Vitale, and Morgan, 1979). Upon careful visual examination of 177d we have also found two distinct fiber bundles.…”

Section: Anatomymentioning

confidence: 97%

Mechanical properties of a slow muscle in the cockroach

Chesler

Fourtner

1981

J. Neurobiol.

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The mechanical properties of the metacoxal muscle, 177d, in the cockroach, Periplaneta americana, was investigated. The muscle exhibited a mean resting tension of 2.6 +/- 1.3g SD. Neurally evoked tension summed with the resting tension and the relaxation phase of the evoked tension varied from less than 1 s to several minutes. This residual tension varied not only in duration but also in amplitude. Stimulation of inhibitory axons increased the rate of relaxation and thereby abolished the residual tension. However, inhibitory stimulation never reduced the resting tension. Stimulation of the main leg nerve at several times the threshold of the inhibitory axons could evoke residual tension. Recording of synaptic potentials from the two histochemically different fiber types (dorsal and ventral groups) revealed large hyperpolarizations in the ventral fibers and decreased duration and amplitude of excitatory potentials in the dorsal fibers. These results suggest that there are a variety of ways in which tension can be evoked, maintained, and controlled in these muscles.

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Section: Anatomymentioning

confidence: 97%

Mechanical properties of a slow muscle in the cockroach

Chesler

Fourtner

1981

J. Neurobiol.

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“…Myosin is so highly conserved in the animal kingdom that more or less comparable physiologic fiber types have been found in the muscles of animals as diverse as cockroaches (Stokes et al, 1979), lizards (Gleeson et al, 1980), and galagos (Sickles and Pinkstaff, 1981). Since the earliest work relating muscle histology of red and white myofibers (Ranvier, 1874) to physiologic function (Denny-Brown, 1929), new myosin species have been discovered, not only by using immunocytochemical and molecular techniques, but also by preincubating the tissue in a range of pH values while employing the standard enzyme histochemistry protocol (Brooke and Kaiser, 1970).…”

Section: Morphological Indicators Of Muscle Physiologymentioning

confidence: 99%

Ontogeny of histochemical fiber types and muscle function in the masseter muscle of miniature swine

Anapol

Herring

2000

Am. J. Phys. Anthropol.

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In this study of masticatory maturation, the ontogeny of the histochemical fiber type composition of musculus masseter is examined in the omnivorous miniature swine (Sus scrofa). Fiber type characteristics are interpreted by comparison with electromyography (EMG) recorded during feeding behavior. Similar to locomotion studies, the results suggest a correspondence between the composition and arrangement of motor units and their recruitment pattern. Serial sections of masseter muscles from 10 minipigs, ranging from 2 weeks to slightly over 1 year of age, were stained for myosin adenosine triphosphatase (mATPase) activity to distinguish slow-twitch from fast-twitch fibers, and for nicotinamide adenosine dehydrogenase-tetrazolium reductase to assess the aerobic capacity of the same fibers. Although maintaining a uniformly high aerobic capacity throughout ontogeny and in adult animals, a transition is observed in the relative proportions of fast- and slow-twitch fibers. The primarily fast-twitch neonatal pig masseter eventually comprises approximately 25-30% slow-twitch fibers in adults, with a higher predominance of slow fibers in the deep (vs. superficial) and anterior (vs. posterior) regions of the muscle. Furthermore, while individual fibers of adult masseters generally stain for either alkaline- or acid-stable mATPase activity, a substantial proportion of cells in developing animals exhibits the presence of both isozymes. EMG results indicate functional heterogeneity within the masseter of adult pigs. During chewing, when pig chow is replaced by cracked corn, EMG activity in the deep portion of the muscle either decreases or increases slightly. In the superficial portion, however, muscle amplitudes become dramatically higher for corn, surpassing levels generated for chewing the less obdurate chow. These results are consistent with a behavioral transition from neonatal suckling to sustained mastication of foods of more complex textures eaten by adult pigs. The relationship between these fiber type and EMG results for pig masseter corresponds to those pertaining to motor unit recruitment in the extensor muscles of locomotion. Implications of this work for the evolutionary morphology of mastication also are discussed.

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“…As a group, the extensors of the hindlimb produce power to extend the leg and accelerate the center of mass forward during running (Full et al, 1991). Homologues of both muscles are ultrastructurally similar and histochemically classified as fast-twitch muscles in a related species, the American cockroach Periplaneta americana (Stokes et al, 1979;Morgan et al, 1980;Stokes, 1987). For this study, we begin by testing the null hypothesis that muscles 178 and 179 function similarly under in vivo conditions.…”

Section: Introductionmentioning

confidence: 99%

In situmuscle power differs without varyingin vitromechanical properties in two insect leg muscles innervated by the same motor neuron

Ahn

Meijer

2006

Journal of Experimental Biology

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The mechanical behavior of muscle during locomotion is often predicted by its anatomy, kinematics, activation pattern and contractile properties. The neuromuscular design of the cockroach leg provides a model system to examine these assumptions, because a single motor neuron innervates two extensor muscles operating at a single joint. Comparisons of the in situ measurements under in vivo running conditions of muscle 178 to a previously examined muscle (179) demonstrate that the same inputs (e.g. neural signal and kinematics) can result in different mechanical outputs. The same neural signal and kinematics, as determined during running, can result in different mechanical functions, even when the two anatomically similar muscles possess the same contraction kinetics, force-velocity properties and tetanic force-length properties. Although active shortening greatly depressed force under in vivo-like strain and stimulation conditions, force depression was similarly proportional to strain, similarly inversely proportional to stimulation level, and similarly independent of initial length and shortening velocity between the two muscles. Lastly, passive prestretch enhanced force similarly between the two muscles. The forces generated by the two muscles when stimulated with their in vivo pattern at lengths equal to or shorter than rest length differed, however. Overall, differences between the two muscles in their submaximal force-length relationships can account for up to 75% of the difference between the two muscles in peak force generated at short lengths observed during oscillatory contractions. Despite the fact that these muscles act at the same joint, are stimulated by the same motor neuron with an identical pattern, and possess many of the same in vitro mechanical properties, the mechanical outputs of two leg extensor muscles can be vastly different.

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Enzyme histochemistry of the mesocoxal muscles of Periplaneta americana

Cited by 110 publications

References 41 publications

Mechanical properties of a slow muscle in the cockroach

Mechanical properties of a slow muscle in the cockroach

Ontogeny of histochemical fiber types and muscle function in the masseter muscle of miniature swine

In situmuscle power differs without varyingin vitromechanical properties in two insect leg muscles innervated by the same motor neuron

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