Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.4.1 (myosin ATPase)
 1,140 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A modified ATPase method for the simultaneous demonstration of capillaries and fiber types in skeletal muscle is presented. Muscle biopsies were obtained from mice, hamsters, rats, cats, and dogs, quick frozen, and sectioned at 8 microns in a cryostat. The frozen slides were fixed in a neutral formalin solution at 4 C for 5 min, and then incubated at 37 C for 1 hr in a medium containing ATP, Pb2+, and Ca2+ in a tris-maleate buffer (pH 7.2). Dilute (NH4)2S was used as a developer. To test the reliability of the proposed method, serial sections of each biopsy were stained separately for capillaries (amylase-PAS method) and for fiber types by a standard myosin ATPase (m-ATPase) method. Fiber type percent and capillary parameters were determined for each biopsy. No difference in results was observed for parameters determined using the modified ATPase method compared to the standard capillary and fiber type staining methods. This modified technique is therefore suitable for the simultaneous demonstration of capillaries and fiber types in skeletal muscle.
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PMID:A histochemical method for the simultaneous demonstration of capillaries and fiber type in skeletal muscle. 244 Jan 55

Skeletal muscle adaptations to training of differing intensities were examined in 10 thoroughbred horses that underwent six weeks of treadmill training followed by six weeks of detraining. The horses were randomly assigned to either a slow group exercised at 40 per cent maximum oxygen uptake (VO2max) or a fast group at 80 per cent VO2max. Resting muscle biopsies were taken before training, after six weeks of training and after six weeks of detraining, from m gluteus medius and m biceps femoris. Muscle was analysed histochemically for fibre type composition (myosin ATPase) and capillary supply (PAS amylase). Cross sectional area and lesser fibre diameter were measured by planimetry and image analysis. No alterations were found in the proportions of different muscle fibre types during training or detraining. Capillary density increased by 54 per cent in m biceps femoris of the fast group during training and decreased to the pretraining level following detraining. Few changes in fibre size occurred as a result of training and detraining. It was not possible to draw conclusions as to the effects of detraining because of the small number of training induced changes. The results suggest that for major adaptations in skeletal muscle, an increasing exercise intensity throughout training may be more significant than the degree of exercise load, when exercise intensity is submaximal.
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PMID:Effect of constant load training on skeletal muscle histochemistry of thoroughbred horses. 768 5

The purpose of this study was to compare muscle fibre type proportions and capillary density in untrained, college-aged blacks (n = 14) and whites (n = 14). Both groups were similar in terms of peak oxygen uptake (VO2peak), measured during cycle ergometry (blacks: 42.6 +/- 4, whites: 44.3 +/- 4 ml.kg-1 min-1, mean +/- SD). Muscle samples were obtained from the quadriceps femoris (vastus lateralis) by the needle biopsy technique. Fibre type was determined by myosin ATPase stain (pH = 4.54) and capillaries were identified by amylase-periodic acid Schiff (PAS) stain. The percentage of type I, IIa, and IIb fibres in the blacks was 39.5 +/- 11.5, 40.0 +/- 8.4, and 22.8 +/- 9.8, respectively. In whites the percentage of type I, IIa, and IIb fibres was 44.9 +/- 8.5, 36.6 +/- 6.9, and 18.3 +/- 9.6, respectively. No significant differences were noted between the two racial groups for type I, IIa, or IIb fibres. Capillary density was 277 +/- 39/mm2 in the blacks compared to 289 +/- 32/mm2 in the whites. Capillary density was positively correlated to percentage of type I fibres (r = 0.497) and negatively correlated to percentage of type IIa fibres (r = -0.389), in the overall study population. These data suggest that if racial differences in fibre type do exist, such differences are small compared to the variability in this measure.
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PMID:Skeletal muscle fibre type and capillary density in college-aged blacks and whites. 923 38

Amylase secretion is induced by the accumulation of cAMP in response to beta-adrenergic stimulation and by the augmentation of intracellular Ca2+ in response to muscarinic-cholinergic stimulation in rat parotid glands. The roles of cytoskeleton and motor proteins in the secretory process are not yet known. We examined the effects of cytoskeleton-modulating reagents on the amylase release induced by isoproterenol (IPR) and carbamylcholine (Cch) in rat parotid acinar cells. The amylase release induced by Cch was decreased by the microtubule-disrupting reagent colchicine (Colch) and the myosin ATPase inhibitor 2,3-butanediene monoxime (BDM), but the release induced by IPR was not. The actin filament-stabilizing reagent jasplakinolide (Jasp) and actin filament-disrupting reagent cytochalasin D (CytoD) decreased the amylase release induced by both the beta-adrenergic and the muscarinic-cholinergic stimulants. Pretreatment with CytoD affected the shape of the acinar cells, which showed an intermediate state between the fusion of the secretory granules with the apical membrane and the retrieval of the membranes only after stimulation with IPR. Myosin and Dynein/dynactin complex were detected in the secretory granule membrane fraction. We concluded from this study that the cytoskeleton played different roles in the beta-adrenergic and the muscarinic-cholinergic secretory processes.
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PMID:Presence of cytoskeleton proteins in parotid glands and their roles during secretion. 1548 39