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)

Spinal isolation (SI), i.e., the isolation of the lumbar spinal cord via a rostral and a caudal cord transection and bilateral dorsal rhizotomy, was used to determine the effects of chronic (6 months) inactivity on the size and metabolic properties of fibers in the cat soleus. Fibers were classified as dark or light, based on their staining reactions to myosin ATPase, alkaline preincubation, and immunohistochemically as expressing fast and/or slow myosin heavy chains (MHC). Succinate dehydrogenase (SDH) and alpha-glycerophosphate dehydrogenase (GPD) activities were assessed histochemically. Following SI, both the light and the dark ATPase fibers in the SI cats were significantly smaller than the light ATPase fibers in the controls. Normally 100% of the fibers were light ATPase and reacted exclusively with the slow antibody. After SI, approximately 45% of the fibers were dark ATPase fibers, many reacting with both fast and slow MHC antibodies. The total amount and concentration of GPD were higher in the light and dark ATPase fibers in SI compared with light ATPase fibers in controls. In contrast, although the total amount of SDH per fiber was decreased, reflecting the decrease in fiber size, the mean SDH concentration per fiber was unchanged following SI. These data indicate that there is a close coordination in the regulation of GPD activity and the type of myosin. SDH activity, on the other hand, appears to be resistant to decreased levels of activity and unloading, i.e., there seems to be a minimum level of oxidative potential in the soleus that is independent of activity level. Fiber sizes, however, are very sensitive to less-than-normal amounts of neuromuscular activity and/or loading.
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PMID:Enzyme and size profiles in chronically inactive cat soleus muscle fibers. 153 Oct 89

A novel type of myosin heavy chain (MHC), called 2X, has been recently identified in type 2 fibers of rat skeletal muscles using an immunochemical approach. In the present study, the same panel of anti-MHC monoclonal antibodies was used in immunohistochemistry combined with enzyme histochemistry to identify and compare type 2X fibers in hindlimb skeletal muscles of rat, mouse, and guinea pig. Immunohistochemistry shows that 2X MHC is localized in a large subset of type 2 fibers and is co-expressed with 2A or 2B MHC in a small number of fibers. Enzyme histochemistry shows that type 2X fibers display low myosin ATPase activity after pre-incubation at pH 4.3 and high activity after paraformaldehyde pre-incubation at pH 10.4. After pre-incubation at pH 4.6, myosin ATPase shows intermediate and high activity in rat and mouse 2X fibers, respectively, whereas it is low in guinea pig 2X fibers. Succinate dehydrogenase displays moderate to high activity in 2X fibers of all species. Taken together, these staining patterns allow this novel fiber population to be distinguished from the other type 2 fibers using only enzyme histochemistry. Nevertheless, the combined use of immuno- and enzyme histochemistry prevents incorrect fiber typing due to the interspecies variability of myosin ATPase activity among the correspondent fiber types, and completely modifies the presently used classification of mouse type 2 fibers.
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PMID:Identification of a novel type 2 fiber population in mammalian skeletal muscle by combined use of histochemical myosin ATPase and anti-myosin monoclonal antibodies. 213 54

The goal was to describe the metabolic profile of ganglionic and cortical arteries and arterioles in aging normotensive male rats. Five enzymes indicative of key metabolic pathways in the vessel walls were semiquantitatively evaluated using bright-field histochemical microscopy. Lactate dehydrogenase showed significant reactivity which increased with vessel diameter in cortical and ganglionic vessels in all age groups tested. Succinate dehydrogenase and cytochrome oxidase showed little reactivity in both cortical and ganglionic vessels, suggesting a reduced role for aerobic metabolic pathways. Myosin ATPase reactivity was high in cortical and ganglionic vessels. Only this enzyme showed an increased reactivity that was correlated with the age and diameter of the vessel. Glucose-6-phosphate dehydrogenase reactivity was more pronounced in cortical than ganglionic vessels, suggesting that the hexose-monophosphate-shunt may be more active in the cortical vessels. There were no regional differences in enzyme reactivity throughout the caudatoputamen. In conclusion, both the cortical and ganglionic vessels are metabolically active, with significant anaerobic glycolysis, and reduced, but observable capacity for aerobic metabolism. The decreased myosin ATPase reactivity and the low level of glucose-6-phosphate dehydrogenase reactivity in the ganglionic arterioles of senescent rats may contribute to the susceptibility of these vessels to cerebrovascular accidents.
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PMID:A histochemical study of cerebral cortical vessels and ganglionic vessels of the caudatoputamen in aging normotensive rats. 315 35

Coronary arteries and arterioles in the left ventricle from the primate Macaca fascicularis were histochemically examined to evaluate their metabolic profiles. Succinate dehydrogenase and cytochrome oxidase activities were assessed to evaluate aerobic metabolic capacity, while myosin ATPase activity was determined as an index of ATP utilization for contraction. Anaerobic capacity was evaluated from lactate dehydrogenase and glycogen reactivity. Glucose-6-phosphate dehydrogenase was examined to determine capacity of the hexose-monophosphate-shunt, while the amounts of deoxyribonucleicc and ribonuclei acids were assessed as possible indicators of protein synthesis. Succinate dehydrogenase and cytochrome oxidase demonstrated slight reactivity in both coronary arteries and arterioles indicating a low capacity for aerobic metabolism. Myosin ATPase showed strong activity in arteries and even stronger reactivity in arterioles, suggesting that arteriolar smooth muscle is more capable of utilizing ATP. Glucose-6-phosphate dehydrogenase activity was extremely low in both arteries and arterioles, while deoxyribonucleic and ribonucleic acids demonstrated only slight to moderate reactivity in both arteries and arterioles, indicating that under normal conditions the coronary vasculature appears quite stable with little cell proliferation.
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PMID:A histochemical evaluation of metabolism in the coronary vasculature of the primate. 617 63

A histochemical study of the metabolism of rat renal arteries and arterioles. Rat renal arteries and arterioles were examined histochemically to determine their metabolic profiles. Succinate, malate and NAD-isocitrate dehydrogenase, cytochrome oxidase and ubiquinone were assessed to determine aerobic metabolism. Glucose-6-phosphate dehydrogenase and DPN diaphorase were evaluated to determine hexose-monophosphate-shunt activity. Anaerobic metabolism was evaluated via lactate dehydrogenase, and the substrate, glycogen. Gomori's lipase, beta-hydroxybutyrate dehydrogenase and amounts of neutral fat and free fatty acids were assessed as indicators of lipid utilization. Myosin ATPase activity was evaluated as an index of ATP utilization for contraction. Deoxyribonucleic and ribonucleic acids were appraised as indicators of protein synthesis. In general, the oxidative enzymes and myosin ATPase demonstrate considerable activity in renal arteries and arterioles which suggests aerobic metabolism and ATP usage. Renal arteries and arterioles also appear capable of anaerobic metabolism as indicated by strong lactate dehydrogenase reactivity and by the presence of slight to moderate quantities of glycogen, while high levels of glucose-6-phosphate dehydrogenase and moderate amounts of deoxyribonucleic acid suggest a potential for beta-hydroxybutyrate dehydrogenase, minimal lipase activity, and the absence of fatty acids with substantial amounts of neutral fat, indicate limited lipid catabolism.
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PMID:A histochemical study of the metabolism of rat renal arteries and arterioles. 620 11

Myocardial preservation during open heart surgery in children was studied using biopsies of the right ventricle taken at the beginning and end of a bypass with a Tru-Cut biopsy needle. Three assessments were used: (1) semi-quantitative cytochemical grading of Baker's acid haematein reaction, and the distribution of succinate dehydrogenase and myosin ATPase; (2) microdensitometry of the succinate dehydrogenase activity; and (3) quantitative birefringence measurements to assess the response of the myocardial fibres to ATP and calcium. For each assessment, the values at the beginning and end of the bypass were compared. In a series of 42 children, two died in low cardiac output and three others required substantial inotropic support. No patient showed deterioration in the overall cytochemical assessment. Two patients showed deterioration in birefringence, one died and one had low cardiac output. The remaining three patients who had post-operative problems had low birefringence values at the beginning of bypass. Thirty-two patients were used for the microdensitometric assays, one died and three required substantial inotropic support. Succinate dehydrogenase activity decreased significantly during bypass in only two patients. One of these died and the other required substantial inotropic support.
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PMID:Cellular chemical indices of right ventricular protection in children. 621 86

Succinate dehydrogenase activity (SDH) was estimated kinetically in individual muscle fibres from the rabbit tibialis anterior, in cryostat sections using computer-linked microphotometry to record initial reaction velocities. These were correlated with fibre type based on myofibrillar actomyosin ATPase staining. Analysis of type IIA and IIB fibre populations in control muscles demonstrated wide variations in SDH activity between fibres of identical myosin ATPase type, with a considerable overlap in oxidative activities of the IIA and IIB populations. Muscles chronically stimulated via the peroneal nerve, using two different frequency patterns, showed increases in SDH activity which were primarily located in the type IIB fibres. This increase was observed both in muscles stimulated continuously at 10 Hz, and when similar numbers of stimuli were applied in brief trains at higher frequency. An earlier onset and more rapid rate of increase of SDH activity was seen with 10 Hz stimulation than with higher frequency, though the levels after 14 days of either pattern of stimulation were not significantly different.
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PMID:Response of succinate dehydrogenase activity in fibres of rabbit tibialis anterior muscle to chronic nerve stimulation. 622 3

1. Succinate dehydrogenase (SDH) activity was assessed in situ in single fibres of cross-sectioned extensor hallucis longus, extensor digitorum longus, and soleus muscles of rat by means of microphotometric recordings of initial maximum reaction rates. 2. Each fibre assessed for SDH activity was subjectively classified into myosin subgroups by its histochemical reaction for myofibrillar actomyosin ATPase (myosin ATPase) following preincubation at pH 4.6 according to Brooke & Kaiser (1970). 3. The majority of fibres classified into myosin types I and IIa were highly reactive for SDH, such that those myosin groups could be interchangeable with the metabolic subgroups of Peter, Barnard, Edgerton, Gillespie & Stempel (1972); myosin I = slow-twitch oxidative, myosin IIa = fast-twitch oxidative glycolytic. 4. The myosin type IIb fibres, however, demonstrated marked variability in activity levels of SDH. Over 40% of those fibres had high SDH activity, and thus could not be equated with the metabolic subgroup fast-twitch glycolytic. 5. The histochemical reaction for myosin ATPase in muscle fibres therefore cannot be used as a reliable means to predict the fibres' metabolic characteristics.
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PMID:Succinate dehydrogenase activity in fibres classified by myosin ATPase in three hind limb muscles of rat. 645 51

1. Contractile and fatigue-resistance characteristics, temperature sensitivity (10-37 degrees C) of contraction, and histochemical fibre types were determined for two of the extraocular muscles, the superior rectus and levator palpebrae superioris (levator), of the rabbit. 2. The levator displayed similar contractile characteristics (time to peak, half-relaxation time of twitch response, and twitch-tetanus force ratio) to mammalian fast-twitch limb muscle at room temperature (20 degrees C). However, normalized twitch and tetanic force levels were significantly less than those found in limb muscle. The superior rectus displayed the characteristics of even faster contraction than the levator at 20 degrees C, but generated lower maximum force levels than the levator. 3. The twitch response of the superior rectus showed a biphasic relaxation phase. This response was not due to non-twitch (tonic) fibres present in the superior rectus as it was unaffected by propranolol application during muscle stimulation. 4. The superior rectus and levator displayed significantly less fatigue in the tetanic force response than fast-twitch limb muscles did in response to a fatiguing electrical stimulation protocol. The levator was significantly more fatigue resistant than the superior rectus. 5. The force responses of both extraocular muscles displayed a similar dependence on temperature (10-37 degrees C) to limb skeletal muscles. 6. The superior rectus and levator exhibited a high proportion of fast-twitch muscle fibres (type II) as shown by myosin ATPase staining. Succinate dehydrogenase activity indicated that these muscles showed a high oxidative capacity, with a staining intensity typical of type I or type II A fibres of limb muscles. 7. The results emphasize the morphological and functional complexity of mammalian extraocular muscles. The combination of very fast contractile properties with high oxidative capacity make these muscles well suited to their role in eye/eyelid movement.
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PMID:Contractile properties and temperature sensitivity of the extraocular muscles, the levator and superior rectus, of the rabbit. 802 38