The value of enzyme histochemical techniques in the classification of fibre types of human skeletal muscle

Meijer, A. E. F. H.; Elias, E. A.; Vloedman, A. H. T.

doi:10.1007/bf00498485

Cited by 27 publications

(6 citation statements)

References 13 publications

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“…Since glycogen acts only as a primer of phosphorylase activity, it is possible that catalytic amounts of glycogen may be present, but only in quantities which the PAS technique may not be capable of demonstrating. Other factors, such as the activity of the muscle fibers at the time of quenching, may influence phosphorylase activity more than glycogen content (Mommaerts et al, 1975). Until the causes for the variations in PAS and phosphorylase staining are defined, we feel that these two techniques offer little practical benefit in fiber typing.…”

Section: Discussionmentioning

confidence: 98%

“…However, it is apparent that definite interspecies differences exist in normal muscles. Many reports have appeared that pertain only to the study of basic muscle biology, but an increasing number of studies are related to the application of histochemical techniques to the study of diseased muscle (Dubowitz and Brooke, 1973;Stern et al, 1975;Spencer and Zorab, 1976;Spencer and Eccles, 1976;Meijer et al, 1977). Data available on human fiber types far exceed those pertaining to nonhuman primates.…”

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confidence: 95%

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Comparative histochemical study of prosimian primate hindlimb muscles. I. Muscle fiber types

Sickles¹,

Pinkstaff²

1981

Am. J. Anat.

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The profiles of fiber types in hindlimb muscles from the tree shrew (Tupaia glis), lesser bushbaby (Galago senegalensis), and the slow loris (Nycticebus coucang) were determined using histochemical techniques. Fibers were classified as fast-twitch oxidative-glycolytic (FOG), fast-twitch glycolytic (FG), slow-twitch oxidative (SO), or fast-twitch oxidative (FO), according to reactions for alkaline-stable ATPase, acid-stable ATPase, alpha-glucan phosphorylase, reduced nicotinamide adenine dinucleotide diaphorase, succinate dehydrogenase, mitochondrial alpha-glycerophosphate dehydrogenase (MaGPDH), and beta-hydroxybutyric dehydrogenase, as well as glycogen staining by the periodic acid-Schiff technique. Prolonged dissection of numerous muscles was carried out on hindlimbs submersed in cold Tyrode's solution; such treatment had no qualitative effect on enzyme staining reactions, but it is not a suitable procedure if one wishes to stain for glycogen. Fast-twitch oxidative (FO) fibers are alkaline-stable ATPase-positive and possess low MalphaGPDH enzyme activity. These fibers have not been reported previously in any hindlimb muscles. No muscles of any species studies were homogeneous with respect to fiber type. Slow loris muscles lacked FG fibers. The majority of the muscles of the slow loris contained numerous SO fibers. The relationship between enzyme activities and locomotor pattern is discussed.

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Section: Discussionmentioning

confidence: 98%

mentioning

confidence: 95%

Comparative histochemical study of prosimian primate hindlimb muscles. I. Muscle fiber types

Sickles¹,

Pinkstaff²

1981

Am. J. Anat.

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“…The method is a modification of that published by Rosenblatt et al (1987), which is in tum a combination of two previously reported techniques (Meijer and Vloedman, 1980;Meijer, 1970). The histochemical bases of the staining reaction are those reported by Meijer (1970) and Meijer and Vossenberg (1977) and quoted by Rosenblatt et al (1987). Briefly, ATP present in the incubation medium is hydrolyzed by capillary endothelial ATPase, which is revealed by the deposition of lead sulfide.…”

Section: Discussionmentioning

confidence: 99%

A histochemical ATPase method for the demonstration of the muscle capillary network.

Fouces

Torrella²,

Palomeque³

et al. 1993

J Histochem Cytochem.

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A histochemical method for demonstration of the cap== in skeletal muscle of birds is proposed. The present method, which is a modification of a previously reported myosin ATPase technique used for simultaneous staining of capillaries and fiber types, provides an accurate count of capillaries associated with different fiber types in avian skeletal musdes. We have applied the original and the modified method to serial adjacent sections of certain skeletal musdes and our results show that after the application of the original technique: (a) in muscles having dark Type Ii fibers, these fibers produce a masking effect on their adjacent capillaries: (b) a consistent and significant undetcounting in cap-

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“…Type II fibres were further classified as Type II A if inhibition was complete with pH 4.5 pre-incubation, Type II B if pH 4.3 pre-incubation was required for complete inhibition and Type II C if inhibition was not complete unless pre-incubation pH was less than 4.0. These characteristics have been useful in classifying muscle fibres of limb skeletal muscles of humans (Meijer & Vossenberg, 1977;Brooke & Kaiser, 1970b;Askansas & Engel, 1975) and laboratory animals (Samaha et al, 1970;Guth & Samaha, 1972;Khan, 1977).…”

Section: Introductionmentioning

confidence: 99%

Lack of ?acid reversal? of myofibrillar adenosine triphosphatase in masticatory muscle fibres of rhesus monkeys

1980

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Myofibrillar adenosine triphosphatase (ATPase) activity was demonstrated in sections of masseter and temporalis muscles and of selected limb muscles of adult rhesus monkeys. Incubations were performed either with no pre-treatment or after prior incubation in alkaline media (pH 10.2-10.4) or acidic media (pH 3.8-4.6). Without pre-treatment, fibres having high or low ATPase activity were observed in limb and masticatory muscles. Following alkaline pre-incubation the difference between high and low ATPase of limb muscle fibres is accentuated, whereas pre-incubation in acidic media (pH 4.3) results in inhibition of high and potentiation of low ATPase activities ('acid reversal'). While pre-incubation of masticatory muscle sections at pH 10.2 accentuates differences in ATPase activity, pre-incubation at pH 10.4 abolishes ATPase activity. In contrast, masticatory muscle fibres showed no reversal of ATPase activity following acidic pre-incubation (pH 4.3). Pre-incubation at pH 3.8 abolished the ATPase activity of both limb and masticatory muscle fibres. The biochemical basis for the differences in ATPase histochemistry between masticatory and limb muscles is not known.

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The value of enzyme histochemical techniques in the classification of fibre types of human skeletal muscle

Cited by 27 publications

References 13 publications

Comparative histochemical study of prosimian primate hindlimb muscles. I. Muscle fiber types

Comparative histochemical study of prosimian primate hindlimb muscles. I. Muscle fiber types

A histochemical ATPase method for the demonstration of the muscle capillary network.

Lack of ?acid reversal? of myofibrillar adenosine triphosphatase in masticatory muscle fibres of rhesus monkeys

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